Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ

Gene. 1996 Dec 12;183(1-2):123-8. doi: 10.1016/s0378-1119(96)00525-2.


A cDNA encoding a novel matrix metalloproteinase (MMP) was isolated from a porcine enamel organ-specific cDNA library. Multiple tissue northern blot analysis revealed the presence of two mRNA transcripts which were expressed only in the enamel organ. The transcripts were 1968 bp or 3420 bp in length and resulted from the utilization of alternative polyadenylation sites. The open reading frame of the cloned mRNA encodes a protein composed of 483 amino acids. The MMP has a predicted molecular mass of 54.1 kDa, which is similar to that of the stromelysins or collagenases, although it is not a member of either of these two classes of MMPs. A motif analysis revealed that the cloned MMP does not contain a consensus hemopexin-like domain because it lacks a critical tryptophan and proline residue at the appropriate positions. Since the cloned MMP is a new member of the MMP gene family and its expression appears limited to the enamel organ, we have named it enamelysin.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary / analysis
  • Enamel Organ / enzymology*
  • Gene Expression Regulation, Developmental / physiology*
  • Gene Expression Regulation, Enzymologic / physiology
  • Genes / genetics
  • Hemopexin / genetics
  • Matrix Metalloproteinase 20
  • Matrix Metalloproteinases*
  • Metalloendopeptidases / genetics*
  • Molecular Sequence Data
  • Open Reading Frames / genetics
  • Organ Specificity
  • Poly A
  • RNA, Messenger / analysis*
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Swine


  • DNA, Complementary
  • RNA, Messenger
  • Poly A
  • Hemopexin
  • Matrix Metalloproteinase 20
  • Matrix Metalloproteinases
  • Metalloendopeptidases

Associated data

  • GENBANK/U54825