Linked Life Data

8038192

Source:http://linkedlifedata.com/resource/pubmed/id/8038192

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-8-19
pubmed:abstractText
Fungal (1,3)-beta-glucan synthases are sensitive to a wide range of lipophilic inhibitors and it has been proposed that enzyme activity is highly sensitive to perturbations of the membrane environment. Yeast membranes were exposed to phospholipases and various lipophilic compounds, and the resultant effects on glucan synthase activity were ascertained. Glucan synthase from Saccharomyces cerevisiae was rapidly inactivated by phospholipase A2 (PLA2), and to a lesser extent by phospholipase C. Inactivation was time and dose-dependent and was protected against by EDTA and fatty-acid binding proteins (bovine and human serum albumins). Albumins also partially protected against inhibition by papulacandin B. PLA2 reaction products were structurally characterized and it was shown that fatty acids and lysophospholipids were the inhibitory moieties, with no novel inhibitory compounds apparent. Glucan synthase was inhibited by a range of fatty acids, monoglycerides and lysophospholipids. Inhibition by fatty acids was non-competitive, and progressive binding of [14C]oleic acid correlated with activity loss. Fluorescence anisotropy studies using diphenylhexatriene (DPH) confirm that fatty acids increase membrane fluidity. These results are consistent with proposals suggesting that glucan synthase inhibition is due in part to non-specific detergent-like disruption of the membrane environment, in addition to direct interactions of lipophilic inhibitors with specific target sites on the enzyme complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
1193
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31-40
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Inhibition of yeast (1,3)-beta-glucan synthase by phospholipase A2 and its reaction products.
pubmed:affiliation
Department of Food Science, Rutgers University, Cook College, New Jersey Agricultural Experiment Station, New Brunswick 08903-0231.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't