Linked Life Data

2793870

Source:http://linkedlifedata.com/resource/pubmed/id/2793870

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1989-11-17
pubmed:abstractText
The structures of cell-associated heparan sulfate (HS) proteoglycans and their interaction with the plasma membrane was studied using rat ovarian granulosa cell culture. HS proteoglycans were either metabolically labeled by incubating cell cultures with [3H] leucine and [35S]sulfate or labeled in plasma membrane preparations with a photoactivatable reagent, 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine (TID), a compound which has been shown to selectively label the hydrophobic membrane-binding domains of several proteins. After purification of HS proteoglycans from the labeled cell cultures or from the labeled membrane preparations by repeated Q-Sepharose ion exchange chromatography in 8 M urea, they were analyzed by Superose 6 gel filtration and octyl-Sepharose chromatography both in 4 M guanidine HCl. The results indicated that the HS proteoglycans were labeled with 125I and therefore have an intramembranous domain. Phospholipase C (Bacillus thuringiensis), which specifically cleaves phosphatidylinositol membrane anchors, released approximately 25% of the 35S-labeled HS proteoglycans from the cell surface as well as 20-30% of the 125I-label from the 125I-TID-labeled HS proteoglycans. These data indicate that a subpopulation of HS proteoglycans are intercalated into the plasma membrane through a linkage structure involving phosphatidylinositol. Phospholipase C-resistant, 125I-labeled HS proteoglycans represent those species inserted into membrane through an intercalated peptide sequence. Core protein size of phosphatidylinositol-anchored species estimated by polyacrylamide gel electrophoresis after heparitinase digestion was approximately 80 kDa, and it was significantly larger than that of the directly intercalated species (approximately 70 kDa).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3-(trifluoromethyl)-3-(3-iodophenyl)..., http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels, http://linkedlifedata.com/resource/pubmed/chemical/Azirines, http://linkedlifedata.com/resource/pubmed/chemical/Heparin, http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Mannosephosphates, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols, http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans, http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases, http://linkedlifedata.com/resource/pubmed/chemical/heparin proteoglycan, http://linkedlifedata.com/resource/pubmed/chemical/inositol 2-monophosphate, http://linkedlifedata.com/resource/pubmed/chemical/mannose-6-phosphate
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17551-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Two forms of plasma membrane-intercalated heparan sulfate proteoglycan in rat ovarian granulosa cells. Labeling of proteoglycans with a photoactivatable hydrophobic probe and effect of the membrane anchor-specific phospholipase C.
pubmed:affiliation
Bone Research Branch, National Institute of Dental Research, Bethesda, Maryland 20892.
pubmed:publicationType
Journal Article