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MMP‐19: cellular localization of a novel metalloproteinase within normal breast tissue and mammary gland tumours
Author(s) -
Djonov Valentin,
Högger Katharina,
Sedlacek Radislav,
Laissue Jean,
Draeger Annette
Publication year - 2001
Publication title -
the journal of pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.964
H-Index - 184
eISSN - 1096-9896
pISSN - 0022-3417
DOI - 10.1002/path.927
Subject(s) - myoepithelial cell , matrix metalloproteinase , pathology , angiogenesis , extracellular matrix , metalloproteinase , biology , mammary gland , blood vessel , immunohistochemistry , matrix (chemical analysis) , chemistry , medicine , microbiology and biotechnology , breast cancer , cancer research , cancer , endocrinology , biochemistry , genetics , chromatography
Matrix metalloproteinases (MMPs) are instrumental in promoting and facilitating the spread of malignant diseases and in the de novo formation of blood vessels. This study has mapped the immunoreactivity of a novel, angiogenesis‐related metalloproteinase – MMP‐19 – in normal breast tissue and in benign and malignant breast lesions and compared this pattern of expression with that of MMP‐2. In the normal resting mammary gland, MMP‐19 was strongly expressed in the myoepithelial layer of the ductal system; the alveolar and ductal epithelia displayed considerable, but lobule‐specific, variations in labelling intensity. MMP‐19 was also present within the smooth muscle and endothelial layers of large and medium‐sized blood vessels, as well as within capillary walls. In benign lesions, all tumour cells and their surrounding vasculature were uniformly and strongly immunoreactive for MMP‐19. Progression towards an invasive phenotype and neoplastic dedifferentiation led to the disappearance of MMP‐19 from tumour cells and blood vessels and a concomitant rise in the levels of MMP‐2. In vitro experiments conducted with isolated smooth muscle cells cultivated on a solid substratum, or within the interstices of a collagen matrix, indicated that the expression of MMP‐19 is influenced by the architecture of the surrounding extracellular matrix. Copyright © 2001 John Wiley & Sons, Ltd.