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Vol. 273, Issue 1, 51-57, January 2, 1998
From the We report a detailed analysis of heparan sulfate
(HS) structure using a model of human colon carcinogenesis.
Metabolically radiolabeled HS was isolated from adenoma and carcinoma
cells. The chain length of HS was the same in both cell populations
(Mr 20,000; 45-50 disaccharides), and the
chains contained on average of two sulfated domains (S domains),
identified by heparinase I scission. This enzyme produced fragments of
approximate size 7 kDa, suggesting that the S domains were evenly
spaced in the intact HS chain. The degree of polymer sulfation and the
patterns of sulfation were strikingly different between the two HS
species. When compared with adenoma HS, the iduronic acid
2-O-sulfate content of the carcinoma-derived material was
reduced by 33%, and the overall level of N-sulfation was
reduced by 20%. However, the level of 6-O-sulfation was
increased by 24%, and this was almost entirely attributable to an
enhanced level of N-sulfated glucosamine 6-O-sulfate, a species whose data implied was mainly
located in the mixed sequences of alternating N-sulfated
and N-acetylated disaccharides. The results indicate that
in the transition to malignancy in human colon adenoma cells, the
overall molecular organization of HS is preserved, but there are
distinct modifications in both the S domains and their flanking mixed
domains that may contribute to the aberrant behavior of the cancer
cell.
Heparan Sulfate Undergoes Specific Structural Changes during the
Progression from Human Colon Adenoma to Carcinoma in
Vitro
,,,, and
Cancer Research Campaign Department,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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