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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Heparanase

Hep, heparanase
Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. The protein encoded by this gene is an enzyme that cleaves heparan sulfate proteoglycans to permit cell movement through remodeling of the extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2011] (from NCBI)
Top mentioned proteins: CAN, V1a, HAD, ACID, PrP
Papers using Hep antibodies
The metabolic enzyme CTP synthase forms cytoskeletal filaments
Supplier
Jhaveri Ravi, In PLoS ONE, 2009
... Representative samples were also tested in other HEp-2 slide brands: Hemagen (Virgo®, Columbia, Maryland, USA), MBL Bion (Des Plaines, Illinois, ...
Low and high affinity receptors mediate cellular uptake of heparanase.
Supplier
Unutmaz Derya, In PLoS ONE, 2007
... Heparanase overexpressing C57BL/6 transgenic ( ...
Human mitochondrial topoisomerase I
Supplier
Andrade Luís Eduardo Coelho et al., In Rheumatology (Oxford, England), 2000
... ] on a variety of cell substrates, including commercial HEp-2 cell slides from six different suppliers [Hemagen Diagnostics, Bion Enterprise, Bio-Rad Laboratories (Columbia, MD, USA), Inova Diagnostics, The Binding Site (Birmingham, UK) and IMMCO ...
Cell surface control of differentiation in Acanthamoeba
Supplier
Descoteaux Albert, In Fems Microbiology Letters, 1993
... In brief, HEp-2 cells were cultured in a 1 : 1 mixture of PC-1 (Bio-Whittaker, Walkersville, MD) and CO2-independent medium (Life Technologies Ltd, Paisley, Scotland) supplemented ...
Papers on Hep
The novel chlamydial adhesin CPn0473 mediates the Lipid Raft-dependent uptake of Chlamydia pneumoniae.
New
Hegemann et al., Düsseldorf, Germany. In Cell Microbiol, Feb 2016
Soluble recombinant CPn0473 as well as rCPn0473-coupled fluorescent latex beads adhere to human epithelial HEp-2 cells.
Surface-modified yeast cells: A novel eukaryotic carrier for oral application.
New
Breinig et al., Saarbrücken, Germany. In J Control Release, Feb 2016
All invasin derivatives were shown to be effectively expressed on the cell surface and recombinant yeast cells showed improved binding to both human HEp-2 cells and M-like cells in vitro.
Quantification for total demethylation potential of environmental samples utilizing the EGFP reporter gene.
New
Wang et al., Beijing, China. In J Hazard Mater, Jan 2016
The demethylation epigenetic toxicity was determined using the Hep G2 cell line transfected with pEGFP-C3 plasmids containing a methylated promoter of the EGFP reporter gene.
"GAG-ing with the neuron": The role of glycosaminoglycan patterning in the central nervous system.
Review
New
Fawcett et al., Cambridge, United Kingdom. In Exp Neurol, Dec 2015
GAGs are classified based on their disaccharide subunits, into the following major groups: chondroitin sulfate (CS), heparan sulfate (HS), heparin (HEP), dermatan sulfate (DS), keratan sulfate (KS) and hyaluronic acid (HA).
From gene discovery to new biological mechanisms: heparanases and congenital urinary bladder disease.
Review
New
Woolf et al., Manchester, United Kingdom. In Nephrol Dial Transplant, Sep 2015
We focus on heparanase proteins and the peripheral nervous system, molecules and tissues that appear to be key players in the pathogenesis of UFS and therefore must also be critical for functional differentiation of healthy bladders.
Heparanase promotes tumor infiltration and antitumor activity of CAR-redirected T lymphocytes.
New
Impact
Dotti et al., Houston, United States. In Nat Med, May 2015
In contrast to freshly isolated T lymphocytes, we found that in vitro-cultured T lymphocytes lack expression of the enzyme heparanase (HPSE), which degrades heparan sulfate proteoglycans, the main components of ECM.
Overexpression of heparanase is associated with preeclampsia by inhibiting invasion of trophocytes.
Luo et al., Chengdu, China. In Int J Clin Exp Med, 2014
As a β-D-glucuronidase enzyme, Heparanase is related to tumor angiogenesis, development and invasion.
The Matricellular Receptor LRP1 Forms an Interface for Signaling and Endocytosis in Modulation of the Extracellular Tumor Environment.
Review
Roebroek et al., Leuven, Belgium. In Front Pharmacol, 2014
As a matricellular receptor it is involved in regulation, mostly by clearing, of various extracellular matrix degrading enzymes including matrix metalloproteinases, serine proteases, protease inhibitor complexes, and the endoglycosidase heparanase.
Extracellular matrix as target for antitumor therapy.
Review
Jeney et al., Budapest, Hungary. In Onco Targets Ther, 2014
At present, the elevated level of heparanase and the prominent expression of αvβ5 integrin are considered as promising therapeutic targets.
Hepatoerythropoietic Porphyria Caused by a Novel Homoallelic Mutation in Uroporphyrinogen Decarboxylase Gene in Egyptian Patients.
Martásek et al., Praha, Czech Republic. In Folia Biol (praha), 2014
Hepatoerythropoietic porphyria (HEP) is a rare type of porphyria caused by the deficiency of the fifth enzyme (uroporphyrinogen decarboxylase, UROD) in this pathway.
Fosfomycin: Uses and potentialities in veterinary medicine.
Review
Soraci et al., Tandil, Argentina. In Open Vet J, 2013
FOS penetration is demonstrated in phagocytic, respiratory (HEP-2) and intestinal (IPEC-J2) cells.
The pulmonary endothelial glycocalyx regulates neutrophil adhesion and lung injury during experimental sepsis.
Impact
Tuder et al., Aurora, United States. In Nat Med, 2012
Glycocalyx degradation involved the specific loss of heparan sulfate and coincided with activation of endothelial heparanase, a TNF-α-responsive, heparan sulfate-specific glucuronidase.
Heparanase procoagulant activity.
GeneRIF
Brenner et al., Haifa, Israel. In Thromb Res, 2012
Taking into account the pro-metastatic and pro-angiogenic functions of heparanase, with over-expression in human malignancies and abundance in platelets and placenta.
Expression of Ext1, Ext2, and heparanase genes in brain of senescence-accelerated OXYS rats in early ontogenesis and during development of neurodegenerative changes.
GeneRIF
Kolosova et al., Novosibirsk, Russia. In Biochemistry (mosc), 2012
Heparanase gene is involved in heparan sulfate proteoglycans metabolism.
Small RNAs targeting transcription start site induce heparanase silencing through interference with transcription initiation in human cancer cells.
GeneRIF
Tong et al., Wuhan, China. In Plos One, 2011
These results suggest that small RNAs targeting transcription start site can induce transcriptional gene silencing of heparanase via interference with transcription initiation.
Heparanase affects food intake and regulates energy balance in mice.
GeneRIF
Dickson et al., Göteborg, Sweden. In Plos One, 2011
heparanase acts as a negative modulator of AgRP signaling at MC4R, through cleavage of heparan sulfate chains presumably linked to syndecan-3
Dissociation between mature phenotype and impaired transmigration in dendritic cells from heparanase-deficient mice.
GeneRIF
Mevorach et al., Jerusalem, Israel. In Plos One, 2011
Together with CCR7 and its ligands, and probably MMP-14, heparanase controls DC trafficking.
An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis.
Impact
Metcalf et al., Urbana, United States. In Nature, 2009
Recent genetic and biochemical studies showed that during phosphinothricin tripeptide biosynthesis 2-hydroxyethylphosphonate (HEP) is converted to hydroxymethylphosphonate (HMP).
Tumor-targeted, systemic delivery of therapeutic viral vectors using hitchhiking on antigen-specific T cells.
Impact
Vile et al., Rochester, United States. In Nat Med, 2005
Productive hand off correlated with local heparanase expression either from malignant tumor cells and/or as a result of T-cell activation by antigen, providing high levels of selectivity for viral transfer to metastatic tumors in vivo.
Cloning of mammalian heparanase, an important enzyme in tumor invasion and metastasis.
Impact
Parish et al., Canberra, Australia. In Nat Med, 1999
The endoglycosidase heparanase is an important in the degradation of the extracellular matrix by invading cells, notably metastatic tumor cells and migrating leukocytes.
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