Thromb Haemost 2005; 93(02): 192-198
DOI: 10.1160/TH04-09-0580
Theme Issue Article
Schattauer GmbH

Soluble and cleaved forms of the urokinase-receptor: degradation products or active molecules?

Nunzia Montuori
1   Istituto di Endocrinologia ed Oncologia Sperimentale (CNR) and Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università “Federico II”, Naples, Italy
,
Valeria Visconte
1   Istituto di Endocrinologia ed Oncologia Sperimentale (CNR) and Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università “Federico II”, Naples, Italy
,
Guido Rossi
1   Istituto di Endocrinologia ed Oncologia Sperimentale (CNR) and Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università “Federico II”, Naples, Italy
,
Pia Ragno
1   Istituto di Endocrinologia ed Oncologia Sperimentale (CNR) and Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università “Federico II”, Naples, Italy
› Author Affiliations
Further Information

Publication History

Received 09 September 2004

Accepted after revision 21 October 2004

Publication Date:
11 December 2017 (online)

Summary

The urokinase-mediated plasminogen activation (PA) system is involved in many physiological and pathological events that include cell migration and tissue remodelling, such as embryogenesis, ovulation, inflammation, wound healing, angiogenesis, and tumor invasion and metastasis. The urokinase receptor (uPAR) is a key molecule of this system and can bind extracellular and cell membrane molecules such as urokinase (uPA), vitronectin (VN), integrins and chemotaxis receptors. These multiple interactions can be modulated by the shedding or the cleavage of the cell membrane receptor. Indeed, cleaved forms of uPAR, lacking the N-terminal D1 domain, have been detected on the surface of cells and in tissues, while soluble forms have been found in biological fluids. Cleaved and soluble forms could represent the intermediary products of the uPAR metabolism or active molecules with precise and distinct functional roles. Here, we review the data concerning the in vitro and in vivo identification of these uPAR forms, their origin and functions, and the role that uPAR shedding and cleavage could play in biological processes.

 
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