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Leksa, V.* ; Schiller, H. B. ; Stockinger, H.*

Biotin-chasing assay to evaluate uPAR stability and cleavage on the surface of cells.

Berlin [u.a.]: Springer, 2018. 39-47 ( ; 1731)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The plasminogen activation system, i.e., the fibrinolytic system, is one of the major plasma proteolytic pathways. The proteolytic conversion of the zymogen plasminogen to the active serine protease plasmin is on the cell surface catalyzed by the serine protease urokinase-type plasminogen activator (urokinase, uPA). Upon binding to the urokinase receptor (uPAR, CD87), single-chain pro-uPA is processed to double-chain uPA which in turn specifically converts cell-bound plasminogen to plasmin. Plasmin is harnessed in many physiological processes, e.g., blood clots’ resolution, or proteolytic activation of growth factors. Plasmin is essential also for migratory cells, for instance, activated immune cells; however, malignant cells hijack plasmin for invasion as well. The activation of plasminogen to plasmin is thus at the physiological level tightly controlled. One of the negative regulators of plasminogen activation has been identified in the cation-independent mannose 6-phosphate/insulin-like growth factor 2 receptor (M6P/IGF2R, CIMPR, CD222). M6P/IGF2R is a multifunctional receptor involved in protein sorting, internalization, and degradation, being considered a tumor suppressor. M6P/IGF2R binds both plasminogen and uPAR and facilitates in this way the proteolytic cleavage of uPAR resulting in the loss of the uPA binding on the cell surface. Hence, this molecular device contributes to the negative feedback loop in regulation of pericellular plasminogen activation and cell invasion. In this chapter, we describe the experimental approach, i.e., biotin-chasing assay, to evaluate uPAR stability and cleavage on the surface of cells.
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Publikationstyp Buch: Sammelband
Schlagwörter Cell Migration ; Fibrinolysis ; Pericellular Proteolysis ; Plasminogen ; Urokinase
Sprache
Veröffentlichungsjahr 2018
HGF-Berichtsjahr 2018
ISSN (print) / ISBN 1064-3745
e-ISSN 1940-6029
Zeitschrift Methods in Molecular Biology
Quellenangaben Band: 1731, Heft: , Seiten: 39-47 Artikelnummer: , Supplement: ,
Verlag Springer
Verlagsort Berlin [u.a.]
Begutachtungsstatus Peer reviewed
Institut(e) German Center for Lung Research (DZL)
POF Topic(s) 80000 - German Center for Lung Research
Forschungsfeld(er) Lung Research
PSP-Element(e) G-501800-810
DOI 10.1007/978-1-4939-7595-2_4
Scopus ID 85040525648
PubMed ID 29318541
Erfassungsdatum 2018-02-08
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