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Titolo:
Nidogen is nonessential and not required for normal type IV collagen localization in Caenorhabditis elegans
Autore:
Kang, SH; Kramer, JM;
Indirizzi:
Northwestern Univ, Sch Med, Dept Cell & Mol Biol, Chicago, IL 60611 USA Northwestern Univ Chicago IL USA 60611 & Mol Biol, Chicago, IL 60611 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 11, volume: 11, anno: 2000,
pagine: 3911 - 3923
SICI:
1059-1524(200011)11:11<3911:NINANR>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
BASEMENT-MEMBRANE PROTEIN; HEPARAN-SULFATE PROTEOGLYCAN; GROWTH-FACTOR PRECURSOR; AMINO-ACID SEQUENCE; C-ELEGANS; EPITHELIAL MORPHOGENESIS; CELL-DIFFERENTIATION; BINDING-SITES; LAMININ; ENTACTIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Kramer, JM Northwestern Univ, Sch Med, Dept Cell & Mol Biol, Chicago, IL 60611 USA Northwestern Univ Chicago IL USA 60611 , Chicago, IL 60611 USA
Citazione:
S.H. Kang e J.M. Kramer, "Nidogen is nonessential and not required for normal type IV collagen localization in Caenorhabditis elegans", MOL BIOL CE, 11(11), 2000, pp. 3911-3923

Abstract

Nidogen (entactin) can form a ternary complex with type IV collagen and laminin and is thought to play a critical role in basement membrane assembly. We show that the Caenorhabditis elegans nidogen homologue nid-1 generates three isoforms that differ in numbers of rod domain endothelial growth factor repeats and are differentially expressed during development. NID-1 appears at the start of embryonic morphogenesis associated with muscle cells andsubsequently accumulates on pharyngeal, intestinal, and gonad primordia. In larvae and adults NID-1 is detected in most basement membranes but accumulates most strongly around the nerve ring and developing gonad. NID-1 is concentrated under dense bodies, at the edges of muscle quadrants, and on thesublateral nerves that run under muscles. Two deletions in nid-1 were isolated: cg119 is a molecular null, whereas cg118 produces truncated NID-1 missing the G2 collagen TV binding domain. Neither deletion causes overt abnormal phenotypes, except for mildly reduced fecundity. Truncated cg118 NID-1 shows wild-type localization, demonstrating that the G2 domain is not necessary for nidogen assembly. Both nid-1 mutants assemble type IV collagen in a completely wild-type pattern, demonstrating that nidogen is not essentialfor type IV collagen assembly into basement membranes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:38:31