Placenta-specific protein 9 |
placodal cells |
lactalbumin-alpha(1-5) |
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Placentin was identified originally as an open reading frame (139 amino acids) from a cDNA clone isolated from a subtracted library of first trimester human placenta (Koman et al, 1996). Placentin is composed of two peptide chains of apparent molecular masses of 4 and 13 kDa and is a member of the insulin family of proteins. The protein is identical with EPIL [early placenta insulin-like peptide]. The approved gene symbol is INSL4 [insulin-like-4].
Placentin stimulates tyrosine phosphorylation (see also: PTK) and DNA synthesis. These effects are not mediated by the insulin receptor. In primary culture of cytotrophoblasts
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