Monoclonal antibody 4C4-mAb specifically recognizes keratan sulphate proteoglycan on human embryonal carcinoma cells

2003 ◽  
Vol 201 (1) ◽  
pp. 90-98 ◽  
Author(s):  
Mariko Fukuma ◽  
Hitoshi Abe ◽  
Hajime Okita ◽  
Taketo Yamada ◽  
Jun-ichi Hata
Keyword(s):  
Monoclonal Antibody ◽  
Embryonal Carcinoma ◽  
Carcinoma Cells ◽  
Embryonal Carcinoma Cells ◽  
Keratan Sulphate ◽  
Sulphate Proteoglycan

scholarly journals A novel keratan sulphate proteoglycan from a human embryonal carcinoma cell line

1992 ◽  
Vol 286 (3) ◽  
pp. 959-966 ◽  
Author(s):  
S Cooper ◽  
M F Pera ◽  
W Bennett ◽  
J T Finch
Keyword(s):  
Embryonal Carcinoma ◽  
Broad Band ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Carcinoma Cells ◽  
Embryonal Carcinoma Cell ◽  
Embryonal Carcinoma Cells ◽  
Keratan Sulphate ◽  
Major Band ◽  
Sulphate Proteoglycan

We describe here the purification and partial characterization of a 200 kDa keratan sulphate proteoglycan found in the pericellular matrix of human embryonal carcinoma cells. Previously we have shown that this molecule is recognized by a monoclonal antibody (GCTM-2). The antigen was isolated using ion-exchange chromatography and gel filtration, purification being monitored by e.l.i.s.a. using GCTM-2. Metabolic labelling of GCT 27 C-4 embryonal carcinoma cells with sodium [35S]sulphate resulted in the incorporation of [35S]sulphate into the purified molecule. Throughout the purification procedure, the peaks of 35S radioactivity were coincident with the peaks of immunoreactivity, and this label was released both by digestion with keratanase and chondroitinase, confirming the proteoglycan nature of the antigen. The intact molecule ran as a single broad band of 200 kDa, which has been identified by silver staining and immunoblotting following gel electrophoresis. Amino acid analysis of the purified antigen indicated a high content of serine, glycine and aspartic acid/asparagine residues. Visualization by rotary-shadowing electron microscopy suggests that the purified material forms large aggregates, even under denaturing conditions. Deglycosylation of this preparation with trifluoromethanesulphonic acid yielded a major band of 55 kDa and a minor band of 48 kDa. The biochemical nature of the molecule described here, along with tissue distribution studies using GCTM-2, indicates that the antigen is not related to previously described keratan sulphate proteoglycans.

An anti-carbohydrate monoclonal antibody inhibits cell-substratum adhesion of F9 embryonal carcinoma cells

1986 ◽  
Vol 164 (1) ◽  
pp. 49-62 ◽  
Author(s):  
Shigeru Nomoto ◽  
Hisako Muramatsu ◽  
Masayuki Ozawa ◽  
Tatsuo Suganuma ◽  
Masaaki Tashiro ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Embryonal Carcinoma ◽  
Carcinoma Cells ◽  
Embryonal Carcinoma Cells ◽  
F9 Embryonal Carcinoma Cells
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