UDP-galactose:globoside galactosyltransferase in murine kidney.

There are increased levels of stage-specific embryonic antigens-3 and -1 (SSEA-3 and SSEA-1) globo-series glycolipids in male versus female DBA/2 and C57BL/6 kidneys, respectively. To determine what enzymatic steps may be responsible for these differences, the activity and properties of UDP-galactos...

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Main Authors: O Koul, M Prada-Maluf, RH McCluer
Format: Article
Language:English
Published: Elsevier 1990-12-01
Series:Journal of Lipid Research
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520421108
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author O Koul
M Prada-Maluf
RH McCluer
author_facet O Koul
M Prada-Maluf
RH McCluer
author_sort O Koul
collection DOAJ
description There are increased levels of stage-specific embryonic antigens-3 and -1 (SSEA-3 and SSEA-1) globo-series glycolipids in male versus female DBA/2 and C57BL/6 kidneys, respectively. To determine what enzymatic steps may be responsible for these differences, the activity and properties of UDP-galactose:globoside galactosyltransferase were studied in male and female mouse kidney microsomes. This enzyme participates in the biosynthesis of galactosylgloboside, SSEA-3 glycolipid; the reaction product was identified by high performance thin-layer chromatography (HPTLC) immunostaining. In C57BL/6 mice, the specific activity of the enzyme, in the presence of CHAPS, was 2-fold greater in the male than that in the female. Optimum pH for the enzyme from both sexes was about 5.6, and Mn2+ was essential for maximal activity. Fifty percent of the male and female enzyme activity was lost after preincubating the microsomes for 1 min at 55 degrees C; thereafter, the enzyme from female microsomes had a slower rate of denaturation. The Km for globoside in presence of sodium cholate for both male and female was 0.035 mM, but it was approximately 2-fold greater for the female in presence of CHAPS. The enzyme in male and female microsomes was differentially activated by CHAPS and cholate. The results suggest the presence of an enzyme modulator in these membranes. In DBA/2 mice, the enzyme activity was about 2-fold greater in males than that in the female. The specific activity of the enzyme in the two strains was of a similar magnitude.(ABSTRACT TRUNCATED AT 250 WORDS)
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spelling doaj.art-530d751c59714863917a0e6161565f442022-12-21T22:09:24ZengElsevierJournal of Lipid Research0022-22751990-12-01311222272234UDP-galactose:globoside galactosyltransferase in murine kidney.O Koul0M Prada-Maluf1RH McCluer2Department of Biochemistry, E. K. Shriver Center, Waltham, MA 02254.Department of Biochemistry, E. K. Shriver Center, Waltham, MA 02254.Department of Biochemistry, E. K. Shriver Center, Waltham, MA 02254.There are increased levels of stage-specific embryonic antigens-3 and -1 (SSEA-3 and SSEA-1) globo-series glycolipids in male versus female DBA/2 and C57BL/6 kidneys, respectively. To determine what enzymatic steps may be responsible for these differences, the activity and properties of UDP-galactose:globoside galactosyltransferase were studied in male and female mouse kidney microsomes. This enzyme participates in the biosynthesis of galactosylgloboside, SSEA-3 glycolipid; the reaction product was identified by high performance thin-layer chromatography (HPTLC) immunostaining. In C57BL/6 mice, the specific activity of the enzyme, in the presence of CHAPS, was 2-fold greater in the male than that in the female. Optimum pH for the enzyme from both sexes was about 5.6, and Mn2+ was essential for maximal activity. Fifty percent of the male and female enzyme activity was lost after preincubating the microsomes for 1 min at 55 degrees C; thereafter, the enzyme from female microsomes had a slower rate of denaturation. The Km for globoside in presence of sodium cholate for both male and female was 0.035 mM, but it was approximately 2-fold greater for the female in presence of CHAPS. The enzyme in male and female microsomes was differentially activated by CHAPS and cholate. The results suggest the presence of an enzyme modulator in these membranes. In DBA/2 mice, the enzyme activity was about 2-fold greater in males than that in the female. The specific activity of the enzyme in the two strains was of a similar magnitude.(ABSTRACT TRUNCATED AT 250 WORDS)http://www.sciencedirect.com/science/article/pii/S0022227520421108
spellingShingle O Koul
M Prada-Maluf
RH McCluer
UDP-galactose:globoside galactosyltransferase in murine kidney.
Journal of Lipid Research
title UDP-galactose:globoside galactosyltransferase in murine kidney.
title_full UDP-galactose:globoside galactosyltransferase in murine kidney.
title_fullStr UDP-galactose:globoside galactosyltransferase in murine kidney.
title_full_unstemmed UDP-galactose:globoside galactosyltransferase in murine kidney.
title_short UDP-galactose:globoside galactosyltransferase in murine kidney.
title_sort udp galactose globoside galactosyltransferase in murine kidney
url http://www.sciencedirect.com/science/article/pii/S0022227520421108
work_keys_str_mv AT okoul udpgalactoseglobosidegalactosyltransferaseinmurinekidney
AT mpradamaluf udpgalactoseglobosidegalactosyltransferaseinmurinekidney
AT rhmccluer udpgalactoseglobosidegalactosyltransferaseinmurinekidney