Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-2-10
pubmed:abstractText
Mucin-type O-glycosylation is initiated by a large family of UDP-GalNAc: polypeptide N -acetyl-galactosaminyltransferases (GalNAc-transferases). Individual GalNAc-transferases appear to have different functions and Northern analysis indicates that they are differently expressed in different organs. This suggests that O-glycosylation may vary with the repertoire of GalNAc-transferases expressed in a given cell. In order to study the repertoire of GalNAc-transferases in situ in tissues and changes in tumors, we have generated a panel of monoclonal antibodies (MAbs) with well defined specificity for human GalNAc-T1, -T2, and -T3. Application of this panel of novel antibodies revealed that GalNAc- transferases are differentially expressed in different cell lines, in spermatozoa, and in oral mucosa and carcinomas. For example, GalNAc-T1 and -T2 but not -T3 were highly expressed in WI38 cells, and GalNAc-T3 but not GalNAc-T1 or -T2 was expressed in spermatozoa. The expression patterns in normal oral mucosa were found to vary with cell differentiation, and for GalNAc-T2 and -T3 this was reflected in oral squamous cell carcinomas. The expression pattern of GalNAc-T1 was on the other hand changed in tumors to either total loss or expression in cytological poorly differentiated tumor cells, where the normal undifferentiated cells lacked expression. These results demonstrate that the repertoire of GalNAc-transferases is different in different cell types and vary with cellular differentiation, and malignant transformation. The implication of this is not yet fully understood, but it suggests that specific changes in sites of O-glycosylation of proteins may occur as a result of changes in the repertoire of GalNAc-transferases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0959-6658
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43-52
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9884405-Animals, pubmed-meshheading:9884405-Antibodies, Monoclonal, pubmed-meshheading:9884405-Baculoviridae, pubmed-meshheading:9884405-Carcinoma, Squamous Cell, pubmed-meshheading:9884405-Cell Differentiation, pubmed-meshheading:9884405-Epithelium, pubmed-meshheading:9884405-Female, pubmed-meshheading:9884405-Glycosylation, pubmed-meshheading:9884405-HeLa Cells, pubmed-meshheading:9884405-Humans, pubmed-meshheading:9884405-Immunohistochemistry, pubmed-meshheading:9884405-Male, pubmed-meshheading:9884405-Mice, pubmed-meshheading:9884405-Mice, Inbred BALB C, pubmed-meshheading:9884405-Mouth Mucosa, pubmed-meshheading:9884405-N-Acetylgalactosaminyltransferases, pubmed-meshheading:9884405-Spermatozoa, pubmed-meshheading:9884405-Spodoptera, pubmed-meshheading:9884405-Tumor Cells, Cultured
pubmed:year
1999
pubmed:articleTitle
Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family.
pubmed:affiliation
Department of Oral Diagnostics, School of Dentistry, Faculty of Health Sciences, University of Copenhagen, Norre Alle 20, 2200 N, Denmark.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't