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  1. What is BPC 157?

    The effect of BPC157, with or without growth hormone (GH), on proliferating cell nuclear antigen (PCNA) gene expression (dRn) in rat tendon fibroblasts. Asterisks indicate significant effects. From Chang et al., Pentadecapeptide BPC 157 enhances the growth hormone receptor expression in tendon fibroblasts, Molecules (Basel, Switzerland). 2014;19(11):19066-19077.

    The effect of BPC157, with or without growth hormone (GH), on proliferating cell nuclear antigen (PCNA) gene expression (dRn) in rat tendon fibroblasts. Asterisks indicate significant effects. From Chang et al., Pentadecapeptide BPC 157 enhances the growth hormone receptor expression in tendon fibroblasts, Molecules (Basel, Switzerland). 2014;19(11):19066-19077.

      BPC157 is a 15-amino acid peptide compound linked to a number of medical and scientific applications1. It is associated with protective effects against stomach ulcers, as assessed by clinical models of this disorder (i.e. 96% ethanol-induced lesions)2. BPC157 is also associated with beneficial effects on blood pressure. The mechanisms of action of BPC157 are not completely understood, but may be indirectly linked to endothelial (cells in the linings of many organs and systems, including the gut) nitric oxide (NO) production. BPC157 has demonstrated an ability to generate NO comparable to that of similar doses of L-arginine in in vitro studies using samples of rat gastric mucosa. Studies using stomach ulcer models have found that the anti-ulcer effects of the NO precursor, L-arginine, are reversed by N(G)-nitro-L-arginine methylester (L-NAME), which inhibits NO production2. However, L-NAME may only attenuate (slow down or partially reverse) the effects of BPC157 on lesions2. Another study investigated the effect of BPC157, alone or combined with L-arginine (200 mg/kg), L-NAME (5 mg/kg), or both, on experimental colonic fistulas (severe gastrointestinal lesions that may connect the colon to other surfaces, including skin) in rats. 10 μg/kg doses of this peptide, intraperitoneally or in drinking water, resulted in rapid healing of these lesions, leading to their closure3. Groups receiving BPC157 with L-NAME, L-arginine or both also exhibited fistula healing, despite the detrimental effect of L-NAME administration (without BPC157 or L-arginine) on the same3. BPC157 may also have a role in the healing of other tissue types, including muscle, ligaments and tendons4. Intraperitoneal or cutaneous (i.e. as a cream) administrations of this peptide improved markers of healing (e.g. reduced edema or hematoma and enzymes such as alanine aminotransferase or creatine kinase) in a rat model of muscle injury5. BPC157 may also affect the central nervous system. A single 10 μg/kg intraperitoneal dose of this peptide resulted in reductions in the synthesis of serotonin in several rat brain regions, including the thalamus, hypothalamus and hippocampus compared to control rats1. However, this also resulted in increased synthesis of the same neurotransmitter in other brain regions, such as the substantia nigra1. A seven-day regimen of subcutaneous BPC157 (10 μg/kg per dose) resulted in significant increases of serotonin synthesis in the substantia nigra, nucleus accumbens and lateral caudate. This indicates that BPC157 may have the potential to affect memory, emotional responses and/or processing and homeostatis1. BPC157 may also be applied to the treatment of alcohol withdrawal and toxicity. A study used a mouse model of toxicity (i.e. acute intoxication with ethanol) to investigate this possibility. A 10 μg/kg intraperitoneal dose of BPC157 quickly reversed the symptoms of acute intoxication (e.g. anesthesia, hypothermia, absence of self-righting reflex and increased risk of mortality)6. This study also assessed the effect of BPC157 on withdrawal after access to 20% ethanol for thirteen days. The same dose of the peptide also resulted in reduced symptoms of this (e.g. seizure). Rats and mice treated with BPC157 showed decreases in clinical biomarkers following experimentally-induced congestive heart failure7. BPC157 (at the doses as above) has also demonstrated beneficial effects on increased portal pressure and liver damage in animal models of chronic alcohol intake7. 1. Tohyama Y, Sikiric P, Diksic M. Effects of pentadecapeptide BPC157 on regional serotonin synthesis in the rat brain: alpha-methyl-L-tryptophan autoradiographic measurements. Life sciences. 2004;76(3):345-357. 2. Sikiric P, Seiwerth S, Grabarevic Z, et al. The influence of a novel pentadecapeptide, BPC 157, on N(G)-nitro-L-arginine methylester and L-arginine effects on stomach mucosa integrity and blood pressure. European journal of pharmacology. 1997;332(1):23-33. 3. Klicek R, Sever M, Radic B, et al. Pentadecapeptide BPC 157, in clinical trials as a therapy for inflammatory bowel disease (PL14736), is effective in the healing of colocutaneous fistulas in rats: role of the nitric oxide-system. Journal of pharmacological sciences. 2008;108(1):7-17. 4. Chang CH, Tsai WC, Hsu YH, Pang JH. Pentadecapeptide BPC 157 enhances the growth hormone receptor expression in tendon fibroblasts. Molecules (Basel, Switzerland). 2014;19(11):19066-19077. 5. Novinscak T, Brcic L, Staresinic M, et al. Gastric pentadecapeptide BPC 157 as an effective therapy for muscle crush injury in the rat. Surgery today. 2008;38(8):716-725. 6. Boban-Blagaic A, Blagaic V, Romic Z, et al. The influence of gastric pentadecapeptide BPC 157 on acute and chronic ethanol administration in mice. The effect of N(G)-nitro-L-arginine methyl ester and L-arginine. Medical science monitor : international medical journal of experimental and clinical research. 2006;12(1):Br36-45. 7. Lovric-Bencic M, Sikiric P, Hanzevacki JS, et al. Doxorubicine-congestive heart failure-increased big endothelin-1 plasma concentration: reversal by amlodipine, losartan, and gastric pentadecapeptide BPC157 in rat and mouse. Journal of pharmacological sciences. 2004;95(1):19-26.
  2. What is Toremifene Citrate?

    toremifene

    "Toremifene" by Fvasconcellos. Licensed under Public Domain via Wikimedia Commons - https://commons.wikimedia.org/wiki/File:Toremifene.svg#mediaviewer/File:Toremifene.svg

      Toremifene Citrate and its Applications in Animal Studies This is a selective estrogen receptor modulator currently associated with the treatment of metastatic breast cancer and disorders associated with menopause in humans. Toremifene is associated with a reduced potential for genotoxicity in comparison to other similar drugs such as tamoxifen1. It is in common use as a standard against which new estrogen receptor modulators (or other agonists/antagonists) are compared in animal trials2. Toremifene was also recently used to validate a transgenic rat assay designed to detect the carcinogenicity of chemicals under evaluation3. Female transgenic rats were given 40mg/kg toremifene by gavage every day for three weeks, to simulate a repeated-dose regimen3. This was found not to result in mutations in comparison to the same dose of tamoxifen at the same frequency3. The transgenic adenocarcinoma of the mouse prostate model is a model of cancer in this organ. Toremifene was found to protect against cancer development in studies using this model4. This drug is also incorporated into animal studies of combined cancer therapies. Toremifene alone and in combination with atamestane (an irreversible estrogen synthesis blocker) were associated with significant decreases in the low-density lipoprotein and serum cholesterol of ovarectomized rats (a model of estrogen-blocking therapy in breast cancer)5. It was also associated with significant positive effects on bones in these rats5. This combination (1mg toremifene plus 1mg atamestane per day) was found to be equal in effect to toremifene alone in reducing uterine tumor growth in mice injected with Ac1 cancer cells6. A combination of 30 or 120mg/day toremifene and local hyperthermia in nude mice injected with MCF-7 breast cancer line cells found that the anti-tumor effects were significantly greater in the groups receiving these treatments than groups receiving either dose of toremifene alone7. Toremifene as an Anti-Infective Toremifene has been shown to prevent the formation of biofilms associated with micro-organisms including several subspecies of Staphylococcus (including S. aureus) and Candida, as well as Pseudomonas aeruginosa8. A rat model of subcutaneous catheter placement demonstrated the efficacy of toremifene against the biofilm formation of S. aureus and C. albicans8. This may indicate the potential role of toremifene in preventing infection in porous implants incorporating metal and other materials9. The pre-incubation of subinhibitory concentrations of toremifene also significantly enhanced the inhibition of C. albicans and C. glabrata biofilms by the classic antifungals caspofungin and amphotericin B10. This also enhanced the inhibition of mixed S. epidermis and C. albicans biofilms by caspofungin10. Toremifene may also be a potent anti-Ebola virus drug11. An in vivo mouse model found that this drug inhibited Ebola virus infection, even in the absence of estrogen receptors11. Toremifene inhibited viral entry after internalization. These findings indicate that the drug may act through alternative pathways to prevent infection11. References: 1. Kim SY, Suzuki N, Laxmi YR, Umemoto A, Matsuda T, Shibutani S. Antiestrogens and the formation of DNA damage in rats: a comparison. Chemical research in toxicology. 2006;19(6):852-858. 2. Kangas L, Harkonen P, Vaananen K, Keskitalo J, Eigeliene N. Effects of ospemifene on breast tissue morphology and proliferation: a comparative study versus other selective estrogen receptor modulators in ovariectomized rats. Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme. 2014;46(5):328-332. 3. Kawamura Y, Hayashi H, Kurata Y, Hiratsuka K, Masumura K, Nohmi T. Evaluation of the genotoxicity of tamoxifen in the liver and kidney of F344 gpt delta transgenic rat in 3-week and 13-week repeated dose studies. Toxicology. 2013;312:56-62. 4. Nguewa PA, Calvo A. Use of transgenic mice as models for prostate cancer chemoprevention. Current molecular medicine. 2010;10(8):705-718. 5. Goss PE, Qi S, Hu H. Comparing the effects of atamestane, toremifene and tamoxifen alone and in combination, on bone, serum lipids and uterus in ovariectomized rats. The Journal of steroid biochemistry and molecular biology. 2009;113(3-5):233-240. 6. Sabnis GJ, Macedo L, Goloubeva O, Schayowitz A, Zhu Y, Brodie A. Toremifene-atamestane; alone or in combination: predictions from the preclinical intratumoral aromatase model. The Journal of steroid biochemistry and molecular biology. 2008;108(1-2):1-7. 7. Kanaya Y, Doihara H, Shiroma K, Ogasawara Y, Date H. Effect of combined therapy with the antiestrogen agent toremifene and local hyperthermia on breast cancer cells implanted in nude mice. Surgery today. 2008;38(10):911-920. 8. De Cremer K, Delattin N, De Brucker K, et al. Oral administration of the broad-spectrum antibiofilm compound toremifene inhibits Candida albicans and Staphylococcus aureus biofilm formation in vivo. Antimicrobial agents and chemotherapy. 2014;58(12):7606-7610. 9. Braem A, De Cremer K, Delattin N, et al. Novel anti-infective implant substrates: Controlled release of antibiofilm compounds from mesoporous silica-containing macroporous titanium. Colloids and surfaces. B, Biointerfaces. 2015. 10. Delattin N, De Brucker K, Vandamme K, et al. Repurposing as a means to increase the activity of amphotericin B and caspofungin against Candida albicans biofilms. The Journal of antimicrobial chemotherapy. 2014;69(4):1035-1044. 11. Johansen LM, Brannan JM, Delos SE, et al. FDA-approved selective estrogen receptor modulators inhibit Ebola virus infection. Science translational medicine. 2013;5(190):190ra179.
  3. What is MGF Peptide?

    mgfpeptidegraph

    Growth rates of cultured rabbit mesenchymal stem cells in response to the administration of MGF peptide at the concentrations outlined in the legend. From Tong et al., Mechano-growth factor accelerates the proliferation and osteogenic differentiation of rabbit mesenchymal stem cells through the PI3K/AKT pathway. BMC Biochemistry. 2015;16(1):1.

      What is MGF Peptide?  Mechano-growth factor peptide (MGF peptide) is a 24-amino acid carboxy-terminal fragment of the insulin-like growth factor (IGF-1) protein1. It is a product of IGF-1 mRNA splicing2. The expression of MGF peptide is related to tissue damage and mechanical stimuli2. For example, the release of MGF peptide has been observed to increase in response to skeletal muscle injury3. This is thought to induce hypertrophy in damaged muscle tissue4. Some proteins found in muscle, such as titin and myomesin, are associated with the expression of this peptide in cultured murine myoblasts and myotubes2. The mechanical stimuli associated with the normal growth of tissues may also result in the expression of MGF peptide4. Other forms of stimulus that may be associated with the synthesis of MGF peptide are increased acidity and heat5. It has been linked to improvements in facets of muscular regeneration. These include delayed myoblast fusion and improved satellite cell proliferation1. MGF peptide has also been linked to protective roles against the death of nerve and heart muscle cells2. Therefore, this peptide may have a role in tissue growth and repair6. Studies involving MGF Peptide An in vitro trial using mouse myoblasts showed that MGF peptide at concentrations of up to 500ng/ml did not increase their proliferation or their differentiation into myotubes1. To confirm this, the researchers then incubated murine skeletal muscle stem cells with the peptide. No effects on the differentiation or numbers of these cells were observed1. On the other hand, MGF peptide has been associated with growth and differentiation in other cell and animal types. The exposure of rabbit mesenchymal stem cells to this peptide resulted in their growth and differentiation into osteoblasts7. This was mediated by the phosphorylation of mTOR and Akt7. (Conversely, the study as above found no increases in the phosphorylation of Akt in murine heart muscle cells, as claimed in previous reports1.) Another study using rat osteoblasts found that there was a significant increase in proliferation, and a slight decrease in differentiation, after three days of MGF peptide administration6. However, after chronic (three weeks) administration, improved differentiation of these cells was observed6. Mouse models of myocardial infarction may be characterized by a significant decline in diastolic and systolic hemodynamics as well as pathological hypertrophy within approximately ten weeks of an infarction8. The administration of MGF peptide within 12 hours of these events in mice had a positive effect on these hemodynamics, but not on hypertrophy8. MGF peptide administration for eight weeks following infarctions resulted in significant improvement in systolic function8. Another study assessed the expression of MGF peptide in the growth plates of piglets4. Porcine Mgf mRNA was found to be increased in the hypertrophic parts of growth plates4. However, the administration of exogenous MGF peptide to cultures of growth plate cells or chondrocytes did not result in proliferation4. A study of the effects of MGF peptide on rat mesenchymal stem cells found that this may enhance the stiffness and traction force associated with the migration of these cells9. The phosphorylation of ERK was associated with MGF peptide-induced migration9. Repetitive stretching in muscles of Wistar rats was associated with the significantly increased expression of Mgf mRNA, but only in the presence of the anabolic steroid metenolone10. References: 1.  Fornaro M, Hinken AC, Needle S, et al. Mechano-growth factor peptide, the COOH terminus of unprocessed insulin-like growth factor 1, has no apparent effect on myoblasts or primary muscle stem cells. American journal of physiology. Endocrinology and metabolism. 2014;306(2):E150-156. 2.  Kravchenko IV, Furalyov VA, Popov VO. Stimulation of mechano-growth factor expression by myofibrillar proteins in murine myoblasts and myotubes. Molecular and cellular biochemistry. 2012;363(1-2):347-355. 3.  Vassilakos G, Philippou A, Tsakiroglou P, Koutsilieris M. Biological activity of the e domain of the IGF-1Ec as addressed by synthetic peptides. Hormones (Athens, Greece). 2014;13(2):182-196. 4.  Schlegel W, Raimann A, Halbauer D, et al. Insulin-like growth factor I (IGF-1) Ec/Mechano Growth factor--a splice variant of IGF-1 within the growth plate. PloS one. 2013;8(10):e76133. 5.  Kravchenko IV, Furalyov VA, Popov VO. Hyperthermia and acidification stimulate mechano-growth factor synthesis in murine myoblasts and myotubes. Biochemical and biophysical research communications. 2008;375(2):271-274. 6.  Xin J, Wang Y, Wang Z, Lin F. Functional and transcriptomic analysis of the regulation of osteoblasts by mechano-growth factor E peptide. Biotechnology and applied biochemistry. 2014;61(2):193-201. 7.  Tong Y, Feng W, Wu Y, Lv H, Jia Y, Jiang D. Mechano-growth factor accelerates the proliferation and osteogenic differentiation of rabbit mesenchymal stem cells through the PI3K/AKT pathway. BMC biochemistry. 2015;16(1):1. 8.  Shioura K, Pena J, Goldspink P. Administration of a Synthetic Peptide Derived from the E-domain Region of Mechano-Growth Factor Delays Decompensation Following Myocardial Infarction. International journal of cardiovascular research. 2014;3(3):1000169. 9.  Wu J, Wu K, Lin F, et al. Mechano-growth factor induces migration of rat mesenchymal stem cells by altering its mechanical properties and activating ERK pathway. Biochemical and biophysical research communications. 2013;441(1):202-207. 10.  Ikeda S, Kamikawa Y, Ohwatashi A, Harada K, Yoshida A. The effect of anabolic steroid administration on passive stretching-induced expression of mechano-growth factor in skeletal muscle. TheScientificWorldJournal. 2013;2013:313605.
  4. Melanotan II?

    melanotanii

    - Chemical structure of Melanotan II by TheCook, made available under the terms of the Creative Commons Attribution-Share Alike 3.0 Unported license.

      What is Melanotan II? This is an analog of the alpha-melanocyte-stimulating hormone, and an agonist of the melanocortin receptor types 3 and 4 (MCR3 and MCR4)1,2. The melanocortin system in the central nervous system is associated with the regulation of social, emotional and food intake behaviors. It is also associated with a role in mediating the beneficial effects of leptin in rats with uncontrolled diabetes3. The MCR4 receptor is also associated with the regulation of bodyweight4. Defective MCR4 is associated with disorders of satiety and with early-onset obesity5. Studies of Melanotan II and its Functions Social Functions Melanotan II may be able to influence factors such as partner preference in monogamous animals. This molecule was found to enhance this behavior in prarie voles, but not in more polygamous meadow voles1. This was found to be associated with the activation of oxytocin-releasing neurons in the hypothalamus and the enhancement of oxytocin release by melanotan II1. Subcutaneous administration of 10 mg/kg melanotan II to males and female neonates of the same species for the first seven days of life resulted in reduced play-fighting in males compared to matched controls6. It also enhanced partner preference in the treated females in adulthood6. Metabolic and Cardiovascular Functions The administration of melanotan II in a rat model of diabetes did not appear to reduce hyperglycemia3. Intraperitoneal melanotan II was associated with rapid decreases in body temperature and energy expenditure4. This did not affect feeding, however4. The effect of melanotan II on body temperature was found to be independent of MCR4 receptor availability, and may be linked to activity at vasopressin V1a receptors instead4. The infusion of melanotan II into the medial preoptic nuclei of rat brains was associated with thermogenesis in brown adipose tissue2. The molecule was also found to be associated with the expression of proteins involved in lipolysis and lipogenesis2. These actions appear to be regulated by the dorsomedial hypothalamus2. Knockdown studies in rats indicates that AMP-activated protein kinase (AMPK) may be involved in the mediation of melanotan II activity7. The microinjection of melanotan II into the paraventricular nucleus of rat brains resulted in an increase in mean arterial pressure8. MCR3 and 4 antagonists reversed this effect8. Melanotan II also increased cAMP in the paraventricular nucleus8. Another study compared mice with MCR4 receptor deficiency to identical animals with selectively restored MCR4 in proopiomelanocortin neurons. (These are associated with the effects of leptin on energy homeostasis9. The knockout of PTP1B, the negative regulator of leptin in these cells, was associated with increased sensitivity to the effects of melanotan II on feeding, bodyweight and energy expenditure in KO mice compared to controls9.) This resulted in observations of increased bodyweight and decreased energy expenditure in the MCR4-deficient mice only, although feeding, blood pressure and heart rate were similar between the two groups10. This may further indicate the role of this receptor - and thus of melanotan II - in energy homeostasis and bodyweight control. References:  1. Modi ME, Inoue K, Barrett CE, et al. Melanocortin receptor agonists facilitate oxytocin-dependent partner preference formation in the prairie vole. Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology. 2015. 2. Monge-Roffarello B, Labbe SM, Lenglos C, et al. The medial preoptic nucleus as a site of the thermogenic and metabolic actions of melanotan II in male rats. American journal of physiology. Regulatory, integrative and comparative physiology. 2014;307(2):R158-166. 3. Meek TH, Matsen ME, Damian V, Cubelo A, Chua SC, Jr., Morton GJ. Role of melanocortin signaling in neuroendocrine and metabolic actions of leptin in male rats with uncontrolled diabetes. Endocrinology. 2014;155(11):4157-4167. 4. Xu Y, Kim ER, Fan S, et al. Profound and rapid reduction in body temperature induced by the melanocortin receptor agonists. Biochemical and biophysical research communications. 2014;451(2):184-189. 5. Fani L, Bak S, Delhanty P, van Rossum EF, van den Akker EL. The melanocortin-4 receptor as target for obesity treatment: a systematic review of emerging pharmacological therapeutic options. International journal of obesity (2005). 2014;38(2):163-169. 6. Barrett CE, Modi ME, Zhang BC, Walum H, Inoue K, Young LJ. Neonatal melanocortin receptor agonist treatment reduces play fighting and promotes adult attachment in prairie voles in a sex-dependent manner. Neuropharmacology. 2014;85:357-366. 7. Tanida M, Yamamoto N, Shibamoto T, Rahmouni K. Involvement of hypothalamic AMP-activated protein kinase in leptin-induced sympathetic nerve activation. PloS one. 2013;8(2):e56660. 8. Li P, Cui BP, Zhang LL, Sun HJ, Liu TY, Zhu GQ. Melanocortin 3/4 receptors in paraventricular nucleus modulate sympathetic outflow and blood pressure. Experimental physiology. 2013;98(2):435-443. 9. De Jonghe BC, Hayes MR, Zimmer DJ, Kanoski SE, Grill HJ, Bence KK. Food intake reductions and increases in energetic responses by hindbrain leptin and melanotan II are enhanced in mice with POMC-specific PTP1B deficiency. American journal of physiology. Endocrinology and metabolism. 2012;303(5):E644-651. 10. do Carmo JM, da Silva AA, Rushing JS, Pace B, Hall JE. Differential control of metabolic and cardiovascular functions by melanocortin-4 receptors in proopiomelanocortin neurons. American journal of physiology. Regulatory, integrative and comparative physiology. 2013;305(4):R359-368.
  5. What is Clenbuterol?

    clenbuterolgraph

    The change in muscle tension as a result of a 5-minute fatigue protocol, showing the differences in maximal force and 50% initial force (black dotted lines), as well as the resistance to fatigue (Tlim) between rat extensor digitorum longus (EDL) muscle treated with clenbuterol and that of controls. From Sirvent et al., Effects of chronic administration of clenbuterol on contractile properties and calcium homeostasis in rat extensor digitorum longus muscle. PloS one. 2014;9(6):e100281.

      What is Clenbuterol?  Clenbuterol is an adrenergic beta-2 receptor agonist associated with increases in skeletal muscle growth1. It is associated with the increase of fast-twitch glycolytic muscle fibers as opposed to slow-twitch oxidative fibers2. This results in rapid changes (or 'remodeling') in the structure of skeletal muscle. Recent animal studies have shown that chronic subcutaneous clenbuterol administration may not increase relevant characteristics of muscular activity such as specific maximal tetanic force and contractile efficiency3. Another study demonstrated that chronic administration did not change relative force in the muscles of male Wistar rats2. However, it was associated with an increase in absolute force2. Clenbuterol increases calpain (a serine protease) activity2. Chronic clenbuterol intake was also found to be associated with an imbalance in calcium (Ca2+) signaling and concentration in muscle fibers2. A study using rat soleus muscle fibers showed inhibitory effects on intracellular Ca2+ and action potential4. The latter was not reversed in the presence of a beta-2 antagonist, indicating clenbuterol may also have activity at alternative receptors4. Therefore, clenbuterol may change the kinetics of muscle contraction via indirect pathways based on the disruption of cellular Ca2+ homeostasis3. Clenbuterol may be associated with the increased risk of muscle fatigue2. The switch to fast-twitch fiber activity results in varying levels of hypertrophy (rapid growth) in different muscle types5. This may be due to the responses of different subtypes of calpain to this drug5. Some researchers argue that clenbuterol administration results in myotoxicity at high doses (approximately 1mg/kg per day)6. Clenbuterol is also associated with damage to cardiac muscle4. Other Functions and Applications of Clenbuterol  Adrenergic beta-receptors are also present in the central nervous system. Their specific roles in the brain may be elicited through the experimental application of clenbuterol. Intraperitoneal clenbuterol (at three different doses) reduced visuospatial learning discrepancies in a rat model of impaired cortical function (elicited by significantly reduced beta-receptor expression in the neocortex)7. The injection of clenbuterol into a brain region (the ventral bed nucleus of the stria terminalis) implicated in the stress-related use of cocaine reinstated this behavior in rats8. This indicates that beta-receptors may regulate the activation of the ventral tegmental area (another brain region) associated with cocaine-seeking8. The infusion of clenbuterol into the basolateral complex of the amygdala enhanced 'emotional' and 'aversive' memory in rats9. Some studies have indicated that beta-2 receptors are associated with the breakdown of glycogen in astrocytes, which supplies energy to neurons in the absence of dietary glucose10. A study using a mouse model of this found that clenbuterol administration did not influence this, but that beta-2 activation was associated with the protection of axons10. Clenbuterol may also have a therapeutic role in developmental disorders. The administration of clenbuterol resulted in the reduction of respiratory and motor co-ordination deficits in a mouse model of Rett syndrome (knockout of the Mecp2 gene)11. It was also associated with improvements in the survival and social recognition abilities of young male mice with this mutation11. Clenbuterol also improved cognition and anxiety in older female heterozygous mice11.  References: 1. Emery PW, Rothwell NJ, Stock MJ, Winter PD. Chronic effects of beta 2-adrenergic agonists on body composition and protein synthesis in the rat. Bioscience reports. 1984;4(1):83-91. 2. Sirvent P, Douillard A, Galbes O, et al. Effects of chronic administration of clenbuterol on contractile properties and calcium homeostasis in rat extensor digitorum longus muscle. PloS one. 2014;9(6):e100281. 3. Py G, Ramonatxo C, Sirvent P, et al. Chronic clenbuterol treatment compromises force production without directly altering skeletal muscle contractile machinery. The Journal of physiology. 2015. 4. Head SI, Ha TN. Acute inhibitory effects of clenbuterol on force, Ca(2)(+) transients and action potentials in rat soleus may not involve the beta(2)-adrenoceptor pathway. Clinical and experimental pharmacology & physiology. 2011;38(9):638-646. 5. Douillard A, Galbes O, Rossano B, et al. Time course in calpain activity and autolysis in slow and fast skeletal muscle during clenbuterol treatment. Canadian journal of physiology and pharmacology. 2011;89(2):117-125. 6. Burniston JG, McLean L, Beynon RJ, Goldspink DF. Anabolic effects of a non-myotoxic dose of the beta2-adrenergic receptor agonist clenbuterol on rat plantaris muscle. Muscle & nerve. 2007;35(2):217-223. 7. Saez-Briones P, Soto-Moyano R, Burgos H, et al. beta-Adrenoceptor stimulation restores frontal cortex plasticity and improves visuospatial performance in hidden-prenatally-malnourished young-adult rats. Neurobiology of learning and memory. 2014;119c:1-9. 8. Vranjkovic O, Gasser PJ, Gerndt CH, Baker DA, Mantsch JR. Stress-induced cocaine seeking requires a beta-2 adrenergic receptor-regulated pathway from the ventral bed nucleus of the stria terminalis that regulates CRF actions in the ventral tegmental area. The Journal of neuroscience : the official journal of the Society for Neuroscience. 2014;34(37):12504-12514. 9. McReynolds JR, Anderson KM, Donowho KM, McIntyre CK. Noradrenergic actions in the basolateral complex of the amygdala modulate Arc expression in hippocampal synapses and consolidation of aversive and non-aversive memory. Neurobiology of learning and memory. 2014;115:49-57. 10. Laureys G, Valentino M, Demol F, et al. beta(2)-adrenergic receptors protect axons during energetic stress but do not influence basal glio-axonal lactate shuttling in mouse white matter. Neuroscience. 2014;277:367-374. 11. Mellios N, Woodson J, Garcia RI, et al. beta2-Adrenergic receptor agonist ameliorates phenotypes and corrects microRNA-mediated IGF1 deficits in a mouse model of Rett syndrome. Proceedings of the National Academy of Sciences of the United States of America. 2014;111(27):9947-9952.
  6. GHRP-2: An overview of the current research

    GHRP-2

    Serum murine GH responses to 10 µg GHRP-2 (or saline (SAL)) in lit/lit (i.e. GHRH-deficient) mice in comparison to heterozygous or WT animals. From Peroni et al., Growth hormone response to growth hormone-releasing peptide-2 in growth hormone-deficient little mice. Clinics (Sao Paulo). 2012;67(3):265-272.

     

    What is GHRP-2?

    GHRP-2 is a small peptide (made of six amino acids) associated with the release of growth hormone (GH)1. This protein is associated with important roles in the regulation of sex hormones and metabolic control2. Decreases in this hormone are also associated with reductions in muscle mass, bone deterioration and possible cognitive deficits3. It is also linked to the increased risk of death from cardiovascular disease3. Growth hormone, as the name suggests, also plays a role in the growth and development of humans and other animals. GH deficiency has been shown to result in growth retardation.

     How does GHRP-2 act to increase GH?

    The release of GH is stimulated by the GH secretagogue (GHS) receptor, which is normally activated by ghrelin (also known as the GHS). GHRP-2 is a synthetic peptide that has also been shown to activate the GHS receptor (GHS-R1a)4. GHRP-2 (and ghrelin) also stimulates the release of prolactin, corticotropin and cortisol4. This has a positive effect on energy expenditure, appetite, heart muscle tone and sleep regulation. There is also a GH-releasing hormone (GHRH) present in humans and other animals, which stimulates the release of GH through its own receptor (GHRH-R). GHRP-2 complements this by potentiating the cAMP activation associated with GHRH-R binding, and may also promote the population of this receptor4. GHRP-2 has been found to significantly increase GH in genetically GHRH-deficient mice4. GHRP-2 is also associated with increases in IGF15.

    Other functions and uses of GHRP-2

    GHRP-2 may be administered orally. However, this is linked to reduced efficacy, as oral formulations have been found to result in poor absorption and thus reduced effects on (for example) GH secretion6. Intravenous solutions of GHRP-2 are regarded as the standard route, although subcutaneous and intraperitoneal administration is also used in some trials5-7. GHRP-2 may also have a potential role in analgesia (pain relief). This is due to recent observations that GHS-R1a activation by ghrelin in mice resulted in analgesia8. A recent study found that GHRP-2 also produced these effects. This was shown to be reversed by naloxone administration, indicating that GHS-R1a may be able to affect opioid receptors in the central nervous system8.

    GHRP-2 has also been found to bind to C36, which is a receptor for the pro-athergenic oxidized low-density lipoprotein5. It was found to reduce oxidative stress, but not plaque size, in a mouse model of atherosclerosis5. Subcutaneous GHRP-2 resulted in improvements of a rat model of acute lung injury9. This was attributed to reductions in TNFalpha, IL-6 and NFkappaB in the lung tissue of GHRP-2-treated rats9. This is further evidence of the anti-inflammatory properties of this peptide.

    Another study found that TNFalpha was also reduced by intraperitoneal GHRP-2 in a rat model of liver damage7. To confirm that this was as a result of exogenous GHRP-2, these researchers administered endotoxins and GHRP-2 to cultures of hepatocytes and nonparenchymal cells with hepatocytes. The peptide caused a reduction in TNFalpha mRNA in the latter, but not the former7. This indicates that GHRP-2 acts directly on the liver through nonparenchymal cells to reduce inflammation.

     References:

    1. Bowers CY. GH releasing peptides--structure and kinetics. J Pediatr Endocrinol. 1993;6(1):21-31.

    2. Veldhuis JD, Roemmich JN, Richmond EJ, Bowers CY. Somatotropic and gonadotropic axes linkages in infancy, childhood, and the puberty-adult transition. Endocr Rev. 2006;27(2):101-140.

    3. Norman C, Rollene NL, Erickson D, Miles JM, Bowers CY, Veldhuis JD. Estradiol regulates GH-releasing peptide's interactions with GH-releasing hormone and somatostatin in postmenopausal women. Eur J Endocrinol. 2014;170(1):121-129.

    4. Peroni CN, Hayashida CY, Nascimento N, et al. Growth hormone response to growth hormone-releasing peptide-2 in growth hormone-deficient little mice. Clinics (Sao Paulo). 2012;67(3):265-272.

    5. Titterington JS, Sukhanov S, Higashi Y, Vaughn C, Bowers C, Delafontaine P. Growth hormone-releasing peptide-2 suppresses vascular oxidative stress in ApoE-/- mice but does not reduce atherosclerosis. Endocrinology. 2009;150(12):5478-5487.

    6. Tanaka T, Hasegawa Y, Yokoya S, Nishi Y. Increased Secretion of Endogenous GH after Treatment with an Intranasal GH-releasing Peptide-2 Spray Does Not Promote Growth in Short Children with GH Deficiency. Clin Pediatr Endocrinol. 2014;23(4):107-114.

    7. Granado M, Martin AI, Lopez-Menduina M, Lopez-Calderon A, Villanua MA. GH-releasing peptide-2 administration prevents liver inflammatory response in endotoxemia. American journal of physiology. Endocrinology and metabolism. 2008;294(1):E131-141.

    8. Zeng P, Li S, Zheng Y-h, et al. Ghrelin receptor agonist, GHRP-2, produces antinociceptive effects at the supraspinal level via the opioid receptor in mice. Peptides. 2014;55:103-109.

    9. Li G, Li J, Zhou Q, Song X, Liang H, Huang L. Growth hormone releasing peptide-2, a ghrelin agonist, attenuates lipopolysaccharide-induced acute lung injury in rats. The Tohoku journal of experimental medicine. 2010;222(1):7-13. 

  7. How do Peptides Work?

    How do Peptides Work? There are a large variety of peptides, which are used in scientific studies for a range of purposes.   Studies have been conducted on animal test subjects to determine which peptides work best for specific projects. Peptides are intended for laboratory research only.  Not for human consumption. What Are Peptides? In layman’s terms, peptides are a compound of two or more amino acids through the binding of the carboxyl group of one and the amino group of the other. The peptide bond is created once the water molecule is eliminated. Peptides can be looked upon as small proteins. For instance, anything that has 49 amino acids or less are considered peptides – however, this isn’t a golden rule for determining what is and isn’t a peptide. A dipeptide is a peptide that consists of two amino acids that are bonded by a single peptide bond. Tripeptides are peptides that have three amino acids that have two peptide bonds that bound them together. Polypeptides are simply one elongated un-branched line of amino acids that are bound together by peptide bonds, but isn’t complex enough to be considered a protein. Proteins, by the way, consist of polypeptides. The Functions of Peptides in the Body In order for the body to work properly, amino acids are needed to produce peptides. The body stops the production of peptides as it ages or due to stress, poor diet and physical changes. These scenarios can cause a down-regulated production of peptides. For instance, as the body ages, the growth factor, known as IGF-1, is reduced naturally. There are a variety of functions that peptides have in the body. Some peptides act similar to neurotransmitters and others act like hormones. When used in test subjects, peptides are shown to influence physical exercise and diet. In order to increase muscle growth, a certain amount of amino acids are needed. This will produce HGH, human growth hormones. Peptides have been used in studies involving bodybuilding and athletic test subjects, to see if it can counteract down-regulations in growth factors. In the studies that administer peptides to animal test subjects, results show that the peptide is easily digested by the body, since it is small enough to be broken down, unlike with larger protein molecules. It is also believed that peptides are more beneficial than amino acids that are un-bonded and unstable. Types of Peptides Creatine and glutamine peptides are widely used in research studies. In the research, it shows that the body absorbs them quicker and has few adverse effects. Peptides can come in powder, pill or injection form. Studies show that peptides that are in the injectable form help to produce growth hormones, enhance lean body mass and reduce the percentage of body fat in test subjects; it is also shown to speed up the recovery process after working out. Some of the peptides within this category include IGF-1, GHRP-6 and Ipamorelin. The peptides that are commonly used in anti-aging studies include SNAP-8 and Pal-GHK. As studies continue for peptides, more research details will be released in regards to their effectiveness for muscle building, weight loss, athletic performance enhancement and anti-aging. Disclaimer: Peptides are still undergoing extensive research and is not intended for consumer use. When purchasing peptides, it’s important that they only be used for experimental purposes. Strict laboratory guidelines should be followed when conducting tests using peptides. It is also recommended that safety equipment be worn by researchers. If exposure to a peptide occurs, it’s important to wash it away as quickly as possible.  
  8. What is ACE-031?

    ACE-031 is categorized within the protein family. It is consistently used in laboratory research to determine its ability to improve muscle mass. This protein is also being used for research in regards to neuromuscular disease treatment. The hypothesis of the studies is to see whether ACE-031 can be used to preserve physical function and boost strength of test subjects. Studies are still ongoing, so more is being learned on a regular basis about what this peptide can do. Proteins like ACE-031 are not approved for human consumption. What Exactly is ACE-031? This is a protein that’s being investigated to determine if it can be used for therapeutic purposes for building muscle and enhancing the strength of test subjects. It does this by allowing molecules to bind to cell surface receptors – this is also where it signals through. These cell surface receptors are known as Activin Receptr Type IIB, also known as ActRIIB. ACE-031 is a recombinant fusion protein that is produced when a portion of the ActRIIB receptor and a part of the standard antibody are joined together. This then creates a decoy version of ActRIIB that circulates and eliminates proteins like GDF-8 (also known as myostatin) and other molecules that limit the muscle’s strength or growth. How the ActRIIB Sends Signals and Promotes Muscle Growth The proteins in the TGF-B superfamily are used to regulate muscle growth. These act as the on and off switch for the production of muscles. In order to stop muscle growth, several molecules, such as GDF-8, intermingle with the ActRIIB receptor, which stops the production of muscle. When these off switches aren’t present, the muscle increases in mass radically. Studies Using ACE-031 for Building Muscles When ACE-031 was administered to test subjects, it showed that it helps to promote muscle growth and inhibit signaling from ActRIIB receptors. ACE-031 then binds together with other proteins that use the ActRIIB receptors to signal a limitation to muscle growth. Once bonded with these proteins, ACE-O31 stops communication with the ActRIIB, which then allows muscles to increase in size. Since ACE-031 stops certain proteins from sending signals through the ActRIIB, its effect on lean muscle exceeds those of just myostatin alone. When used on test subjects, ACE-031 shows growth of lean muscle and increased strength over test subjects that haven’t been treated with the protein. This has been used on healthy test subjects and those with diseases related to muscle wasting and weakness. For research involving skeletal muscle building, a single dose of ACE-031 was administered to test subjects. In two weeks, over two pounds of muscle was developed in those test subjects. It was also noted that the ACE-031 decreased leptin and increased adiponectin, which altered the biomarkers of fat metabolism and the formation of bone. It also changed resorption due to the decreased CTX and increased BSAP. The side effects of ACE-031 doses of different levels were mild or transient. No serious adverse effects were seen. Some of the adverse effects that were witnessed in test subjects included bleeding from the nose, signs of a headache and reactions at the injection site. The half-life of ACE-031 is 12 days, according to research. Disclaimer: ACE-031 is not intended for use in humans. The studies that were performed using this protein were for the purpose of research and experimentation only. It’s not recommended for purchase for any other reason than for testing. It is advised that any research conducted using ACE-031 should be done in an experimental setting that complies with strict lab guidelines. It is important that safety equipment be worn while experimenting with ACE-031. If one of the researchers is exposed to the protein, the area should be cleansed thoroughly to avoid adverse reactions.
  9. What is Snap 8 Peptide?

    SNAP 8 peptide’s scientific name is Acetyle Glutamyl Heptapeptide-1. It is being tested for use for anti-wrinkle solutions. Studies show that SNAP 8 has properties that enable it to reduce the depth of wrinkles that are caused by everyday muscle contractions. In animal test subjects, it has shown significant results around the eyes and forehead. This product is considered to be a milder, more cost-effective and safer alternative to Botulinum Toxin. SNAP 8 works similarly to Botulinum Toxin by targeting the same wrinkle formations, but in a unique way. Test Results of SNAP 8 Peptide VIVO testing was performed to determine how effective small peptides are with providing stability for the SNARE complex. This allowed the researchers to follow the thermal stability and formation of the reconstituted SNARE protein complex. This basically evaluates the effectiveness of the peptides that are patterned like SNAP-25 N and its ability to amass with synaptobrein and syntaxin that is being formed with the SNARE complex. The final result was that the short peptides that came from the N-terminal end of SNP-25 were able to compete with the natural protein and stop it from forming SNARE complex by changing the stability. Another test was done with test subjects. The cream used consisted of 10 percent SNAP 8. Researchers obtained silicon imprints from around the eyes of 17 test subjects. These silicon imprints were taken before the test began. The test subjects applied the cream twice daily, and then another sample was taken 28 days later. The imprints were analyzed using control laser scanning microscopy to see the difference between the skin surface of the sample taken before and after treatment. In order to see a three dimensional view of the samples, skin topography images were created. Within these images, it was observed that the depth of the wrinkles had decreased significantly after receiving treatment for 28 days. The max reduction that was seen with the 10 percent SNAP 8 solution was 63.18 percent. How SNAP 8 Peptides Work SNAP 8 is a copy of the N-terminal end of SNAP-25. This competes with SNAP-25 to position itself within the SNARE complex, which then modulates its creation. When the SNARE complex is destabilized slightly, it is impossible for the vesicle to release neurotransmitters in an efficient manner. Because of this, muscle contractions are reduced, so that wrinkles and lines are prevented. It will also help reduce existing fine lines and wrinkles by inhibiting the formation of SNARE complex and the release of catecholamine. With regular use in test subjects, it also prevented the development of wrinkles and lines. Clinical studies show that SNAP 8 helped to reduce wrinkles surrounding the eyes by up to 63.13 percent. Testing for vitro and vivo efficiency showed that SNAP 8 has 30 percent more activity than parent peptides like Argireline. Disclaimer: SNAP 8 peptide is a solution that is still currently being tested in the scientific community. It is not intended for use on humans or animals. It is recommended to purchase SNAP 8 for the sole purpose of experimentation within a laboratory setting. It should not be purchased and used for any other reason. This substance has not been approved for use by people. It is recommended that experiments conducted with SNAP 8 be performed under experimental circumstances that are under strict lab guidelines. Safety equipment should be used at all times throughout experimentation with this product. In the event that someone is exposed to the substance, thorough cleansing of the area immediately after is recommended to avoid potential harm.
  10. What does Thymosin Beta 4 Do?

    Thymosin Beta4 is a peptide that was first found within the thymus gland. Since its discovery, other types of thymosin have been found in different tissues throughout test subjects. Thymosin Beta 4 is typically found in both types of muscles – skeletal (the muscles that are required to move) and smooth muscles (such as the heart). When damage occurs in a tissue, Thymosin Beta 4 is upregulated. Then when traumas take place, Thymosin Beta 4 is released in order to help the subject heal from the trauma. This peptide also helps to prevent adhesions from forming, which means there will be less scar tissue and potentially more flexibility. It has potent anti-inflammatory characteristics. Thymosin Beta 4 is a potent peptide that comes from a family of 16 related molecules that are localized in circulating cells and tissues within the body. These molecules also have a high conservation of sequence. TB 500 conjoins with actin and prevents actin polymerization. It is noted as being the actin-sequestering molecule within eukaryotic cells. It also boosts extracellular matrix-degrading enzyme production. The Benefits of Thymosin Beta 4 Thymosin Beta 4 is a protein that is made up of 43 amino acids. The TMSB4X gene found in the test subject's body encodes the peptide. There have been a variety of clinical trials that have been performed using this peptide. In the research, it’s been found that the Thymosin Beta 4 may be used after a heart attack takes place in order to reactivate the cells in the cardiac progenitor, so that repair can be done to the damaged tissue in the heart. The molecule of this peptide is very big, so it isn’t able to completely fit within a receptor. Each area of the molecule has different functions. For instance, TB 500 is responsible for promoting majority of the useful effects, such as the healing, muscle cells, new blood and repair. In some scenarios, TB 500 could be used rather than the whole Thymosin Beta 4 protein. TB 500’s main ability is to regulate Actin, which is a cell-building protein. There are thousands of proteins found inside of cells, but actin makes up to 10 percent of the total amount of proteins, giving it a major role in the cell’s genetic makeup. Some of the benefits associated with TB 500 include:
    • Increased muscle growth
    • Increased endurance
    • Calmed muscle spasms
    • Muscle tone improvement
    • Improved substance exchanges between cells
    • Promotes tissue repair
    • Allows connective tissue to stretch
    • Maintains flexibility
    • Reduces joint tissue inflammation
    • Stops adhesions and fibrous bands from forming on ligaments, muscles and tendons
    Research behind Thymosin Beta 4 The studies that have been conducted have determined that this peptide is potent and that it occurs totally naturally. It does help to repair wounds using its anti-inflammatory characteristics. Unlike with growth factors and other repair factors, this peptide increases the migration of endothelial and keratinocyte. It also does not conjoin to extracellular matrixes and is noted as having a molecular weight that is very low, which enables it to travel far distances within tissues. Disclaimer: Thymosin Beta 4 is a peptide that should only be purchased for use in experimentation and research. It should not be purchased for human use or any other purpose than for research. It is advised that once purchased, the peptide is used within experimental circumstances that are under strict lab regulations. It is recommended that researchers use protective gear in order to prevent contact with the substance. However, if exposure is made with the peptide, it is very important to cleanse the area immediately to prevent harm.

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