Molecular cloning, expression and chromosomal localization of a human gene encoding a 33 kDa putative metallopeptidase (PRSM1)

The zincins are a superfamily of structurally-related Zn 2+-binding metallopeptidases which play a major role in a wide range of biological processes including pattern formation, growth factor activation and extracellular matrix synthesis and degradation. In this paper we report the identification a...

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Veröffentlicht in:Gene 1996-09, Vol.174 (1), p.135-143
Hauptverfasser: Scott, Ian C., Halila, Ritva, Jenkins, Joanne M., Mehan, Sharon, Apostolou, Sinoula, Winqvist, Robert, Callen, David F., Prockop, Darwin J., Peltonen, Leena, Kadler, Karl E.
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Sprache:eng
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Zusammenfassung:The zincins are a superfamily of structurally-related Zn 2+-binding metallopeptidases which play a major role in a wide range of biological processes including pattern formation, growth factor activation and extracellular matrix synthesis and degradation. In this paper we report the identification and complete primary structure of a novel 33 kDa protein which contains the zinc-binding HEXXH motif found in the zincin superfamily. We have named this novel protein PRSM1 (PRoteaSe, Metallo, number 1). The gene was identified by the immunoscreening of a human placental cDNA library using polyclonal antibodies raised to the 70 kDa human matrix metalloendopeptidase, type III procollagen N-proteinase [Halila, R. and Peltonen, L. (1986) Purification of human procollagen type III N-proteinase from placenta and preparation of antiserum. Biochem. J. 239, 47–52]. The protein is found in placenta and cultured osteosarcoma cells. PRSM1 could share sequence homology with the type III procollagen N-proteinase. The prsml gene is represented once in the human genome and is localized on chromosome 16 (q24.3).
ISSN:0378-1119
1879-0038
DOI:10.1016/0378-1119(96)00510-0