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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.

   

PNC-27, an anticancer peptide, containing an HDM-2 binding domain corresponding to p53 residues 12-26 and a transmembrane penetrating domain, has been found to kill cancer cells but not normal cells by inducing membrane lysis. The 3D structure of the p53 residue of PNC-27 directly overlaps the structure of the same residue that binds HDM-2, suggesting that this peptide may target HDM-2 in the cell membrane. The researchers found significant levels of HDM-2 in the cell membranes of a variety of cancer cells but not in some untransformed cell lines. In colocalization experiments, PNC-27 bound to cell membrane-bound HDM-2. The researchers used a membrane localization signal to transfect a plasmid expressing full-length HDM-2 into PNC-27-insensitive untransformed MCF-10-2A cells and found that these cells expressed full-length HDM-2 on their cell surface. cells versus PNC-27. We concluded that PNC-27 targets HDM-2 in cancer cell membranes, allowing it to selectively induce membrane lysis in these cells.

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