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Titolo:
CALCIUM DETERMINES THE SHAPE OF FIBRILLIN
Autore:
REINHARDT DP; MECHLING DE; BOSWELL BA; KEENE DR; SAKAI LY; BACHINGER HP;
Indirizzi:
SHRINERS HOSP CHILDREN,RES UNIT,3101 SW SAM JACKSON PK RD PORTLAND OR97201 OREGON HLTH SCI UNIV,DEPT BIOCHEM & MOL BIOL PORTLAND OR 97201
Titolo Testata:
The Journal of biological chemistry
fascicolo: 11, volume: 272, anno: 1997,
pagine: 7368 - 7373
SICI:
0021-9258(1997)272:11<7368:CDTSOF>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
COAGULATION FACTOR-X; FACTOR-LIKE DOMAINS; EGF-LIKE DOMAINS; HUMAN FACTOR-IX; MARFAN-SYNDROME; EXTRACELLULAR-MATRIX; 3-DIMENSIONAL STRUCTURE; BLOOD-COAGULATION; GENE-PRODUCT; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
D.P. Reinhardt et al., "CALCIUM DETERMINES THE SHAPE OF FIBRILLIN", The Journal of biological chemistry, 272(11), 1997, pp. 7368-7373

Abstract

Velocity sedimentation experiments using authentic fibrillin-1 demonstrated sedimentation coefficients of s(20,w)(0) = 5.1 +/- 0.1 in the Ca2+ form and s(20,w)(0) = 6.2 +/- 0.1 in the Ca2+-free form. Calculations based on these results and the corresponding molecular mass predicted a shortening of fibrillin by similar to 25% and an increase in width of similar to 13-17% upon removal of Ca2+, These observations were confirmed by analysis of Ca2+-loaded and Ca2+-free rotary shadowed fibrillin molecules. Analysis of recombinant fibrillin-1 subdomain rF17, consisting primarily of an array of 12 Ca2+-binding epidermal growth factor (cbEGF)-like repeats, by analytical ultracentrifugation and rotary shadowing further confirmed Ca2+-dependent structural changes in the tertiary structure of fibrillin-1. Based on these results, the contribution of a single cbEGF-like repeat to the length of tandem arrays is predicted to be similar to 3 nm in the Ca2+ form, Ca2+-free forms demonstrated a decrease of 20-30% in length, indicating significant structural changes of these motifs when they occur in tandem, Circular dichroism measurements of rF17 in the presence and absence of Ca2+ indicated secondary structural changes within and adjacent to the interdomain regions that connect cbEGF-like repeats. The results presented here suggest a flexible structure for the Ca2+-free form of fibrillin whichbecomes stabilized, more extended, and rigid in the Ca2+ form.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 07:28:31