Linked Life Data

12473113

Source:http://linkedlifedata.com/resource/pubmed/id/12473113

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2002-12-10
pubmed:abstractText
O-Glycosylation of three consecutive Thr residues in a fluorescein-conjugated peptide PTTTPLK - which mimics a portion of mucin 2 - by four isozymes of UDP-N-acetylgalactosaminyltransferases (pp-GalNAc-T1, T2, T3, or T4) was investigated. Partially glycosylated versions of this peptide, PT*TTPLK, PTTT*PLK, PT*TT*PLK, PTT*T*PLK, PT* degrees TTPLK, and PTTT* degrees PLK (*, N-acetylgalactosamine; degrees, galactose), were also tested. The products were separated by RP-HPLC and characterized by MALDI-TOF MS and peptide sequencing. The first and the third Thr residues act as the peptide's initial glycosylation sites for pp-GalNAc-T4, which were different from the sites for pp-GalNAc-T1 and T2 (the first Thr residue) or T3 (the third Thr residue) shown in our previous report. All pp-GalNAc-T isozymes tested exhibited distinct specificities toward glycopeptides. The most notable findings were: (a) prior incorporation of an N-acetylgalactosamine residue at the third Thr greatly enhanced N-acetylgalactosamine incorporation into the other Thr residues when pp-GalNAc-T2, T3, or T4 were used; (b) the enhancing effect of the N-acetylgalactosamine residue on the third Thr was completely abrogated by galactosylation of this N-acetylgalactosamine; (c) prior incorporation of an N-acetylgalactosamine at the first Thr did not have any enhancing effect; (d) pp-GalNAc-T2 was unique as it transferred N-acetylgalactosamine into the second Thr residue only when N-acetylgalactosamine was attached to the third one.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6173-83
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:12473113-Acetylgalactosamine, pubmed-meshheading:12473113-Amino Acid Sequence, pubmed-meshheading:12473113-Chromatography, High Pressure Liquid, pubmed-meshheading:12473113-Detergents, pubmed-meshheading:12473113-Galactosyltransferases, pubmed-meshheading:12473113-Glycopeptides, pubmed-meshheading:12473113-Glycosylation, pubmed-meshheading:12473113-Humans, pubmed-meshheading:12473113-Molecular Sequence Data, pubmed-meshheading:12473113-Peptides, pubmed-meshheading:12473113-Protein Binding, pubmed-meshheading:12473113-Protein Isoforms, pubmed-meshheading:12473113-Protein Structure, Tertiary, pubmed-meshheading:12473113-Recombinant Proteins, pubmed-meshheading:12473113-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:12473113-Substrate Specificity, pubmed-meshheading:12473113-Threonine, pubmed-meshheading:12473113-Time Factors, pubmed-meshheading:12473113-Uridine Diphosphate N-Acetylgalactosamine
pubmed:year
2002
pubmed:articleTitle
O-GalNAc incorporation into a cluster acceptor site of three consecutive threonines. Distinct specificity of GalNAc-transferase isoforms.
pubmed:affiliation
Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't