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Titolo:
AN ALTERNATIVE INSERT OF 3 AMINO-ACIDS IS INCORPORATED INTO COLLAGEN XIV IN A DEVELOPMENTALLY-REGULATED FASHION
Autore:
IMHOF M; TRUEB B;
Indirizzi:
UNIV BERN,ME MULLER INST BIOMECH,POB 30 CH-3010 BERN SWITZERLAND UNIV BERN,ME MULLER INST BIOMECH CH-3010 BERN SWITZERLAND
Titolo Testata:
FEBS letters
fascicolo: 3, volume: 438, anno: 1998,
pagine: 325 - 328
SICI:
0014-5793(1998)438:3<325:AAIO3A>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
FIBRIL-ASSOCIATED COLLAGENS; TISSUE-SPECIFIC EXPRESSION; VONWILLEBRAND-FACTOR; FIBRONECTIN; PROTEINS; MODULES; BINDING; UNDULIN; MEMBER; REGION;
Keywords:
ALTERNATIVE SPLICING; COLLAGEN XIV; EXTRACELLULAR MATRIX; FIBRONECTIN TYPE III REPEAT; FNIII MODULE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
M. Imhof e B. Trueb, "AN ALTERNATIVE INSERT OF 3 AMINO-ACIDS IS INCORPORATED INTO COLLAGEN XIV IN A DEVELOPMENTALLY-REGULATED FASHION", FEBS letters, 438(3), 1998, pp. 325-328

Abstract

We have identified a novel splice variant of chicken collagen XIV which contains an insert of three amino acids (Val-Arg-Thr) in the sixth fibronectin type III-like (FNIII) domain, The codons for these amino acids are inserted into the mRNA by skipping of a splice donor site andusage of another donor site 9 bp further downstream in the collagen XIV gene, The percentage of the new splice variant in the total collagen XIV mRNA varies between 22 and 46% in different embryonic tissues. After hatching, however, this percentage increases dramatically and reaches 86% in adult skeletal muscle and 58% in adult gizzard, indicatingdevelopmental regulation of this splicing event, Computer modeling suggests that the three extra amino acids cause an increase in the size of a flexible loop connecting two beta-strands in the sixth FNIII domain, This increase might affect the exact arrangement of the FNIII domain in the collagen XIV molecule, thereby modulating its interactions with other matrix molecules, (C) 1998 Federation of European Biochemical Societies.

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Documento generato il 27/11/20 alle ore 01:33:42