In vitro galactosylation of a 110-kDa glycoprotein by an endogenous cell surface galactosyltransferase correlates with the invasiveness of adrenal carcinoma cells
- Johns Hopkins Univ. School of Medicine, Baltimore, MD (USA)
- National Institutes of Health, Bethesda, MD (USA)
The authors have examined the role of a cell surface galactosyltransferase, laminin, and laminin-binding protein (receptor) in the invasion of clonal derivatives of a murine adrenal carcinoma cell line. Although a 10-fold variation was found in the ability to invade a reconstituted basement membrane matrix, levels of intracellular laminin and the laminin-binding protein were shown to be present and secreted equally in all lines. Of the eight lines tested, seven showed a correlation between invasion and the incorporation of ({sup 3}H)galactose from UDP-({sup 3}H)galactose into a 90- to 110-kDa protein. One noninvasive line (clone HSR), however, retained high galactosyltransferase activity yet could not galactosylate the endogenous 90- to 110-kDa substrate. Interestingly, this clone was unable to attach to laminin. Although high galactosyltransferase activity can be consistent with cells of high invasiveness, the results suggest that the galactosylation status of a 90- to 110-kDa Y1 cell surface glycoprotein is most indicative of invasion potential.
- OSTI ID:
- 6983901
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (USA), Vol. 86:16; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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GLYCOPROTEINS
RECEPTORS
GLYCOSYL TRANSFERASES
BIOCHEMISTRY
TRITIUM COMPOUNDS
UPTAKE
TUMOR CELLS
ENZYME ACTIVITY
CARCINOMAS
GALACTOSE
MEMBRANE PROTEINS
MICE
RECOMBINANT DNA
SECRETION
ALDEHYDES
ANIMAL CELLS
ANIMALS
CARBOHYDRATES
CHEMISTRY
DISEASES
DNA
ENZYMES
HEXOSES
HYDROGEN COMPOUNDS
MAMMALS
MONOSACCHARIDES
NEOPLASMS
NUCLEIC ACIDS
ORGANIC COMPOUNDS
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RODENTS
SACCHARIDES
TRANSFERASES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques