Abstract:
:The regulation of neutral cytosolic cholesterol ester hydrolase was studied in isolated rat liver cells. Addition of glucagon to cell suspensions caused a decrease in the enzyme activity which was significant at 1 nM concentration. The cyclic nucleotide analogue bibutyryl cyclic AMP (10 and 100 microM) also inhibited the esterase activity. In the absence of calcium, glucagon did not produce any effect on the enzyme. To see if calcium was involved in a regulatory mechanism, cholesterol ester hydrolase activity was measured in cytosol from cells preincubated in a medium without calcium and containing EGTA. This treatment produced a marked reduction in cytosolic Ca2+ concentration with a concomitant threefold stimulation of the esterase activity. Readdition of calcium to Ca2(+)-deprived cells diminished the activation due to calcium deficiency. The present results suggest that 1) cholesterol ester hydrolase could be modulated by a cAMP-mediated mechanism elicited by glucagon in which Ca2+ appears to be involved and 2) the enzyme activity may also be regulated by changes in the intracellular calcium concentration.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Ruiz MB,Ochoa B,Lacort Mdoi
10.1093/oxfordjournals.jbchem.a123070subject
Has Abstractpub_date
1990-03-01 00:00:00pages
476-9issue
3eissn
0021-924Xissn
1756-2651journal_volume
107pub_type
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更新日期:1975-04-01 00:00:00
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更新日期:1996-02-01 00:00:00
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更新日期:2001-08-01 00:00:00
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更新日期:1994-08-01 00:00:00
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更新日期:1985-01-01 00:00:00
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更新日期:1985-03-01 00:00:00
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更新日期:1987-08-01 00:00:00
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pub_type: 杂志文章
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更新日期:1996-01-01 00:00:00
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更新日期:2020-12-26 00:00:00
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pub_type: 杂志文章
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更新日期:1992-06-01 00:00:00