Linked Life Data

8939951

Source:http://linkedlifedata.com/resource/pubmed/id/8939951

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
47
pubmed:dateCreated
1997-1-13
pubmed:abstractText
Type II secretory phospholipase A2 (sPLA2) has been shown to be induced by a variety of proinflammatory stimuli and, therefore, has been implicated in the inflammatory process. In order to determine whether association of sPLA2 with cell surfaces via heparan sulfate proteoglycan is important for its effects on cellular functions, we have identified the critical domain in sPLA2 for heparin and cell surface binding and examined its role in cellular prostaglandin (PG) biosynthesis. Replacement of several conserved Lys residues in the C-terminal region of mouse and rat sPLA2s by Glu resulted in a marked reduction of their capacities to bind to heparin and mammalian cell surfaces without affecting their enzymatic activities toward dispersed phospholipid as a substrate. CHO cells stably transfected with wild-type sPLA2 released about twice as much arachidonic acid (AA) during culture for 10 h with fetal calf serum and interleukin-1beta than cells transfected with vector alone, whereas the ability to enhance AA release was impaired in sPLA2 mutants incapable of binding to cell surfaces. AA released by wild-type sPLA2-transfected CHO cells was metabolized to prostaglandin E2 via prostaglandin endoperoxide H synthase (PGHS)-2 after IL-1beta stimulation, revealing a particular functional linkage of sPLA2 to PGHS-2. In contrast, A23187-initiated immediate AA release over 30 min was not affected by sPLA2 overexpression. Taken together, these results suggest that sPLA2 expressed endogenously and anchored on cell surfaces via its C-terminal heparin-binding domain is involved in the PGHS-2-dependent delayed PG biosynthesis initiated by growth factors and cytokines during long term culture.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30041-51
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Type II secretory phospholipase A2 associated with cell surfaces via C-terminal heparin-binding lysine residues augments stimulus-initiated delayed prostaglandin generation.
pubmed:affiliation
Department of Health Chemistry, School of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't