Sialyltransferase activity in normal and atherosclerotic human aorta intima

Sialyltransferase activity has been determined in Golgi membrane fractions isolated from atherosclerotic and normal intima of human aorta by measuring the transfer of N-acetylneuraminic acid (NeuAc) from CMP-NeuAc to asialofetuin. The asialofetuin-sialyltransferase activity was found to be twofold h...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2001-04, Vol.66 (4), p.397-401
Main Authors: Gracheva, E V, Samovilova, N N, Golovanova, N K, Il'inskaya, O P, Tararak, E M, Prokazova, N V
Format: Article
Language:English
Subjects:
Adult
Aged
Aorta - enzymology
Arteriosclerosis - enzymology
Enzyme Activation - physiology
Enzymes
Female
Humans
In Vitro Techniques
Kinetics
Male
Membrane Glycoproteins - analysis
Membrane Glycoproteins - isolation & purification
Membrane Glycoproteins - metabolism
Membranes
Reference Values
Sialyltransferases - analysis
Sialyltransferases - isolation & purification
Sialyltransferases - metabolism
Tissues
Tunica Intima - enzymology
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Summary:Sialyltransferase activity has been determined in Golgi membrane fractions isolated from atherosclerotic and normal intima of human aorta by measuring the transfer of N-acetylneuraminic acid (NeuAc) from CMP-NeuAc to asialofetuin. The asialofetuin-sialyltransferase activity was found to be twofold higher in the atherosclerotic intima than in the normal intima. The mean value of the apparent Michaelis constant (Km) for the sialylating enzyme in both tissues did not differ and was 57 microM. In contrast, the maximal velocity (Vmax) was 2-fold higher for the atherosclerotic intima than for the normal intima. These results suggest that expression of asialofetuin-sialyltransferases of the aortal intima may be increased in atherosclerosis.
ISSN:0006-2979
1608-3040
DOI:10.1023/A:1010245328209