Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression

Citation
Dp. Cerretti et al., Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression, BIOC BIOP R, 263(3), 1999, pp. 810-815
Citations number
35
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006291X → ACNP
Volume
263
Issue
3
Year of publication
1999
Pages
810 - 815
Database
ISI
SICI code
0006-291X(19991005)263:3<810:IOTNM(>2.0.ZU;2-2
Abstract
Metalloproteinase-disintegrins (ADAMs) are type 1 transmembrane proteins th at contain a unique domain structure including a zinc-binding metalloprotei nase domain, We have isolated cDNAs encoding two novel members of this fami ly, ADAM29 and ADAM30 which show testis-specific expression. Three forms of ADAM29 were found that encode proteins of 820, 786 and 767 amino acids. Al l of the amino acid differences are located in the cytoplasmic domain. Two forms of ADAM30 were isolated that encode proteins of 790 and 781 amino aci ds, with the difference in the coding region occurring in the cytoplasmic d omain. ADAM29 and ADAM30 map to human chromosome 4q34 and 1p11-13, respecti vely. An ancestral analysis of all known mammalian ADAMs indicates that the zinc-binding motif in the catalytic domain arose once in a common ancestor and was subsequently lost by those members lacking this motif. (C) 1999 Ac ademic Press.