Heat shock induction of a 65 kDa ATP-binding proteinase in rat C6 glioma cells.
The 45, 55, 65 and 100 kDa ATP-binding proteinases (ATP-BPases) of the heat-shocked (44 degrees C for 30 min, recovery for 12 h) rat C6 glioma cells were purified by DEAE-ionexchange and ATP-affinity chromatography. Their molecular masses, isoelectric points (pI), pH-optima and other properties were analyzed by native proteinase gels. It was shown that the 65 kDa ATP-BPase is specifically induced by heat shock and not detectable in control cells. Its N-terminal 1-9 amino acid sequence was determined by Edman degradation, but no homologies to other proteins in the protein data bases were found. 30 and 31 kDa proteinases can be cleaved from the 45, 55 and 65 kDa proteinases to which they are linked. A possible relationship of the heat-induced 65 kDa ATP-BPase with the ATP-dependent proteinases (ATP-DPases) in prokaryotes and eukaryotes is discussed.
Xu
C S
CS
Department of Biology, Henan Normal University, Xinxiang. Peanut@public2.zz.ha.cn
Zhang
W M
WM
Techel
D
D
Meyer
M
M
Li
Y Z
YZ
Rensing
L
L
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002448:Cell Adhesion; D048429:Cell Size; D004790:Enzyme Induction / Q000187:drug effects; D005910:Glioma / Q000201:enzymology* / Q000473:pathology; D018869:Heat-Shock Response / Q000502:physiology*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D012697:Serine Endopeptidases / Q000096:biosynthesis* / Q000737:chemistry* / Q000302:isolation & purification; D014407:Tumor Cells, Cultured
D000596:Amino Acids; D000255:Adenosine Triphosphate; C121397:ATP-binding proteinase, 65 kDa; D012697:Serine Endopeptidases