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Titolo:
Interactions of fibrillin-1 with heparin/heparan sulfate, implications formicrofibrillar assembly
Autore:
Tiedemann, K; Batge, B; Muller, PK; Reinhardt, DP;
Indirizzi:
Med Univ Lubeck, Inst Med Mol Biol, D-23538 Lubeck, Germany Med Univ Lubeck Lubeck Germany D-23538 Mol Biol, D-23538 Lubeck, Germany
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 38, volume: 276, anno: 2001,
pagine: 36035 - 36042
SICI:
0021-9258(20010921)276:38<36035:IOFWHS>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
FACTOR-LIKE DOMAINS; MARFAN-SYNDROME; EXTRACELLULAR-MATRIX; HEPARAN-SULFATE; CALCIUM-BINDING; PROTEOGLYCAN SYNTHESIS; DERMAL FIBROBLASTS; MOLECULAR-CLONING; CELL-ADHESION; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Reinhardt, DP Med Univ Lubeck, Inst Med Mol Biol, Ratzeburger Allee 160, D-23538 Lubeck,Germany Med Univ Lubeck Ratzeburger Allee 160 Lubeck GermanyD-23538
Citazione:
K. Tiedemann et al., "Interactions of fibrillin-1 with heparin/heparan sulfate, implications formicrofibrillar assembly", J BIOL CHEM, 276(38), 2001, pp. 36035-36042

Abstract

Fibrillin-1 is a major constituent of the 10-12 nm extracellular microfibrils. Here we identify, characterize, and localize heparin/heparan sulfate-binding sites in fibrillin-1 and report on the role of such glycosaminoglycans in the assembly of fibrillin-1. By using different binding assays, we localize two calcium-independent heparin-binding sites to the N-terminal (Arg(45)-Thr(450)) and C-terminal (Asp(1528)-Arg(2731)) domains of fibrillin-1. A calcium-dependent-binding site was localized to the central (Asp(1028)-Thr(1486)) region of fibrillin-1. Heparin binding to these sites can be inhibited by a highly sulfated and iduronated form of heparan sulfate but not by chondroitin 4-sulfate, chondroitin 6-sulfate, and dermatan sulfate, demonstrating that the heparin binding regions represent binding domains for heparan sulfate. When heparin or heparan sulfate was added to cultures of skinfibroblasts, the assembly of fibrillin-1 into a microfibrillar network wassignificantly reduced. Western blot analysis demonstrated that this effectwas not due to a reduced amount of fibrillin-1 secreted into the culture medium. Inhibition of the attachment of glycosaminoglyeans to core proteins of proteoglycans by beta -D-xylosides resulted in a significant reduction of the fibrillin-1 network. These studies suggest that binding of fibrillin-1 to protcoglycan-associated heparan sulfate chains is an important step inthe assembly of microfibrils.

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Documento generato il 04/12/20 alle ore 03:17:20