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Titolo:
FIBRILLIN-1 - ORGANIZATION IN MICROFIBRILS AND STRUCTURAL-PROPERTIES
Autore:
REINHARDT DP; KEENE DR; CORSON GM; POSCHL E; BACHINGER HP; GAMBEE JE; SAKAI LY;
Indirizzi:
SHRINERS HOSP CRIPPLED CHILDRENS,RES DEPT PORTLAND OR 97201 SHRINERS HOSP CRIPPLED CHILDRENS,RES DEPT PORTLAND OR 97201 UNIV ERLANGEN NURNBERG,INST EXPTL MED D-91054 ERLANGEN GERMANY
Titolo Testata:
Journal of Molecular Biology
fascicolo: 1, volume: 258, anno: 1996,
pagine: 104 - 116
SICI:
0022-2836(1996)258:1<104:F-OIMA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
CONNECTIVE-TISSUE MICROFIBRILS; MARFAN-SYNDROME; CALCIUM-BINDING; SEQUENCE; DOMAINS; EGF; COMPONENT; COLLAGEN; LAMININ; LINKAGE;
Keywords:
ASSEMBLY; ELECTRON MICROSCOPY; EUKARYOTIC EXPRESSION; FIBRILLIN; MICROFIBRIL ORGANIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
D.P. Reinhardt et al., "FIBRILLIN-1 - ORGANIZATION IN MICROFIBRILS AND STRUCTURAL-PROPERTIES", Journal of Molecular Biology, 258(1), 1996, pp. 104-116

Abstract

To investigate the microfibrillar organization and structural properties of fibrillin-1, we produced overlapping recombinant peptides in human cells which altogether span the fibrillin-1 molecule. The peptideswere purified under non-denaturing conditions and extensive characterization indicated correct folding. The purified proteins were used to map monoclonal antibodies 26, 69 and 201. The binding sites are located at the N-terminal end between amino acid residues 45 and 450 (mAb 26), 451 and 909 (mAb 201) and at the C-terminal end between residues 2093 and 2871 (mAb 69). Immunolocalization of these antibodies to extended beaded structures (microfibrils) demonstrated that the N- and C-terminal ends of fibrillin-1 are located in proximity and on opposite sides of the beads, and more central parts of the molecule are located between the beads. Each epitope is present once between each bead. Thesedata allow two possible models for the organization of fibrillin in microfibrils. However, comparison of distances between antibody bindingsites on the recombinant peptides and labeling events in tissue suggests that fibrillin molecules are compacted within their tissue form asmicrofibrils. Additional analyses of the recombinant peptides providenew information regarding the eight-cysteine motif, a novel domain present in fibirillins and TGFP binding proteins, and suggest that fibrillins are processed at their N- and C-terminal ends. (C) 1996 AcademicPress Limited

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 07:39:22