Brevican and phosphacan expression and localization following transient middle cerebral artery occlusion in the rat. 2007

G Haddock, and A K Cross, and S Allan, and B Sharrack, and J Callaghan, and R A D Bunning, and D J Buttle, and M N Woodroofe
Biomedical Research Centre, Faculty of Health and Well-being, Sheffield Hallam University, Howard St, Sheffield S1 1WB, UK. G.Haddock@shu.ac.uk

The ECM (extracellular matrix) is a complex molecular framework that provides physical support to cells and tissues, while also providing signals for cell growth, migration, differentiation and survival. The ECM of the CNS (central nervous system) is unusual in that it is rich in CSPGs (chondroitin sulfate proteoglycans), hyaluronan and tenascins. The CSPGs are widely expressed throughout the developing and adult CNS and have a role in guiding or limiting neurite outgrowth and cell migration. Alterations in the synthesis or breakdown of the ECM may contribute to disease processes. Here, we examine changes in the brain-specific CSPGs, brevican and phosphacan, following transient middle cerebral artery occlusion, a model of stroke in the rat. We have investigated their expression at various time points as well as their spatial relationship with ADAMTS-4 (a disintegrin and metalloprotease with thrombospondin motifs 4). The co-localization of ADAMTS or its activity may indicate a functional role for this matrix-protease pair in degeneration/regeneration processes that occur in stroke.

UI MeSH Term Description Entries
D009419 Nerve Tissue Proteins Proteins, Nerve Tissue,Tissue Proteins, Nerve
D011508 Chondroitin Sulfate Proteoglycans Proteoglycans consisting of proteins linked to one or more CHONDROITIN SULFATE-containing oligosaccharide chains. Proteochondroitin Sulfates,Chondroitin Sulfate Proteoglycan,Proteochondroitin Sulfate,Proteoglycan, Chondroitin Sulfate,Proteoglycans, Chondroitin Sulfate,Sulfate Proteoglycan, Chondroitin,Sulfate Proteoglycans, Chondroitin
D004195 Disease Models, Animal Naturally-occurring or experimentally-induced animal diseases with pathological processes analogous to human diseases. Animal Disease Model,Animal Disease Models,Disease Model, Animal
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D017027 Protein Tyrosine Phosphatases An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis. Phosphotyrosine Phosphatase,Protein-Tyrosine-Phosphatase,Tyrosyl Phosphoprotein Phosphatase,PTPase,Phosphotyrosyl Protein Phosphatase,Protein-Tyrosine Phosphatase,Phosphatase, Phosphotyrosine,Phosphatase, Phosphotyrosyl Protein,Phosphatase, Protein-Tyrosine,Phosphatase, Tyrosyl Phosphoprotein,Phosphatases, Protein Tyrosine,Phosphoprotein Phosphatase, Tyrosyl,Protein Phosphatase, Phosphotyrosyl,Protein Tyrosine Phosphatase,Tyrosine Phosphatases, Protein
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus
D054633 Receptor-Like Protein Tyrosine Phosphatases, Class 5 A subclass of receptor-like protein tryosine phosphatases that contain an extracellular fibronectin III-like domain along with a carbonic anhydrase-like domain. Protein Tyrosine Phosphatase, Receptor Type G,Protein Tyrosine Phosphatase, Receptor Type Z,PTPRG Phosphatase,Phosphacan,Protein Tyrosine Phosphatase, Receptor Type, G,Protein Tyrosine Phosphatase, Receptor-Type Z,Ptprz Phosphatase,RPTP-zeta,RPTPbeta,RPTPgamma,RPTPzeta-beta,Receptor Protein Tyrosine Phosphatase gamma,Receptor Protein Tyrosine Phosphatase zeta-beta,Receptor Protein Tyrosine Phosphatase-beta,Receptor Protein Tyrosine Phosphatase-zeta,Receptor-Like Protein Tyrosine Phosphatases, Class V,Receptor-Type Protein-Tyrosine Phosphatase-beta,Phosphatase, PTPRG,Phosphatase, Ptprz,Phosphatase-beta, Receptor-Type Protein-Tyrosine,Protein-Tyrosine Phosphatase-beta, Receptor-Type,Receptor Like Protein Tyrosine Phosphatases, Class 5,Receptor Like Protein Tyrosine Phosphatases, Class V,Receptor Protein Tyrosine Phosphatase beta,Receptor Protein Tyrosine Phosphatase zeta,Receptor Protein Tyrosine Phosphatase zeta beta,Receptor Type Protein Tyrosine Phosphatase beta
D058581 Brevican A BRAIN-specific hyalectin that may play a role in terminally differentiating NEURONS. It is found highly overexpressed in primary BRAIN TUMORS and in experimental models of GLIOMA. Brain-Enriched Hyaluronan-Binding Protein,Chondroitin Sulfate Proteoglycan 7,Brain Enriched Hyaluronan Binding Protein,Hyaluronan-Binding Protein, Brain-Enriched
D020244 Infarction, Middle Cerebral Artery NECROSIS occurring in the MIDDLE CEREBRAL ARTERY distribution system which brings blood to the entire lateral aspects of each CEREBRAL HEMISPHERE. Clinical signs include impaired cognition; APHASIA; AGRAPHIA; weak and numbness in the face and arms, contralaterally or bilaterally depending on the infarction. Cerebral Infarction, Middle Cerebral Artery,Embolic Infarction, Middle Cerebral Artery,MCA Infarct,Middle Cerebral Artery Embolus,Middle Cerebral Artery Infarction,Stroke, Middle Cerebral Artery,Thrombotic Infarction, Middle Cerebral Artery,Embolus, Middle Cerebral Artery,Left Middle Cerebral Artery Infarction,MCA Infarction,Middle Cerebral Artery Circulation Infarction,Middle Cerebral Artery Embolic Infarction,Middle Cerebral Artery Occlusion,Middle Cerebral Artery Stroke,Middle Cerebral Artery Syndrome,Middle Cerebral Artery Thrombosis,Middle Cerebral Artery Thrombotic Infarction,Occlusion, Middle Cerebral Artery,Right Middle Cerebral Artery Infarction,Thrombosis, Middle Cerebral Artery,Infarct, MCA,Infarcts, MCA,MCA Infarcts
D037181 Lectins, C-Type A class of animal lectins that bind to carbohydrate in a calcium-dependent manner. They share a common carbohydrate-binding domain that is structurally distinct from other classes of lectins. C-Type Lectin Receptor,C-Type Lectins,C-Type Lectin,Lectin, C-Type,Receptors, C-Type Lectin,C Type Lectin,C Type Lectin Receptor,C Type Lectins,C-Type Lectin Receptors,Lectin Receptor, C-Type,Lectin Receptors, C-Type,Lectin, C Type,Lectins, C Type,Receptor, C-Type Lectin,Receptors, C Type Lectin

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