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Papers In Press, published online ahead of print June 18, 2002
J. Biol. Chem, 10.1074/jbc.M204708200
Submitted on May 14, 2002
Revised on June 5, 2002
Accepted on June 18, 2002

Interaction of human breast fibroblasts with collagen I increases secretion of procathepsin B

Jennifer E. Koblinski, Julie Dosescu, Mansoureh Sameni, Kamiar Moin, Katherine Clark, and Bonnie F. Sloane

Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201

Corresponding Author: bsloane{at}med.wayne.edu

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 alpha 1, alpha 2, and beta 1 integrin subunits prevented procathepsin B secretion from fibroblasts grown on collagen. In addition, procathepsin B secretion was induced when cells were plated on beta 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.


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