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18 results on '"Vlodavsky, Israel"'

3. Heparanase: A Potential New Factor Involved in the Renal Epithelial Mesenchymal Transition (EMT) Induced by Ischemia/Reperfusion (I/R) Injury

Author

Masola, Valentina, primary, Zaza, Gianluigi, additional, Gambaro, Giovanni, additional, Onisto, Maurizio, additional, Bellin, Gloria, additional, Vischini, Gisella, additional, Khamaysi, Iyad, additional, Hassan, Ahmad, additional, Hamoud, Shadi, additional, Nativ, Omri, additional, N. Heyman, Samuel, additional, Lupo, Antonio, additional, Vlodavsky, Israel, additional, and Abassi, Zaid, additional

Published
2016
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7. Correction: Heparanase Affects Food Intake and Regulates Energy Balance in Mice

Author

Karlsson-Lindahl, Linda, primary, Schmidt, Linnéa, additional, Haage, David, additional, Hansson, Caroline, additional, Taube, Magdalena, additional, Egeciouglu, Emil, additional, Tan, Ying-xia, additional, Admyre, Therese, additional, Jansson, John-Olov, additional, Vlodavsky, Israel, additional, Li, Jin-Ping, additional, Lindahl, Ulf, additional, and Dickson, Suzanne L., additional

Published
2012
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11. Heparanase Affects Food Intake and Regulates Energy Balance in Mice

Author

Karlsson-Lindahl, Linda, primary, Schmidt, Linnéa, additional, Haage, David, additional, Hansson, Caroline, additional, Taube, Magdalena, additional, Egeciouglu, Emil, additional, Tan, Ying-xia, additional, Admyre, Therese, additional, Jansson, John-Olov, additional, Vlodavsky, Israel, additional, Li, Jin-Ping, additional, Lindahl, Ulf, additional, and Dickson, Suzanne L., additional

Published
2012
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17. Accelerated Resolution of AA Amyloid in Heparanase Knockout Mice Is Associated with Matrix Metalloproteases.

Author

Bo Wang, Ying-xia Tan, Juan Jia, Digre, Andreas, Xiao Zhang, Vlodavsky, Israel, and Jin-ping Li

Subjects
METALLOPROTEINASES, AMYLOID, HEPARANASE, PEPTIDES, SPLEEN, LABORATORY mice
Abstract

AA-amyloidosis is a disease characterized by abnormal deposition of serum A amyloid (SAA) peptide along with other components in various organs. The disease is a complication of inflammatory conditions that cause persistent high levels of the acute phase reactant SAA in plasma. In experimental animal models, the deposited amyloid is resolved when the inflammation is stopped, suggesting that there is an efficient clearance mechanism for the amyloid. As heparan sulfate (HS) is one of the major components in the amyloid, its metabolism is expected to affect the pathology of AA amyloidosis. In this study, we investigated the effect of heparanase, a HS degradation enzyme, in resolution of the AA amyloid. The transgenic mice deficient in heparanase (Hpa-KO) produced a similar level of SAA in plasma as the wildtype control (Ctr) mice upon induction by injection of AEF (amyloid enhancing factor) and inflammatory stimuli. The induction resulted in formation of SAA amyloid 7-days post treatment in the spleen that displayed a comparable degree of amyloid load in both groups. The amyloid became significantly less in the Hpa-KO spleen than in the Ctr spleen 10-days post treatment, and was completely resolved in the Hpa-KO spleen on day 21 post induction, while a substantial amount was still detected in the Ctr spleen. The rapid clearance of the amyloid in the Hpa-KO mice can be ascribed to upregulated matrix metalloproteases (MMPs) that are believed to contribute to degradation of the protein components in the AA amyloid. The results indicate that both heparanase and MMPs play important parts in the pathological process of AA amyloidosis. [ABSTRACT FROM AUTHOR]

Published
2012
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18. Newly Generated Heparanase Knock-Out Mice Unravel Co-Regulation of Heparanase and Matrix etalloproteinases.

Author

Zcharia, Eyal, Juan Jia, Xiao Zhang, Baraz, Lea, Lindahl, Ulf, Peretz, Tamar, Vlodavsky, Israel, and Jin-Ping Li

Subjects
LABORATORY mice, GLUCURONIDASE, MAMMARY glands, DRUG development, CONNECTIVE tissue cells, NEOVASCULARIZATION, METASTASIS, CHROMATIN
Abstract

Background: Heparanase, a mammalian endo-β-D-glucuronidase, specifically degrades heparan sulfate proteoglycans ubiquitously associated with the cell surface and extracellular matrix. This single gene encoded enzyme is over-expressed in most human cancers, promoting tumor metastasis and angiogenesis. Principal Findings: We report that targeted disruption of the murine heparanase gene eliminated heparanase enzymatic activity, resulting in accumulation of long heparan sulfate chains. Unexpectedly, the heparanase knockout (Hpse-KO) mice were fertile, exhibited a normal life span and did not show prominent pathological alterations. The lack of major abnormalities is attributed to a marked elevation in the expression of matrix metalloproteinases, for example, MMP2 and MMP14 in the Hpse-KO liver and kidney. Co-regulation of heparanase and MMPs was also noted by a marked decrease in MMP (primarily MMP-2,-9 and 14) expression following transfection and over-expression of the heparanase gene in cultured human mammary carcinoma (MDA-MB-231) cells. Immunostaining (kidney tissue) and chromatin immunoprecipitation (ChIP) analysis (Hpse-KO mouse embryonic fibroblasts) suggest that the newly discovered co-regulation of heparanase and MMPs is mediated by stabilization and transcriptional activity of β-catenin. Conclusions/Significance: The lack of heparanase expression and activity was accompanied by alterations in the expression level of MMP family members, primarily MMP-2 and MMP-14. It is conceivable that MMP-2 and MMP-14, which exert some of the effects elicited by heparanase (i.e., over branching of mammary glands, enhanced angiogenic response) can compensate for its absence, in spite of their different enzymatic substrate. Generation of viable Hpse-KO mice lacking significant abnormalities may provide a promising indication for the use of heparanase as a target for drug development. [ABSTRACT FROM AUTHOR]

Published
2009
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