Results 71 to 80 of about 11,910 (223)

Heparanase in Acute Kidney Injury [PDF]

, 2020
Recent years have brought about fledgling realization of the role played by heparanase in the pathogenesis of diverse diseases including kidney diseases and, specifically, acute kidney injury. Human heparanase-1 is critically and uniquely engaged in cleavage of heparan sulfate, an integral part of glycocalyx and extracellular matrix where it harbors ...
Zaid, Abassi, M S, Goligorsky
openaire   +2 more sources

Increased chemotactic migration and growth in heparanase-overexpressing human U251n glioma cells

Journal of Experimental & Clinical Cancer Research, 2008
Heparanase is an endoglycosidase that degrades heparan sulfate, the main polysaccharide constituent of the extracellular matrix (ECM) and basement membrane.
Zheng Xuguang, Zhang Xuepeng, Zhang Zheng, Kalkanis Steven N, Jiang Feng, Hong Xin, Jiang Hao, Mikkelsen Tom, Chopp Michael   +8 more
doaj   +1 more source

Syndecan-3 is selectively pro-inflammatory in the joint and contributes to antigen-induced arthritis in mice [PDF]

, 2014
INTRODUCTION: Syndecans are heparan sulphate proteoglycans expressed by endothelial cells. Syndecan-3 is expressed by synovial endothelial cells of rheumatoid arthritis (RA) patients where it binds chemokines, suggesting a role in leukocyte trafficking ...
Boyes, C, Eustace, A, Kalia, N, Kehoe, O, King, S, Middleton, J, Patterson, A, Reizes, O, Williams, A   +8 more
core   +4 more sources

Pushing Frontiers for Proteoglycans

Proteoglycan Research, Volume 4, Issue 2, April 2026.
ABSTRACT Almost half of proteins have one or more post‐translational glycosylation modifications involving the addition of glycan structures. Proteoglycans are a class of glycosylated proteins with one or more glycosaminoglycan (GAG) chains covalently attached to the core protein.
Marissa L. Maciej‐Hulme
wiley   +1 more source

Enzymatic Remodelling of Tumour Microenvironment Enhances Anti‐CEACAM5 CAR T‐Cell Efficacy Against Colorectal Cancer

Advanced Science, Volume 13, Issue 13, 3 March 2026.
This study shows anti‐CEACAM5 CAR T‐cells are ineffective against colorectal cancer (CRC) because of CEACAM5 sequestration at intercellular junctions and the thick tumour cell glycocalyx. Enzymatic treatments of CRC cell monolayer/tissue section with trypsin or hyaluronidase restore CEACAM5 availability, enhance CAR T‐cell activation, increase ...
Debasis Banik, Christopher J. Ward, Soura Chakraborty, Ziwei Zhang, Daniel Heraghty, Prasanna Suresh, Bing Li, Shekhar Kedia, Jhuma Pramanik, Simon J. Davis, James P. Roy, Michael A. Chapman, Bidesh Mahata, David Klenerman   +13 more
wiley   +1 more source

Leukocyte Heparanase: A Double-Edged Sword in Tumor Progression

Frontiers in Oncology, 2019
Heparanase is a β-D-endoglucuronidase that cleaves heparan sulfate, a complex glycosaminoglycan found ubiquitously throughout mammalian cells and tissues.
Alyce J. Mayfosh, Nikola Baschuk, Nikola Baschuk, Mark D. Hulett   +3 more
doaj   +1 more source

The anticancer activity of lytic peptides is inhibited by heparan sulfate on the surface of the tumor cells [PDF]

, 2009
Background Cationic antimicrobial peptides (CAPs) with antitumor activity constitute a promising group of novel anticancer agents. These peptides induce lysis of cancer cells through interactions with the plasma membrane.
Bodil Fadnes, Øystein Rekdal, Lars Uhlin-Hansen, HG Boman, D Hultmark, B Cornet, ZQ Li, B Bechinger, IV Polozov, LT Eliassen, LT Eliassen, N Papo, Y Chen, SR Dennison, JS Mader, SA Johnstone, RA Cruciani, Y Ohsaki, S Kim, K Matsuzaki, Y Pouny, Z Oren, HM Ellerby, MR Yeaman, T Utsugi, CD Bucana, M Sugimura, LV Rao, YJ Kim, DH Dube, L Kjellen, K Sugahara, E Tkachenko, DL Rabenstein, F Zsila, J Kleeff, K Matsuda, RD Sanderson, GC Jayson, F Safaiyan, JS Mader, YC Yoo, H Jenssen, JD Esko, X Bai, LT Eliassen, KM Keller, M Yanagishita, JE Shively, H Greve, L Uhlin-Hansen, SE Stringer, A Risso, H Schroder-Borm, CD Klaassen, F Safaiyan, L Zhang, TF Smetsers, A Molist, GH Guibinga, M Ueda, M Bernfield, LA Fransson, S Tumova, SG Rees, A Schmidtchen, W Baranska-Rybak, A Schmidtchen, H Jenssen, JH Andersen, A Roseanu, S Ashikari-Hada, Y Yuguchi, M Kusche, Y Mahalingam, M Rintala, K Harada, H Kurokawa, K Bame, N Ilan   +79 more
core   +3 more sources

Extramedullary Disease—Achilles Heel in Myeloma?

American Journal of Hematology, Volume 101, Issue 3, Page 521-536, March 2026.
ABSTRACT Despite advances in therapy, extramedullary disease (EMD) remains an aggressive form of multiple myeloma associated with poor outcomes. Patients with true EMD, in which plasmacytomas have become completely independent of bone, have a particularly poor prognosis. The pathogenesis of EMD is driven by complex mechanisms involving loss of adhesion
Shaji Kumar, Joshua Richter, Saad Z. Usmani, Yael C. Cohen, Jing Christine Ye, María‐Victoria Mateos, Vania Hungria, Elena Zamagni   +7 more
wiley   +1 more source

Heparanase Involvement in Exosome Formation [PDF]

, 2020
Exosomes are secreted vesicles involved in signaling processes. The biogenesis of a class of these extracellular vesicles depends on syntenin, and on the interaction of this cytosolic protein with syndecans. Heparanase, largely an endosomal enzyme, acts as a regulator of the syndecan-syntenin-exosome biogenesis pathway. The upregulation of syntenin and
David, Guido, Zimmermann, Pascale
openaire   +3 more sources

Heparanase Localization and Expression by Head and Neck Cancer: Correlation with Tumor Progression and Patient Survival

Neoplasia: An International Journal for Oncology Research, 2006
Heparanase is an endoglycosidase that specifically cleaves heparan sulfate (HS) side chains of HS proteoglycans, the major proteoglycans in the extracellular matrix and cell surfaces. Traditionally, heparanase activity was implicated in cellular invasion
Ilana Doweck, Victoria Kaplan-Cohen, Inna Naroditsky, Edmond Sabo, Neta Ilan, Israel Vlodavsky   +5 more
doaj   +1 more source