000931602 000__ 03206cam\a2200493Ia\4500 000931602 001__ 931602 000931602 005__ 20230306151523.0 000931602 006__ m\\\\\o\\d\\\\\\\\ 000931602 007__ cr\un\nnnunnun 000931602 008__ 200418s2020\\\\sz\\\\\\o\\\\\001\0\eng\d 000931602 019__ $$a1150942683$$a1153307275 000931602 020__ $$a9783030345211$$q(electronic book) 000931602 020__ $$a3030345211$$q(electronic book) 000931602 020__ $$z9783030345204 000931602 020__ $$z3030345203 000931602 0247_ $$a10.1007/978-3-030-34521-1$$2doi 000931602 035__ $$aSP(OCoLC)on1151193777 000931602 035__ $$aSP(OCoLC)1151193777$$z(OCoLC)1150942683$$z(OCoLC)1153307275 000931602 040__ $$aEBLCP$$beng$$cEBLCP$$dGW5XE$$dEBLCP$$dYDX$$dUPM 000931602 049__ $$aISEA 000931602 050_4 $$aQP609.P78 000931602 08204 $$a572/.76$$223 000931602 24500 $$aHeparanase :$$bfrom basic research to clinical applications /$$cIsrael Vlodavsky, Ralph D. Sanderson, Neta Ilan, editors. 000931602 260__ $$aCham :$$bSpringer,$$c2020. 000931602 300__ $$a1 online resource (871 pages). 000931602 336__ $$atext$$btxt$$2rdacontent 000931602 337__ $$acomputer$$bc$$2rdamedia 000931602 338__ $$aonline resource$$bcr$$2rdacarrier 000931602 347__ $$atext file$$bPDF$$2rda 000931602 4901_ $$aAdvances in Experimental Medicine and Biology ;$$vv.1221 000931602 500__ $$aIncludes index. 000931602 506__ $$aAccess limited to authorized users. 000931602 520__ $$aProteases and their involvement in cancer progression have been well addressed and documented; however, the emerging premise presented within this book is that Heparanase is a master regulator of aggressive cancer phenotypes and crosstalk with the tumor microenvironment. This endoglycosidase contributes to tumor-mediated remodeling of the extracellular matrix and cell surfaces, augmenting the bioavailability of pro-tumorigenic and pro-inflammatory growth factors and cytokines that are bound to Heparan sulfate. Compelling evidence ties Heparanase with all steps of tumor progression including tumor initiation, growth, angiogenesis, metastasis, and chemoresistance, supporting the notion that Heparanase is an important contributor to the poor outcome of cancer patients and a validated target for therapy. Unlike Heparanase, heparanase-2, a close homolog of Heparanase, lacks enzymatic activity, inhibits Heparanase, and regulates selected genes that promote normal differentiation and tumor suppression. Written by internationally recognized leaders in Heparanase biology, this volume presents a comprehensive understanding of Heparanase's multifaceted activities in cancer, inflammation, diabetes and other diseases, as well as its related clinical applications to scientists, clinicians and advanced students in cell biology, tumor biology and oncology. 000931602 588__ $$aDescription based on print version record. 000931602 650_0 $$aProteolytic enzymes. 000931602 7001_ $$aVlodavsky, Israel. 000931602 7001_ $$aSanderson, Ralph D. 000931602 7001_ $$aIlan, Neta. 000931602 77608 $$iPrint version:$$aVlodavsky, Israel$$tHeparanase : From Basic Research to Clinical Applications$$dCham : Springer,c2020$$z9783030345204 000931602 830_0 $$aAdvances in experimental medicine and biology ;$$vv. 1221. 000931602 852__ $$bebk 000931602 85640 $$3SpringerLink$$uhttps://univsouthin.idm.oclc.org/login?url=http://link.springer.com/10.1007/978-3-030-34521-1$$zOnline Access$$91397441.1 000931602 909CO $$ooai:library.usi.edu:931602$$pGLOBAL_SET 000931602 980__ $$aEBOOK 000931602 980__ $$aBIB 000931602 982__ $$aEbook 000931602 983__ $$aOnline 000931602 994__ $$a92$$bISE