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Titolo:
Mouse ten-m/odz is a new family of dimeric type II transmembrane proteins expressed in many tissues
Autore:
Oohashi, T; Zhou, XH; Feng, K; Richter, B; Morgelin, M; Perez, MT; Su, WD; Chiquet-Ehrismann, R; Rauch, U; Fassler, R;
Indirizzi:
Univ Lund, Dept Expt Pathol, S-22185 Lund, Sweden Univ Lund Lund Sweden S-22185 nd, Dept Expt Pathol, S-22185 Lund, Sweden Univ Lund, Dept Ophthalmol, S-22185 Lund, Sweden Univ Lund Lund Sweden S-22185 und, Dept Ophthalmol, S-22185 Lund, Sweden Friedrich Miescher Inst, CH-4058 Basel, Switzerland Friedrich Miescher Inst Basel Switzerland CH-4058 058 Basel, Switzerland Max Planck Inst Biochem, D-82152 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82152 Martinsried, Germany Okayama Univ, Sch Med, Dept Mol Biol & Biochem, Okayama 700, Japan OkayamaUniv Okayama Japan 700 pt Mol Biol & Biochem, Okayama 700, Japan
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 3, volume: 145, anno: 1999,
pagine: 563 - 577
SICI:
0021-9525(19990503)145:3<563:MTIANF>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
PAIR-RULE GENE; EXTRACELLULAR-MATRIX PROTEINS; ODD OZ; DROSOPHILA; IDENTIFICATION; INTEGRINS; FRAGMENTS; SEQUENCE; TENASCIN; ADHESION;
Keywords:
ten-m/odz; transmembrane protein; pair rule; epidermal growth factor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Fassler, R Univ Lund, Dept Expt Pathol, S-22185 Lund, Sweden Univ Lund Lund Sweden S-22185 pt Pathol, S-22185 Lund, Sweden
Citazione:
T. Oohashi et al., "Mouse ten-m/odz is a new family of dimeric type II transmembrane proteins expressed in many tissues", J CELL BIOL, 145(3), 1999, pp. 563-577

Abstract

The Drosophila gene ten-m/odz is the only pair rule gene identified to date which is not a transcription factor, In an attempt to analyze the structure and the function of ten-m/odz in mouse, we isolated four murine ten-m cDNAs which code for proteins of 2,700-2,800 amino acids. All four proteins (Ten-m1-4) lack signal peptides at the NH2 terminus, but contain a short hydrophobic domain characteristic of transmembrane proteins, 300-400 amino acids after the NH2 terminus. About 200 amino acids COOH-terminal to this hydrophobic region are eight consecutive EGF-like domains. Cell transfection, biochemical, and electronmicroscopic studies suggest that Ten-mi is a dimeric type II transmembrane protein. Expression of fusion proteins composed of the NH2-terminal and hydrophobic domain of ten-mi attached to the alkaline phosphatase reporter gene resulted in membrane-associated staining of the alkaline phosphatase. Electronmicroscopic and electrophoretic analysis of a secreted form of the extracellular domain of Ten-mi showed that Ten-mi is a disulfide-linked dimer and that the dimerization is mediated by EGF-like modules 2 and 5 which contain an odd number of cysteines. Northern blot and immunohistochemical analyses revealed widespread expression of mouse ten-m genes, with most prominent expression in brain. All fourten-m genes can be expressed in variously spliced mRNA isoforms, The extracellular domain of Ten-mi fused to an alkaline phosphatase reporter bound to specific regions in many tissues which were partially overlapping with the Ten-mi immunostaining. Far Western assays and electronmicroscopy demonstrated that Ten-mi can bind to itself.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 15:52:32