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J. Biol. Chem., Vol. 277, Issue 35, 32220-32227, August 30, 2002
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From the Interactions of stromal and tumor cells with the
extracellular matrix may regulate expression of proteases including the
lysosomal proteases cathepsins B and D. In the present study, we
determined whether the expression of these two proteases in human
breast fibroblasts was modulated by interactions with the extracellular matrix component, collagen I. Breast fibroblasts were isolated from
non-malignant breast tissue as well as from tissue surrounding malignant human breast tumors. Growth of these fibroblasts on collagen
I gels affected cell morphology, but not the intracellular localization
of vesicles staining for cathepsin B or D. Cathepsins B and D levels
(mRNA or intracellular protein) were not affected in fibroblasts
growing on collagen I gels or plastic, nor was cathepsin D secreted
from these cells. In contrast, protein expression and secretion of
cathepsin B, primarily procathepsin B, was induced by growth on
collagen I gels. The induced secretion appeared to be mediated by
integrins binding to collagen I, as inhibitory antibodies against
Interaction of Human Breast Fibroblasts with Collagen I
Increases Secretion of Procathepsin B*
§,
, and¶**
Barbara Ann Karmanos Cancer Institute and
¶ Department of Pharmacology, Wayne State University, School
of Medicine, Detroit, Michigan 48201 and the Craniofacial
Developmental Biology and Regeneration Branch, NIDCR, National
Institutes of Health, Bethesda, Maryland 20892
1, 2, and 
1 integrin
subunits prevented procathepsin B secretion from fibroblasts grown on
collagen. In addition, procathepsin B secretion was induced when cells
were plated on 1 integrin antibodies. To our knowledge,
this is the first examination of cathepsin B and D expression and
localization in human breast fibroblasts and their regulation by a
matrix protein. Secretion of the cysteine protease procathepsin B from
breast fibroblasts may have physiological and pathological
consequences, as proteases are required for normal development
and for lactation of the mammary gland, yet can also initiate and
accelerate the progression of breast cancer.
*
This work was supported by United States Public Health
Service Grants CA36481 and CA56586. The Zeiss LSM-310 confocal
microscope was supported in part by National Institutes of Health NIEHS
Grant P30ES06639 and NCI Grant P30CA22453. The Barbara Ann Karmanos Cancer Institute Comprehensive Cancer Center Cell Resources and the
Flow Cytometry cores were supported by National Institutes of Health
NCI Grant P30CA22453.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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