EFFECT of MONENSIN ON the SULFATION of HEPARAN-SULFATE PROTEOGLYCAN FROM ENDOTHELIAL-CELLS

EFFECT of MONENSIN ON the SULFATION of HEPARAN-SULFATE PROTEOGLYCAN FROM ENDOTHELIAL-CELLS

Autor Sampaio, L. O. Google Scholar
Dietrich, C. P. Google Scholar
Colburn, P. Google Scholar
BUONASSISI, V Google Scholar
Nader, H. B. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo Monensin is a monovalent metal ionophore that affects the intracellular translocation of secretory proteins at the level of trans-Golgi cisternae. Exposure of endothelial cells to monensin results in the synthesis of heparan sulfate and chondroitin sulfate with a lower degree of sulfation. the inhibition is dose dependent and affects the ratio [S-35]-sulfate/[H-3]-hexosamine of heparan sulfate from both cells and medium, with no changes in their molecular weight. By the use of several degradative enzymes (heparitinases, glycuronidase, and sulfatases) the fine structure of the heparan sulfate synthesized by control and monensin-treated cells was investigated. the results have shown that among the six heparan sulfate disaccharides there is a specific decrease of the ones bearing a sulfate ester at the 6-position of the glucosamine moiety. All other biosynthetic steps were not affected by monensin. the results are indicative that monensin affects the hexosamine C-6 sulfation, and that this sterification is the last step of the heparan sulfate biosynthesis and should occur at the trans-Golgi compartment.
Palavra-chave GLYCOSAMINOGLYCAN-GOLGI COMPLEX
GLYCOSAMINOGLYCAN BIOSYNTHESIS
6-SULFATION INHIBITION
Idioma Inglês
Data de publicação 1992-09-01
Publicado em Journal of Cellular Biochemistry. New York: Wiley-liss, v. 50, n. 1, p. 103-110, 1992.
ISSN 0730-2312 (Sherpa/Romeo, fator de impacto)
Publicador Wiley-Blackwell
Extensão 103-110
Fonte http://dx.doi.org/10.1002/jcb.240500115
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1992JL75100012
Endereço permanente http://repositorio.unifesp.br/handle/11600/25274

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