Sodium-n-butyrate induces secretion and substrate accumulation of p52 in Kirsten sarcoma virus-transformed rat kidney fibroblasts.
1. A group of five transformation-responsive secreted proteins, ranging in molecular mass from 31 to 70 kDa, were identified in cultured normal rat kidney (NRK) fibroblasts. 2. One such protein (p52) was found to be a major secreted and substrate-attached component of NRK cells. 3. Kirsten sarcoma virus-transformed NRK cells failed to accumulate p52 in either the secreted or substrate-associated protein compartments; this protein was inducible, however, in transformed cells by culture in 2 mM sodium-n-butyrate. 4. Kinetics of p52 induction in transformed NRK cells, relative to the time course of increased cell spreading, and its enrichment in the substrate-associated protein fraction suggest that p52 might function in cell-substrate attachment.
Ryan
M P
MP
Laboratory of Cell and Molecular Biology, Veterans Administration Medical Center, Albany, NY 12208.
Higgins
P J
PJ
D000818:Animals; D002087:Butyrates / Q000494:pharmacology*; D020148:Butyric Acid; D002461:Cell Line, Transformed; D002472:Cell Transformation, Viral; D003470:Culture Media; D005347:Fibroblasts / Q000187:drug effects; D007668:Kidney / Q000187:drug effects* / Q000378:metabolism / Q000382:microbiology; D007708:Kirsten murine sarcoma virus; D008562:Membrane Glycoproteins / Q000378:metabolism*; D009053:Sarcoma Viruses, Murine
D002087:Butyrates; D003470:Culture Media; D008562:Membrane Glycoproteins; C048022:substrate adhesion molecules; D020148:Butyric Acid