Linked Life Data

7225401

Source:http://linkedlifedata.com/resource/pubmed/id/7225401

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1981-7-9
pubmed:abstractText
In vitro regulation of the key enzyme of cholesterol synthesis, 3-hydroxy-3-methylglutaryl-CoA reductase (EC 1.1.1.34) by compactin, a competitive inhibitor of the enzyme, and mevalonate was studied in rabbit ileum organ culture. Addition of compactin suppressed ileum homogenate reductase activity by over 80% at concentrations up to 0.5 microgram/ml. In contrast, compactin at the same concentrations added to the culture medium induced reductase activity up to 240% of controls. This increase was blocked by cycloheximide and mevalonolactone at 10 mM, but not by mevalonate (salt form) and cholesterol. Similarly, in contrast to ionized mevalonate, mevalonolactone significantly suppressed reductase activity of cultured intestine at 1 and 10 mM by 23 and 62%, respectively. A minor effect was also observed with preformed enzyme in fresh mucosal homogenate. When endogenous cholesterol synthesis was blocked by compactin, mucosal alkaline phosphatase activity decreased progressively, whereas medium activity from desquamated cells did not change. This distribution of the villous cell marker enzyme is characteristic of a decrease in crypt cell renewal and/or villous cell differentiation. This effect of compactin was also reversible with mevalonolactone. The reductase enzyme induced by compactin was probably latent intracellularly, since tissue cholesterol contents dropped sharply after blockade of endogenous sterol synthesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
663
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
613-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Regulation of 3-hydroxy-3-methylglutaryl-CoA reductase by endogenous sterol synthesis in cultured intestinal mucosa.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't