The role of a cell surface inhibitor in early signal transduction associated with the regulation of cell division and differentiation.
Serum stimulation of quiescent human fibroblast cultures resulted in a hyperphosphorylation of the nuclear retinoblastoma gene susceptibility product (RB).  However, serum stimulation in the presence of 9 x 10(-8) M of a purified bovine sialoglycopeptide (SGP) cell surface inhibitor abrogated the hyperphosphorylation of the RB protein and the subsequent progression of cells through the mitotic cycle.  The experimental results suggest that the SGP mediated its cell cycle arrest at a site in the cell cycle that was at the time of RB phosphorylation or somewhat upstream of the modification of this regulatory protein of cell division.  Both cells serum-deprived and serum stimulated in the presence of the SGP displayed only a hypophosphorylated RB protein, consistent with the SGP-mediated cell cycle arrest point being near the G1/S interface.
Johnson
T C
TC
Division of Biology, Kansas State University, Manhattan 66506-4903, USA.
Enebo
D J
DJ
Moos
P J
PJ
Fattaey
H K
HK
D002453:Cell Cycle / Q000502:physiology; D002454:Cell Differentiation; D002455:Cell Division; D002478:Cells, Cultured; D005347:Fibroblasts / Q000166:cytology / Q000187:drug effects / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism / Q000494:pharmacology / Q000502:physiology*; D010766:Phosphorylation; D016160:Retinoblastoma Protein / Q000378:metabolism*; D012795:Sialoglycoproteins / Q000494:pharmacology / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*
D008565:Membrane Proteins; D016160:Retinoblastoma Protein; D012795:Sialoglycoproteins