Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution.

@article{Pends1997IdentificationAC,
  title={Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution.},
  author={Alberto M Pend{\'a}s and Vera Kn{\"a}uper and Xose S. Puente and Elena Baixeras Llano and Marie Genevi{\`e}ve Mattei and Shree Apte and Gillian A. Murphy and Carlos L{\'o}pez-Ot{\'i}n},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 7},
  pages={
          4281-6
        }
}
We have cloned a novel member of the matrix metalloproteinase (MMP) family of proteins from a human liver cDNA library. The isolated cDNA contains an open reading frame coding for a polypeptide of 508 amino acids, which has been tentatively called MMP-19. This protein exhibits the domain structure characteristic of previously described MMPs, including a signal sequence, a prodomain with the cysteine residue essential for maintaining the latency of these enzymes, an activation locus with the… CONTINUE READING
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