Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
1998-2-2
pubmed:databankReference
pubmed:abstractText
The structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Poly-N-acetyllactosamines are also modified by various carbohydrate residues, forming functional oligosaccharides such as sialyl Lex. Herein we describe the isolation and functional expression of a cDNA encoding beta-1,3-N-acetylglucosaminyltransferase (iGnT), an enzyme that is essential for the formation of poly-N-acetyllactosamine. For this expression cloning, Burkitt lymphoma Namalwa KJM-1 cells were transfected with cDNA libraries derived from human melanoma and colon carcinoma cells. Transfected Namalwa cells overexpressing the i antigen were continuously selected by fluorescence-activated cell sorting because introduced plasmids containing Epstein-Barr virus replication origin can be continuously amplified as episomes. Sibling selection of plasmids recovered after the third consecutive sorting resulted in a cDNA clone that directs the increased expression of i antigen on the cell surface. The deduced amino acid sequence indicates that this protein has a type II membrane protein topology found in almost all mammalian glycosyltransferases cloned to date. iGnT, however, differs in having the longest transmembrane domain among glycosyltransferases cloned so far. The iGnT transcript is highly expressed in fetal brain and kidney and adult brain but expressed ubiquitously in various adult tissues. The expression of the presumed catalytic domain as a fusion protein with the IgG binding domain of protein A enabled us to demonstrate that the cDNA encodes iGnT, the enzyme responsible for the formation of GlcNAcbeta1 --> 3Galbeta1 --> 4GlcNAc --> R structure and poly-N-acetyllactosamine extension.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-107170, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-1329093, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-13292836, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-1531336, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-1544942, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-1699667, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-1701274, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-1701275, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-2243101, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-2451668, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-2579340, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-2662714, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-2841588, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-2953071, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-2954821, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-2970459, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-3015940, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-3597368, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-3624248, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-4291934, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-429966, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-438154, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-6088518, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-6226657, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-6386148, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-6432790, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-6490658, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-6491606, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-6725252, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-6745495, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-6783649, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-7507108, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-7615638, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-7901202, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-8101764, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-8182079, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-8195250, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-8262950, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-8449405, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-8567623, http://linkedlifedata.com/resource/pubmed/commentcorrection/9405606-8631981
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14294-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Expression cloning of cDNA encoding a human beta-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis.
pubmed:affiliation
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida, Tokyo 194, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't