人类肌肉生长类固醇激素肽肌肉生长抑制素GDF 8 GDF-8

产品描述：

肌肉生长抑制素（也称为生长分化因子8，简称GDF-8）是肌细胞，肌细胞产生和释放肌肉细胞的肌肉细胞的自分泌功能，以抑制肌肉细胞生长和分化的肌肉细胞。在人类中，它由MSTN基因编码。肌生长抑制素是分泌的生长分化因子，其是TGFβ蛋白家族的成员。
动物缺乏肌生成抑制素或用阻断肌生成抑制素活性的物质治疗具有显着更多的肌肉质量。此外，在肌肉生长抑制素基因的两个拷贝中具有突变的个体具有显着更多的肌肉质量并且比正常强。阻断氯化筒箭毒碱的活性可能在治疗肌肉消耗性疾病如肌肉营养不良中具有治疗应用。

发现和测序

编码氯化筒箭毒碱的基因是由遗传学家Se-Jin Lee和Alexandra McPherron于1997年发现的，他们产生缺失该基因的突变小鼠品系。这些肌肉生长抑制素敲除小鼠具有大约是正常小鼠两倍的肌肉。这些小鼠随后被命名为“强大的小鼠”。
已经在牛中由Ravi Kambadur，whippets和人发现了肌肉生长抑制素的天然存在的缺陷;在每种情况下，结果是肌肉质量的显着增加。 Texel羊中的肌生成抑制素基因的3'UTR中的突变产生了微RNA miR-1和miR-206的靶位点。这可能导致这种品种的羊的肌肉表型。

结构和作用机制
人肌肉生长抑制素由两个相同的亚基组成，每个亚基由109（NCBI数据库声称人肌肉生长抑制素是375个残基长）氨基酸残基组成。其总分子量为25.0kDa。蛋白质无活性，直到蛋白酶切割分子的NH 2 - 末端或“前结构域”部分，导致活性COOH-末端二聚体。肌生长抑制素与激活素II型受体结合，导致协同受体Alk-3或Alk-4的募集。该共同受体然后在肌肉中启动细胞信号级联，其包括SMAD家族中的转录因子的激活--SMAD2和SMAD3。 {{|}}这些因素然后诱导肌肉生长抑制素特异性基因调节。当应用于成肌细胞时，肌生成抑制素抑制它们分化成成熟肌纤维。
肌抑制素还抑制Akt，Akt是足以引起肌肉肥大的激酶，部分通过蛋白质合成的激活。然而，Akt不负责由肌肉抑制素抑制介导的所有观察到的肌营养不良影响。因此肌生成抑制素以两种方式起作用：通过抑制肌肉分化和通过抑制Akt诱导的蛋白质合成。



临床意义

突变
已经开发了用于检测肌肉生长抑制素变体中的突变的技术。减少功能性肌肉生长抑制素产生的突变导致肌肉组织的过度生长。肌肉生长抑制素相关的肌肉肥大有不完全的常染色体显性遗传模式。在每个细胞（纯合子）中的MSTN基因的两个拷贝中具有突变的人具有显着增加的肌肉质量和强度。在每个细胞（杂合体）中具有一个拷贝的MSTN基因突变的人具有增加的肌肉体积，但程度较轻。
在2004年，一个德国男孩被诊断​​出在两个副本的肌肉生长抑制素生产基因的突变，使他相当强于他的同行。他的母亲在该基因的一个拷贝中具有突变。 2005年出生的美国男孩被诊断​​为临床上类似的病症，但原因有些不同：他的身体产生正常水平的功能性肌肉生长抑制素;但是，因为他比他的年龄大多数人更强壮和更肌肉，据信他的肌肉生长抑制素受体的缺陷防止他的肌肉细胞正常响应肌肉生长抑制素。他出现在电视节目，世界上最强的蹒跚学步。
治疗潜力（编辑）
对肌肉生长抑制素和肌肉生长抑制素基因的进一步研究可能导致肌营养不良的治疗。该想法是引入阻断肌肉生长抑制素的物质。肌肉生长抑制素特异性单克隆抗体增加小鼠和猴子的肌肉质量。

用可溶性激活素IIB型受体（通常附着于细胞并与肌肉生长抑制素结合的分子）的正常小鼠的两周治疗导致肌肉质量显着增加（高达60％）。（33）认为结合的肌生长抑制素与可溶性激活素受体的结合防止其与细胞结合的受体相互作用。
目前还不清楚是否用肌肉抑制素抑制剂长期治疗肌营养不良是有益的，因为肌肉干细胞的消耗可能使疾病恶化。截至2012年，没有用于人的肌肉生长抑制素抑制药物在市场上。经遗传工程化以中和肌肉生长抑制素的抗体stamulumab（其正由制药公司Wyeth。开发）不再处于开发中。一些运动员，渴望得到他们的手上这样的药物，转向互联网，假的'myostatin阻止剂被卖。

肌肉抑制素水平通过肌酸补充有效降低。

基因掺杂

参见基因掺杂
抑制肌肉生长抑制素导致肌肉增生和肥大。肌抑制素抑制剂可以改善运动性能，因此存在这些抑制剂可能在运动领域中被滥用的担心。然而，在小鼠研究表明肌抑制素抑制不直接增加个别肌肉纤维的强度。

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Human Muscle Growth Steroid Hormone Peptide Myostatin GDF 8 GDF-8

Products Description:

Myostatin (also known as growth differentiation factor 8, abbreviated GDF-8) is a myokine, a protein produced and released by myocytes that acts on muscle cells' autocrine function to inhibit myogenesis: muscle cell growth and differentiation. In humans it is encoded by the MSTN gene. Myostatin is a secreted growth differentiation factor that is a member of the TGF beta protein family.
Animals either lacking myostatin or treated with substances that block the activity of myostatin have significantly more muscle mass. Furthermore, individuals who have mutations in both copies of the myostatin gene have significantly more muscle mass and are stronger than normal. Blocking the activity of myostatin may have therapeutic application in treating muscle wasting diseases such as muscular dystrophy.

Discovery and sequencing

The gene encoding myostatin was discovered in 1997 by geneticists Se-Jin Lee and Alexandra McPherron who produced a strain of mutant mice that lack the gene. These myostatin 'knockout' mice have approximately twice as much muscle as normal mice. These mice were subsequently named 'mighty mice'.
Naturally occurring deficiencies of myostatin have been identified in cattle by Ravi Kambadur, whippets, and humans; in each case the result is a dramatic increase in muscle mass. A mutation in the 3' UTR of the myostatin gene in Texel sheep creates target sites for the microRNAs miR-1 and miR-206. This is likely to cause the muscular phenotype of this breed of sheep.

Structure and mechanism of action
Human myostatin consists of two identical subunits, each consisting of 109 (NCBI database claims human myostatin is 375 residues long) amino acid residues. Its total molecular weight is 25.0 kDa. The protein is inactive until a protease cleaves the NH2-terminal, or 'pro-domain' portion of the molecule, resulting in the active COOH-terminal dimer. Myostatin binds to the activin type II receptor, resulting in a recruitment of either coreceptor Alk-3 or Alk-4. This coreceptor then initiates a cell signaling cascade in the muscle, which includes the activation of transcription factors in the SMAD family - SMAD2 and SMAD3. {{|}}These factors then induce myostatin-specific gene regulation. When applied to myoblasts, myostatin inhibits their differentiation into mature muscle fibers.
Myostatin also inhibits Akt, a kinase that is sufficient to cause muscle hypertrophy, in part through the activation of protein synthesis. However, Akt is not responsible for all of the observed muscle hyperthrophic effects which are mediated by myostatin inhibition Thus myostatin acts in two ways: by inhibiting muscle differentiation, and by inhibiting Akt-induced protein synthesis.



Clinical significance

Mutations
A technique for detecting mutations in myostatin variants has been developed. Mutations that reduce the production of functional myostatin lead to an overgrowth of muscle tissue. Myostatin-related muscle hypertrophy has an incomplete autosomal dominance pattern of inheritance. People with a mutation in both copies of the MSTN gene in each cell (homozygotes) have significantly increased muscle mass and strength. People with a mutation in one copy of the MSTN gene in each cell (heterozygotes) have increased muscle bulk, but to a lesser degree.
In 2004, a German boy was diagnosed with a mutation in both copies of the myostatin-producing gene, making him considerably stronger than his peers. His mother has a mutation in one copy of the gene. An American boy born in 2005 was diagnosed with a clinically similar condition but with a somewhat different cause: his body produces a normal level of functional myostatin; but, because he is stronger and more muscular than most others his age, it is believed that a defect in his myostatin receptors prevents his muscle cells from responding normally to myostatin. He appeared on the television show, World's Strongest Toddler.
Therapeutic potential(edit)
Further research into myostatin and the myostatin gene may lead to therapies for muscular dystrophy. The idea is to introduce substances that block myostatin. A monoclonal antibody specific to myostatin increases muscle mass in mice and monkeys.

A two-week treatment of normal mice with soluble activin type IIB receptor, a molecule that is normally attached to cells and binds to myostatin, leads to a significantly increased muscle mass (up to 60%).(33) It is thought that binding of myostatin to the soluble activin receptor prevents it from interacting with the cell-bound receptors.
It remains unclear as to whether long-term treatment of muscular dystrophy with myostatin inhibitors is beneficial, as the depletion of muscle stem cells could worsen the disease later on. As of 2012, no myostatin-inhibiting drugs for humans are on the market. An antibody genetically engineered to neutralize myostatin, stamulumab, which was under development by pharmaceutical company Wyeth., is no longer under development. Some athletes, eager to get their hands on such drugs, turn to the internet where fake 'myostatin blockers' are being sold.

Myostatin levels are effectively decreased by creatine supplementation.

Gene doping

See Gene doping
Inhibition of myostatin leads to muscle hyperplasia and hypertrophy. Myostatin inhibitors can improve athletic performance and therefore there is a concern these inhibitors might be abused in the field of sports. However, studies in mice suggest that myostatin inhibition does not directly increase the strength of individual muscle fibers.

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Polypeptide: