Results 11 to 20 of about 7,996 (174)

Leukocyte Heparanase: A Double-Edged Sword in Tumor Progression

open access: yesFrontiers 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   +3 more
doaj   +2 more sources

Heparanase and the hallmarks of cancer

open access: yesJournal of Translational Medicine, 2020
Heparanase is the only mammalian enzyme that cleaves heparan sulphate, an important component of the extracellular matrix. This leads to the remodelling of the extracellular matrix, whilst liberating growth factors and cytokines bound to heparan sulphate.
Krishnath M. Jayatilleke, Mark D. Hulett
doaj   +2 more sources

Newly generated heparanase knock-out mice unravel co-regulation of heparanase and matrix metalloproteinases.

open access: yesPLoS ONE, 2009
BackgroundHeparanase, a mammalian endo-beta-D-glucuronidase, specifically degrades heparan sulfate proteoglycans ubiquitously associated with the cell surface and extracellular matrix.
Eyal Zcharia   +7 more
doaj   +2 more sources

Structural insights into pixatimod (PG545) inhibition of heparanase, a key enzyme in cancer and viral infections [PDF]

open access: yes, 2022
Pixatimod (PG545), a heparan sulfate (HS) mimetic and anticancer agent currently in clinical trials, is a potent inhibitor of heparanase. Heparanase is an endo‐β‐glucuronidase that degrades HS in the extracellular matrix and basement membranes and is ...
Neha S. Gandhi   +14 more
core   +1 more source

Mechanisms and integrative machine learning approaches to blood-brain barrier biomarker profiling for personalized ischemic stroke management. [PDF]

open access: yesPhysiol Rep
Abstract Ischemic stroke remains a leading cause of death and disability worldwide, with blood–brain barrier (BBB) disruption playing a central role in vasogenic edema, neuroinflammation, hemorrhagic transformation, and secondary neuronal injury. The BBB is a specialized neurovascular unit composed of endothelial tight junctions, pericytes, astrocytes,
Nzobokela J   +4 more
europepmc   +2 more sources

Accumulation of Ym1 and formation of intracellular crystalline bodies in alveolar macrophages lacking heparanase [PDF]

open access: yes, 2010
Heparanase is a heparan sulfate (HS) degrading endoglucuronidase that has been implicated in cell migration and inflammatory conditions. Here we used mice deficient of heparanase (Hpse−/−) to study the impact of heparanase on airway leukocytes.
Vlodavsky, Israel   +12 more
core   +1 more source

A Fluorogenic Heparan Sulfate Disaccharide for the Measurement of Heparanase Activity [PDF]

open access: yes, 2020
The endo-β-glucuronidase heparanase mediates mammalian heparan sulfate catabolism, and is of considerable medical interest due to its prominent role in cancer aggression and metastasis.
Vito, Ferro   +3 more
core   +2 more sources

Evidence for a genetic basis of urogenital carcinoma in the wild California sea lion [PDF]

open access: yes, 2014
This work was funded by a grant from the US National Marine Fisheries Service John H. Prescott Marine Mammal Rescue Assistance grant programme, and H.M.B. was funded by a UK Natural Environment Research Council PhD studentship. J.A.H.
Dagleish, Mark P.   +8 more
core   +1 more source

Heparinase selectively sheds heparan sulphate from the endothelial glycocalyx [PDF]

open access: yes, 2008
A healthy vascular endothelium is coated by the endothelial glycocalyx. Its main constituents are transmembrane syndecans and bound heparan sulphates. This structure maintains the physiological endothelial permeability barrier and prevents leukocyte and ...
Rehm, Markus   +6 more
core   +1 more source

Immunohistochemical expression of heparanase isoforms and syndecan-1 proteins in colorectal adenomas

open access: yesEuropean Journal of Histochemistry, 2016
The proteoglycan syndecan-1 and the endoglucuronidases heparanase-1 and heparanase-2 are involved in molecular pathways that deregulate cell adhesion during carcinogenesis.
J. Waisberg   +6 more
doaj   +1 more source

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