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Effects of glypican‐1 on turkey skeletal muscle cell proliferation, differentiation and fibroblast growth factor 2 responsiveness
Author(s) -
Velleman Sandra G.,
Liu Caini,
Coy Cynthia S.,
McFarland Douglas C.
Publication year - 2006
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/j.1440-169x.2006.00860.x
Subject(s) - fibroblast growth factor , microbiology and biotechnology , cell growth , glypican 3 , transfection , basic fibroblast growth factor , growth factor , perlecan , cell , intracellular , proteoglycan , biology , chemistry , cell culture , extracellular matrix , receptor , biochemistry , immunology , genetics , immunohistochemistry
The heparan sulfate proteoglycan, glypican‐1, is a low affinity receptor for fibroblast growth factor 2 (FGF2). Fibroblast growth factor 2 is a potent stimulator of skeletal muscle cell proliferation and an inhibitor of differentiation. Heparan sulfate proteoglycans like glypican‐1 are required for FGF2 to transduce an intracellular signal. Understanding the role of glypican‐1 in the regulation of FGF2‐mediated signaling is important in furthering the understanding of the biological processes involved in muscle development and growth. In the current study, a turkey glypican‐1 expression vector construct was transfected into turkey myogenic satellite cells resulting in the overexpression of glypican‐1. The proliferation, differentiation, and responsiveness to FGF2 were measured in control and transfected cell cultures. The overexpression of glypican‐1 in turkey myogenic satellite cells increased both satellite cell proliferation and FGF2 responsiveness, but decreased the rate of differentiation. The current data support glypican‐1 modulation of both proliferation and differentiation through an FGF2‐mediated pathway.