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Titolo:
Initial steps in assembly of microfibrils - Formation of disulfide-cross-linked multimers containing fibrillin-1
Autore:
Reinhardt, DP; Gambee, JE; Ono, RN; Bachinger, HP; Sakai, LY;
Indirizzi:
Shriners Hosp Crippled Childrens, Portland, OR 97201 USA Shriners Hosp Crippled Childrens Portland OR USA 97201 land, OR 97201 USA Oregon Hlth Sci Univ, Dept Biochem & Mol Biol, Portland, OR 97201 USA Oregon Hlth Sci Univ Portland OR USA 97201 l Biol, Portland, OR 97201 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 3, volume: 275, anno: 2000,
pagine: 2205 - 2210
SICI:
0021-9258(20000121)275:3<2205:ISIAOM>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
BETA-BINDING-PROTEIN; MARFAN-SYNDROME; CALCIUM-BINDING; LATENT; MUTATIONS; COMPONENT; GENE; IDENTIFICATION; ORGANIZATION; SEQUENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Sakai, LY Shriners Hosp Crippled Childrens, 3101 SW Sam Jackson Pk Rd, Portland, OR 97201 USA Shriners Hosp Crippled Childrens 3101 SW Sam Jackson PkRd Portland OR USA 97201
Citazione:
D.P. Reinhardt et al., "Initial steps in assembly of microfibrils - Formation of disulfide-cross-linked multimers containing fibrillin-1", J BIOL CHEM, 275(3), 2000, pp. 2205-2210

Abstract

Fibrillins are the major constituents of extracellular microfibrils, How fibrillin molecules assemble into microfibrils is not known. Sequential extractions and pulse-chase labeling of organ cultures of embryonic chick aortae revealed rapid formation of disulfide-cross-linked aggregates containing fibrillin-1. These results demonstrated that intermolecular disulfide bond formation is an initial step in the assembly process. To identify free cysteine residues available for intermolecular cross-linking, small recombinantpeptides of fibrillin-1 harboring candidate cysteine residues were analyzed. Results revealed that the first four cysteine residues in the unique N terminus form intramolecular disulfide bonds. One cysteine residue (Cys(204)) in the first hybrid domain of fibrillin-1 was found to occur as a free thiol and is therefore a good candidate for intermolecular disulfide bonding in initial steps of the assembly process, Furthermore, evidence indicated that the comparable cysteine residue in fibrillin-2 (Cys(233)) also occurs as a free thiol. These free cysteine residues in fibrillins are readily available for intermolecular disulfide bond formation, as determined by reaction with Ellman's reagent. In addition to these major results, the cleavage site of the fibrillin-1 signal peptide and the N-terminal sequence of monomeric authentic fibrillin-1 from conditioned fibroblast medium were determined.

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Documento generato il 25/11/20 alle ore 07:06:48