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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

A heparin-like glycosaminoglycan from shrimp containing high levels of 3-O-sulfated D-glucosamine groups in an unusual trisaccharide sequence

Texto completo
Chavante, Suely F. [1] ; Brito, Adriana S. [1, 2] ; Lima, Marcelo [3, 4] ; Yates, Edwin [3, 4] ; Nader, Helena [3] ; Guerrini, Marco [5] ; Torri, Giangiacomo [5] ; Bisio, Antonella [5]
Número total de Autores: 8
Afiliação do(s) autor(es):
[1] Univ Fed Rio Grande do Norte, Dept Bioquim, BR-59072970 Natal, RN - Brazil
[2] Univ Fed Rio Grande do Norte, Fac Ciencias Saude Trairi, Santa Cruz, CA - USA
[3] Univ Fed Sao Paulo, Dept Bioquim, Sao Paulo - Brazil
[4] Univ Liverpool, Dept Struct & Chem Biol, Liverpool L69 3BX, Merseyside - England
[5] Ist Ric Chim & Biochim G Ronzoni, Milan - Italy
Número total de Afiliações: 5
Tipo de documento: Artigo Científico
Fonte: Carbohydrate Research; v. 390, p. 59-66, MAY 22 2014.
Citações Web of Science: 14

The detailed characterization of a novel heparin-like glycosaminoglycan purified from the viscera (heads) of the shrimp Litopenaeus vannamei is reported. Structural analysis performed by mono-and two-dimensional nuclear magnetic resonance (NMR) spectroscopy revealed it to be rich in both glucuronic acid and N, 6-sulfated glucosamine residues. The key peculiarities were its high 3-O-sulfated glucosamine content compared to mammalian heparins; a residue which is usually associated with the antithrombin (AT) binding site, and the location of these residues within 2-O-sulfated iduronate and glucuronate-containing sequences (I(2S-)A{*}-G), a situation not found in mammalian heparin. It also exhibited higher molecular weight (similar to 36 kDa) than conventional heparin (similar to 16 kDa) but, negligible anticoagulant activity (similar to 5 IU/mg compared to heparin similar to 190 IU/mg) and stabilization of AT, which has been linked directly to anticoagulation activity. A high affinity fraction, eluting at a similar salt concentration (0.75-1.5 M NaCl) from an antithrombin affinity column, to the high affinity fraction of heparin, also showed only weak thermal stabilization of AT (+ similar to 2 degrees C). These structural peculiarities may help elucidate more clearly the relationship between structure and function of sulfated polysaccharides, and provide useful model compounds with which to better understand interactions of biological significance. (C) 2014 Published by Elsevier Ltd. (AU)

Processo FAPESP: 12/00850-1 - Compostos bioativos obtidos a partir de resíduos de carcinicultura e modificações químicas de heparina
Beneficiário:Marcelo Andrade de Lima
Linha de fomento: Bolsas no Brasil - Pós-Doutorado