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- Title
Disintegration of Lysosomes Mediated by GTPγS-Treated Cytosol Possible Involvement of Phospholipases1.
- Authors
Sai, Yoshimichi; Matsuda, Tomoko; Arai, Kunizo; Ohkuma, Shoji
- Abstract
We showed previously that cytosol treated with guanosine 5'-O-(3-thiotriphosphate) (GTPγS) disintegrated lysosomes in vitro [Sai, Y. et al. (1994) Biochem. Biophys. Res. Commun. 198, 869-877] in time-, temperature-, and dose-dependent manners. This also requires ATP, however, the latter can be substituted with deoxy-ATP, ADP, or ATPγS, suggesting no requirement of ATP hydrolysis. The lysis was inhibited by several chemical modifiers, including N-ethylmaleimide, 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole, and 4, 4'-diisothiocyanatostilbene-2, 2'-disulfonic acid, and by various phospholipase inhibitors (trifluoperazine, p-bromophenacyl bromide, nordihydroguaiaretic acid, W-7, primaquine, compound 48/80, neomycin, and gentamicin), but not by ONO-RS-082, an inhibitor of phospholipase A2. The reaction was also inhibited by phospholipids (phosphatidylinositol, phosphatidylserine, phosphatidic acid, and phosphatidylcholine) and diacylglycerol. Among the phospholipase A2 hydrolysis products of phospholipids, unsaturated fatty acids (oleate, linoleate, and arachidonate) and lysophospholipid (lysophosphatidylcholine) by themselves broke lysosomes down directly, whereas saturated fatty acids (palmitate and stearate) had little effect. We found that GTPγS-stimulated cytosolic phospholipase A2 activity was highly sensitive to ONO-RS-082. These results suggest the participation of phospholipase(s), though not cytosolic phospholipase A2, in the GTPγS-dependent lysis of lysosomes.
- Subjects
LYSOSOMES; PHOSPHOLIPASE A2; ANTIBACTERIAL agents; GUANOSINE triphosphate; SOLVOLYSIS
- Publication
Journal of Biochemistry, 1998, Vol 123, Issue 4, p630
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/oxfordjournals.jbchem.a021984