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Published 20 June 2005. doi:10.1083/jcb.200411153
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 6, 977-985
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Article

Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy



Alejandro C. Curino1, Lars H. Engelholm4, Susan S. Yamada3, Kenn Holmbeck3, Leif R. Lund4, Alfredo A. Molinolo2, Niels Behrendt4, Boye Schnack Nielsen4, and Thomas H. Bugge1

1 Proteases and Tissue Remodeling Unit, Oral and Pharyngeal Cancer Branch
2 Molecular Carcinogenesis Unit, Oral and Pharyngeal Cancer Branch
3 Matrix Metalloproteinase Unit, Craniofacial and Skeletal Diseases Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892
4 Finsen Laboratory, Rigshospitalet, DK-2100 Copenhagen Ø, Denmark

Correspondence to Thomas H. Bugge: thomas.bugge{at}nih.gov

We recently reported that uPARAP/Endo180 can mediate the cellular uptake and lysosomal degradation of collagen by cultured fibroblasts. Here, we show that uPARAP/Endo180 has a key role in the degradation of collagen during mammary carcinoma progression. In the normal murine mammary gland, uPARAP/Endo180 is widely expressed in periductal fibroblast-like mesenchymal cells that line mammary epithelial cells. This pattern of uPARAP/Endo180 expression is preserved during polyomavirus middle T–induced mammary carcinogenesis, with strong uPARAP/Endo180 expression by mesenchymal cells embedded within the collagenous stroma surrounding nests of uPARAP/Endo180-negative tumor cells. Genetic ablation of uPARAP/Endo180 impaired collagen turnover that is critical to tumor expansion, as evidenced by the abrogation of cellular collagen uptake, tumor fibrosis, and blunted tumor growth. These studies identify uPARAP/Endo180 as a key mediator of collagen turnover in a pathophysiological context.

Abbreviation used in this paper: PymT; polyomavirus middle T.


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