Inhibition of the degradation of the precursor and of the mature beta 1 integrin subunit by different protein synthesis inhibitors and by ATP depletion.
A stabilization of both the precursor and the mature beta 1 integrin subunit was observed in metabolically labeled human skin fibroblasts and Molt-4 T lymphocytes upon addition of protein synthesis inhibitors or by ATP depletion. Differential effects of protein synthesis inhibitors are reported since the slow degradation of the mature beta 1 subunit was sensitive to cycloheximide but not to puromycin. We also show that the half-life of the mature subunit was not dependent on intracellular lysosomal degradation or on ubiquitination suggesting that VLA turn-over occurs at the cell surface and might involve proteins or proteases with short half-life.
Vekeman
S
S
Center for Human Genetics, University of Leuven, Belgium.
Jaspers
M
M
Cassiman
J J
JJ
D000255:Adenosine Triphosphate / Q000378:metabolism*; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts / Q000187:drug effects; D006207:Half-Life; D006801:Humans; D009584:Nitrogen / Q000494:pharmacology; D011233:Precipitin Tests; D011498:Protein Precursors / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology*; D016029:Receptors, Very Late Antigen / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012969:Sodium Fluoride / Q000494:pharmacology; D013601:T-Lymphocytes / Q000187:drug effects
D011498:Protein Precursors; D011500:Protein Synthesis Inhibitors; D016029:Receptors, Very Late Antigen; C003320:sodium nitride; D000255:Adenosine Triphosphate; D012969:Sodium Fluoride; D009584:Nitrogen