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

Ian C. Scott, Ritva Halila, Joanne M. Jenkins, Sharon Mehan, Sinoula Apostolou, Robert Winqvist, David F. Callen, Darwin J. Prockop, Leena Peltonen, Karl E. Kadler

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

Abstract

The zincins are a superfamily of structurally-related Zn2+-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. The protein is found in placenta and cultured osteosarcoma cells. PRSM1 could share sequence homology with the type III procollagen N-proteinase. The prsm1 gene is represented once in the human genome and is localized on chromosome 16 (q24.3).

Original languageEnglish
Pages (from-to)135-143
Number of pages9
JournalGene
Volume174
Issue number1
DOIs
Publication statusPublished - 26 Sept 1996
Externally publishedYes

Keywords

  • Gluzincin
  • Immunoscreening
  • Metalloendopeptidase
  • Metalloproteinase
  • Metzincin
  • Primary structure
  • Recombinant protein
  • Type III collagen
  • Type III procollagen N-proteinase
  • Zincin

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