Document Detail


Characterization of a family of structurally related glycoproteins expressing beta 1-6-branched asparagine-linked oligosaccharides in human colon carcinoma cells.
MedLine Citation:
PMID:  1567368     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Previous studies have established that metastatic tumour cells express high levels of beta 1-6-branched Asn-linked oligosaccharides which can be detected with the lectin leucoagglutinin (L-PHA) [Dennis, Laferté, Waghorne, Breitman & Kerbel (1987) Science 236, 582-585]. In order to identify L-PHA-binding glycoproteins which may play a role specifically in colon cancer, we have prepared monoclonal antibodies (MAbs) to the moderately well-differentiated human colon carcinoma cell line HT29. In this paper we present the initial characterization of a family of structurally related L-PHA-binding glycoproteins detected by MAb 1H9 which are differentially expressed and processed by HT29 cells and by two other human colon carcinoma cell lines, SW480 and SW620. In contrast to HT29, the SW480 and SW620 cell lines were established from a poorly differentiated grade III/IV primary tumour and one of its lymph node metastases respectively. MAb 1H9 detects in HT29 cells a conformational determinant present on three L-PHA-binding glycoproteins of 100, 70 and 25kDa, as well as a 74 kDa glycoprotein with high-mannose-type Asn-linked oligosaccharides. Pulse-chase experiments and peptide mapping analyses revealed that the 74 kDa and 100 kDa species are related by carbohydrate processing and are probably derived from a common 76 kDa precursor. On the other hand, the 70 kDa glycoprotein is synthesized from an endoglycosidase H-sensitive precursor of 56 kDa which is structurally related to, but distinct from, the aforementioned 76 kDa precursor. In addition, the 100 kDa species is secreted into the culture medium, whereas the 70 kDa glycoprotein is retained intracellularly. SW480 and SW620 cells showed qualitative and quantitative differences from HT29 cells, including increased secretion of a smaller L-PHA-binding glycoprotein of 92 kDa into the culture medium, as well as apparent differences in glycosylation of the intracellular 66 kDa glycoprotein. These results suggested that the expression, glycosylation and subcellular localization of this family of L-PHA-binding glycoproteins may correlate with the differentiation status of colon cancer cells and/or reflect biochemical changes. characteristic of more progressive metastatic tumours.
Authors:
S Laferté; L C Loh
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  283 ( Pt 1)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1992 Apr 
Date Detail:
Created Date:  1992-05-19     Completed Date:  1992-05-19     Revised Date:  2010-09-07    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  193-201     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Saskatchewan, Saskatoon, Canada.
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MeSH Terms
Descriptor/Qualifier:
Agglutinins / metabolism
Animals
Antibodies, Monoclonal
Antigens, CD*
Antigens, Neoplasm / analysis,  biosynthesis
Asparagine / chemistry*
Carbohydrate Sequence
Colonic Neoplasms / chemistry*,  immunology,  metabolism
Culture Media
Fluorescent Antibody Technique
Glycoproteins / chemistry*
Humans
Leukocytes / immunology
Lysosome-Associated Membrane Glycoproteins
Membrane Glycoproteins
Mice
Mice, Inbred BALB C
Molecular Sequence Data
Neoplasm Proteins / chemistry*
Oligosaccharides / chemistry*
Structure-Activity Relationship
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
0/Agglutinins; 0/Antibodies, Monoclonal; 0/Antigens, CD; 0/Antigens, Neoplasm; 0/Culture Media; 0/Glycoproteins; 0/Lysosome-Associated Membrane Glycoproteins; 0/Membrane Glycoproteins; 0/Neoplasm Proteins; 0/Oligosaccharides; 7006-34-0/Asparagine
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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