Cancer Letters

Cancer Letters

Volume 107, Issue 1, 1 October 1996, Pages 5-10
Cancer Letters

Matrilysin is associated with progression of colorectal tumor

https://doi.org/10.1016/0304-3835(96)04336-4Get rights and content

Abstract

Matrilysin and gelatinase A, B mRNA expressions were examined in colorectal tumors. Matrilysin mRNA was observed exclusively in tumors, while the others were also found in normal mucosa surrounding tumors. Further analysis revealed that colorectal adenomas with severe dysplasia, not with mild dysplasia, expressed matrilysin with lower levels than cancers. The level of matrilysin mRNA expression increased with the advancement of stages of colorectal cancers, consequently a relatively higher expression was observed in liver metastatic tumors than primary tumors. These results suggest that matrilysin mRNA expression was correlated with the progression of colorectal tumors, and this enzyme may also play a role in developing metastatic tumors in liver.

References (19)

  • U.I. Sires et al.

    Degradation of entactin by matrix metalloproteinase. Susceptibility to matrilysin and identification of cleavage sites

    J. Biol. Chem.

    (1993)
  • T. Ishikawa et al.

    Construction of cDNA bank; synthesis, storage on the plastic plates and repeated synthesis of cDNA from endoscopic biopsies and surgical specimens

    Gastoenterology

    (1994)
  • R.E. Galardy et al.

    Inhibition of angiogenesis by the matrix metalloprotease inhibitor N-[2R-2-(hydroxamidocarbonymethy)-4-methypentanoyl)]-l-tryptophan methylamide

    Cancer Res.

    (1994)
  • L.M. Matrisian

    The matrix-degrading metalloproteinases

    Bioassays

    (1992)
  • M. Mitsuhashi et al.

    Gene manipulation on plastic plates

    Nature

    (1992)
  • M. Mitsuhashi et al.

    Oligonucleotide probe design—a new approach

    Nature

    (1994)
  • K. Miyazaki et al.

    Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (PUMP-1), secreted from human rectal carcinoma cell line

    Cancer Res.

    (1990)
  • M. Mori et al.

    Overexpression of matrix metalloproteinase-7 mRNA in human colon carcinomas

    Cancer Suppl.

    (1995)
  • M.A. Moses et al.

    A metalloproteinase inhibitor as an inhibitor of neovascularization

    J. Cell. Biochem.

    (1991)
There are more references available in the full text version of this article.

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