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Changes in glycosaminoglycan synthesis and in heparan sulfate deposition in human colorectal adenocarcinomas
Author(s) -
Bouziges Françoise,
SimonAssmann P.,
Leberquier C.,
Marescaux J.,
Bellocq J. P.,
Haffen K.,
Kedinger M.
Publication year - 1990
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910460208
Subject(s) - hyaluronic acid , glycosaminoglycan , chondroitin sulfate , proteoglycan , heparan sulfate , chemistry , basement membrane , staining , stromal cell , microbiology and biotechnology , glycoprotein , biochemistry , sulfation , pathology , biology , extracellular matrix , cancer research , medicine , anatomy
Biosynthesis of glycosaminoglycans (GAGs) was studied in morphologically normal colonic mucosa, in peritumoral and tumoral areas, and in colorectal polyps of tumor‐bearing patients. After GAG purification, overall biosynthesis was determined: the general trend was a decrease in GAG production in neoplastic colon, lowest GAG synthesis being observed in Dukes' stage C tumors. Separation by ion‐exchange chromatography of various GAG species and further characterization revealed the presence of hyaluronic acid (HA) and heparan sulfate (HS) molecules in all specimens studied. Chondroitin‐4 sulfate (CS4) was occasionally found in tumor samples. The relative proportion of HA and HS was modified in tumor tissue: i. e. increased HA and decreased HS were observed. Differences in DEAE‐chromatographic behavior were obvious in pathological samples as compared to controls, the hydrodynamic form of HA and the charge density of HS being decreased. The latter could be attributed to undersulfatation of HS molecules. Immunocytochemical detection of HS proteoglycan molecules revealed regular and bright labelling at epithelial‐stromal interface in control samples. In pathological samples, staining was patchy and discontinuous, showing large areas of basement membrane interruption.