Linked Life Data

12138164

Source:http://linkedlifedata.com/resource/pubmed/id/12138164

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
2002-9-30
pubmed:databankReference
pubmed:abstractText
Heparan sulfate 3-O-sulfotransferase transfers sulfate to the 3-OH position of a glucosamine residue of heparan sulfate (HS) to form 3-O-sulfated HS. The 3-O-sulfated glucosamine residue contributes to two important biological functions of HS: binding to antithrombin and thereby carrying anticoagulant activity, and binding to herpes simplex viral envelope glycoprotein D to serve as an entry receptor for herpes simplex virus 1. A total of five HS 3-O-sulfotransferase isoforms were reported previously. Here we report the isolation and characterization of a novel HS 3-O-sulfotransferase isoform, designated as HS 3-O-sulfotransferase isoform 5 (3-OST-5). 3-OST-5 cDNA was isolated from a human placenta cDNA library and expressed in COS-7 cells. The disaccharide analysis of 3-OST-5-modified HS revealed that 3-OST-5 generated at least three 3-O-sulfated disaccharides as follows: IdoUA2S-AnMan3S, GlcUA-AnMan3S6S, and IdoUA2S-AnMan3S6S. Transfection of the plasmid expressing 3-OST-5 rendered wild type Chinese hamster ovary cells susceptible to the infection by herpes simplex virus 1, suggesting that 3-OST-5-modified HS serves as an entry receptor for herpes simplex virus 1. In addition, 3-OST-5-modified HS bound to herpes simplex viral envelope protein glycoprotein D. Furthermore, we found that 3-OST-5-modified HS also bound to antithrombin, suggesting that 3-OST-5 also produces anticoagulant HS. In summary, our results indicate that a new member of 3-OST family generates both anticoagulant HS and an entry receptor for herpes simplex virus 1. These results provide a new insight regarding the mechanism for the biosynthesis of biologically active HS.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37912-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12138164-Animals, pubmed-meshheading:12138164-Antithrombins, pubmed-meshheading:12138164-Base Sequence, pubmed-meshheading:12138164-Binding Sites, pubmed-meshheading:12138164-Cell Line, pubmed-meshheading:12138164-Chromatography, High Pressure Liquid, pubmed-meshheading:12138164-DNA, Complementary, pubmed-meshheading:12138164-DNA Primers, pubmed-meshheading:12138164-Disaccharides, pubmed-meshheading:12138164-Herpesvirus 1, Human, pubmed-meshheading:12138164-Humans, pubmed-meshheading:12138164-Isoenzymes, pubmed-meshheading:12138164-Mice, pubmed-meshheading:12138164-Molecular Sequence Data, pubmed-meshheading:12138164-Polymerase Chain Reaction, pubmed-meshheading:12138164-Receptors, Virus, pubmed-meshheading:12138164-Recombinant Proteins, pubmed-meshheading:12138164-Sequence Alignment, pubmed-meshheading:12138164-Sequence Homology, Amino Acid, pubmed-meshheading:12138164-Spodoptera, pubmed-meshheading:12138164-Substrate Specificity, pubmed-meshheading:12138164-Sulfotransferases, pubmed-meshheading:12138164-Transfection
pubmed:year
2002
pubmed:articleTitle
Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1.
pubmed:affiliation
Cell and Molecular Biology, Biomedical Center C13, Lund University, Lund S-22184, Sweden.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't