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Research Article Free access | 10.1172/JCI115104

Sites of synthesis of urokinase and tissue-type plasminogen activators in the murine kidney.

A P Sappino, J Huarte, J D Vassalli, and D Belin

Division of Onco-Haematology, University of Geneva Medical School, Switzerland.

Find articles by Sappino, A. in: PubMed | Google Scholar

Division of Onco-Haematology, University of Geneva Medical School, Switzerland.

Find articles by Huarte, J. in: PubMed | Google Scholar

Division of Onco-Haematology, University of Geneva Medical School, Switzerland.

Find articles by Vassalli, J. in: PubMed | Google Scholar

Division of Onco-Haematology, University of Geneva Medical School, Switzerland.

Find articles by Belin, D. in: PubMed | Google Scholar

Published March 1, 1991 - More info

Published in Volume 87, Issue 3 on March 1, 1991
J Clin Invest. 1991;87(3):962–970. https://doi.org/10.1172/JCI115104.
© 1991 The American Society for Clinical Investigation
Published March 1, 1991 - Version history
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Abstract

Kidneys have long been recognized as a major source of plasminogen activators (PAs). However, neither the sites of synthesis of the enzymes nor their role in renal function have been elucidated. By the combined use of zymographies on tissue sections and in situ hybridizations, we have explored the cellular distribution of urokinase-type (u-PA) and tissue-type (t-PA) plasminogen activators and of their mRNAs in developing and adult mouse kidneys. In 17.5-d old embryos, renal tubules synthesize u-PA, while S-shaped bodies produce t-PA. In the adult kidney, u-PA is synthesized and released in urine by the epithelial cells lining the straight parts of both proximal and distal tubules. In contrast, t-PA is produced by glomerular cells and by epithelial cells lining the distal part of collecting ducts. The precise segmental distribution of PAs suggests that both enzymes may be implicated in the maintenance of tubular patency, by catalyzing extracellular proteolysis to prevent or circumvent protein precipitation.

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