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Titolo:
Molecular remodeling of members of the relaxin family during primate evolution
Autore:
Klonisch, T; Froehlich, C; Tetens, F; Fischer, B; Hombach-Klonisch, S;
Indirizzi:
Univ Halle Wittenberg, Fac Med, Dept Anat & Cell Biol, D-06097 Halle, Germany Univ Halle Wittenberg Halle Germany D-06097 Biol, D-06097 Halle, Germany
Titolo Testata:
MOLECULAR BIOLOGY AND EVOLUTION
fascicolo: 3, volume: 18, anno: 2001,
pagine: 393 - 403
SICI:
0737-4038(200103)18:3<393:MROMOT>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEY I-L; RECEPTOR-BINDING SITE; INSULIN-LIKE PEPTIDE; REPRODUCTIVE TISSUES; CALLITHRIX-JACCHUS; GENE-EXPRESSION; MARMOSET MONKEY; ACID SEQUENCE; FACTOR RLF; LOCALIZATION;
Keywords:
relaxin; relaxin-like factor; RLF; INSL3; Strepsirrhini; lemuriformes;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
70
Recensione:
Indirizzi per estratti:
Indirizzo: Klonisch, T Univ Halle Wittenberg, Fac Med, Dept Anat & Cell Biol, Grosse Steinstr 52,D-06097 Halle, Germany Univ Halle Wittenberg Grosse Steinstr 52Halle Germany D-06097
Citazione:
T. Klonisch et al., "Molecular remodeling of members of the relaxin family during primate evolution", MOL BIOL EV, 18(3), 2001, pp. 393-403

Abstract

Employing comparative analysis of the cDNA-coding sequences of the unique preprorelaxin of the Afro-lorisiform Galago crassicaudatus and the Malagasylemur Varecia variegata and the relaxin-like factor (RLF) of G. crassicaudatus, we demonstrated distinct differences in the dynamics of molecular remodeling of both hormones during primate evolution. The lorisiform and lemuriform preprorelaxin sequences encoded identical hormones, providing the first endocrinological evidence for the monophyletic origin of all Strepsirrhini. Structural analysis revealed the lemuriform members of the relaxin family to be potentially bioactive single-gene products. In contrast to the "two-prong" relaxin receptor-binding motif (RELVR) present within the B-domains of other primate relaxins, strepsirrhine relaxin contained a unique "three-prong" motif (RRLIR) with highest sequence homology to the receptor-binding motif of the evolutionarily much older skate relaxin. In contrast to relaxin, the RLF molecule was highly conserved during primate evolution and contained within its B-domain the putative relaxin receptor-binding motif anda pentameric sequence implicated in binding to specific RLF receptors. Mutually exclusive expression of strepsirrhine preprorelaxin and RLF were observed in the fetal villous trophoblast cells of the strepsirrhine placenta and postpubertal testicular Leydig cells, respectively, reflecting distinct functional roles for both hormones within the reproductive tract of Strepsirrhini.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 15:12:19