Biosynthesis of EGF receptor, transferrin receptor and colligin by cultured human keratinocytes and the effect of retinoic acid.
The biosynthesis of EGF and transferrin receptor by human keratinocytes in culture has been followed using specific monoclonal antibodies. In addition, keratinocytes are shown to synthesise a Mr 47 000 protein that binds to gelatin-Sepharose. Peptide mapping confirms the identity of this protein with colligin, a newly described cell surface-associated glycoprotein that also binds to native collagens (Kurkinen et al., J biol chem 259 (1984) 5915) [9]. Vitamin A and its analogues have profound effects on the differentiation, morphology and motility of human keratinocytes in culture. We show here that retinoic acid (RA) has no effect on the growth rate of the cells or the synthesis of EGF receptor and colligin, but stimulates the synthesis of transferrin receptor.
Taylor
A
A
Hogan
B L
BL
Watt
F M
FM
D000911:Antibodies, Monoclonal; D002352:Carrier Proteins / Q000096:biosynthesis*; D002455:Cell Division / Q000187:drug effects; D002478:Cells, Cultured; D066246:ErbB Receptors; D006023:Glycoproteins; D006801:Humans; D011956:Receptors, Cell Surface / Q000096:biosynthesis*; D011990:Receptors, Transferrin; D012867:Skin / Q000378:metabolism*; D014212:Tretinoin / Q000494:pharmacology*
D000911:Antibodies, Monoclonal; D002352:Carrier Proteins; D006023:Glycoproteins; D011956:Receptors, Cell Surface; D011990:Receptors, Transferrin; C046289:colligin; D014212:Tretinoin; D066246:ErbB Receptors