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Matrilysin Expression in the Involuting Rat Ventral Prostate
Author(s) -
Powell William C.,
Domann Frederick E.,
Mitchen Joan M.,
Matrisian Lynn M.,
Nagle Raymond B.,
Tim Bowden G.
Publication year - 1996
Publication title -
the prostate
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.295
H-Index - 123
eISSN - 1097-0045
pISSN - 0270-4137
DOI - 10.1002/1097-0045(199609)29:3<159::aid-pros2990290304>3.0.co;2-l
Subject(s) - prostate , matrilysin , medicine , prostate disease , prostate cancer , endocrinology , immunohistochemistry , biology , pathology , cancer
Matrilysin (PUMP‐1) is a member of the matrix metalloproteinase (MMP) family of extracellular matrix degrading enzymes that has been found to be overexpressed in human prostate cancer. The rat ventral prostate (RVP) following castration has been used as a model for both tissue involution and apoptosis. Northern analysis and in situ hybridization were used to determine the time course and localization of matrilysin during 8 days of RVP involution. Northern analysis revealed that the 1.2 kb matrilysin mRNA was undetectable in normal RVP. An increase in the steady‐state levels of matrilysin mRNA was observed 5 days after castration, and the levels began to decline by 8 days after castration. The mRNAs for tissue inhibitor of metalloproteinase‐1 and urokinase‐type plasminogen activator also showed a time‐dependent induction during the course of involution. Localization of matrilysin by in situ hybridization indicated that the mRNA was produced by epithelial cells of the involuting RVP. The matrilysin message was observed in a small number of glands within the whole RVP. Matrilysin protein was present in the RVP and peaked 3 days after castration. The combination of proteinase genes expressed in the RVP following castration indicate that the Mh4P and serine protease families of enzymes may interact during tissue remodeling of the RVP following castration. © 1996 Wiley‐Liss, Inc.