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
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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. / Mandel, U; Hassan, H; Therkildsen, M H; Rygaard, J; Jakobsen, M H; Juhl, B R; Dabelsteen, Erik; Clausen, H.
In: Glycobiology, Vol. 9, No. 1, 01.1999, p. 43-52.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas
T2 - immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family
AU - Mandel, U
AU - Hassan, H
AU - Therkildsen, M H
AU - Rygaard, J
AU - Jakobsen, M H
AU - Juhl, B R
AU - Dabelsteen, Erik
AU - Clausen, H
PY - 1999/1
Y1 - 1999/1
N2 - 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.
AB - 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.
KW - Animals
KW - Antibodies, Monoclonal
KW - Baculoviridae
KW - Carcinoma, Squamous Cell
KW - Cell Differentiation
KW - Epithelium
KW - Female
KW - Glycosylation
KW - HeLa Cells
KW - Humans
KW - Immunohistochemistry
KW - Male
KW - Mice
KW - Mice, Inbred BALB C
KW - Mouth Mucosa
KW - N-Acetylgalactosaminyltransferases
KW - Spermatozoa
KW - Spodoptera
KW - Tumor Cells, Cultured
M3 - Journal article
C2 - 9884405
VL - 9
SP - 43
EP - 52
JO - Glycobiology
JF - Glycobiology
SN - 0959-6658
IS - 1
ER -
ID: 119593790