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 journalJournal articleResearchpeer-review

Harvard

Mandel, U, Hassan, H, Therkildsen, MH, Rygaard, J, Jakobsen, MH, Juhl, BR, Dabelsteen, E & Clausen, H 1999, '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', Glycobiology, vol. 9, no. 1, pp. 43-52.

APA

Mandel, U., Hassan, H., Therkildsen, M. H., Rygaard, J., Jakobsen, M. H., Juhl, B. R., ... Clausen, H. (1999). 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. Glycobiology, 9(1), 43-52.

Vancouver

Mandel U, Hassan H, Therkildsen MH, Rygaard J, Jakobsen MH, Juhl BR et al. 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. Glycobiology. 1999 Jan;9(1):43-52.

Author

Mandel, U ; Hassan, H ; Therkildsen, M H ; Rygaard, J ; Jakobsen, M H ; Juhl, B R ; Dabelsteen, Erik ; Clausen, H. / 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. In: Glycobiology. 1999 ; Vol. 9, No. 1. pp. 43-52.

Bibtex

@article{96a018153f3b4ecead58871f68184644,
title = "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",
abstract = "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.",
keywords = "Animals, Antibodies, Monoclonal, Baculoviridae, Carcinoma, Squamous Cell, Cell Differentiation, Epithelium, Female, Glycosylation, HeLa Cells, Humans, Immunohistochemistry, Male, Mice, Mice, Inbred BALB C, Mouth Mucosa, N-Acetylgalactosaminyltransferases, Spermatozoa, Spodoptera, Tumor Cells, Cultured",
author = "U Mandel and H Hassan and Therkildsen, {M H} and J Rygaard and Jakobsen, {M H} and Juhl, {B R} and Erik Dabelsteen and H Clausen",
year = "1999",
month = "1",
language = "English",
volume = "9",
pages = "43--52",
journal = "Glycobiology",
issn = "0959-6658",
publisher = "Oxford University Press",
number = "1",

}

RIS

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

VL - 9

SP - 43

EP - 52

JO - Glycobiology

JF - Glycobiology

SN - 0959-6658

IS - 1

ER -

ID: 119593790