Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.2.2.7 (heparinase)
 1,270 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cultured rat Schwann cells produce a basal lamina (BL)-associated heparan sulphate proteoglycan (HSPG). The HSPG has an apparent molecular weight of greater than 450 kD, is sensitive to both heparinase and heparitinase and contains a core protein of approximately 400 kD. Two independently derived monoclonal antibodies, B3 and C17, recognize this HSPG. Using B3 and C17, we found that this HSPG, or immunologically related material, is present in BLs throughout the body and in a small number of connective tissue sites without a formed BL. In the PNS it is present in BLs of Schwann cell-axon units, in synaptic and extrasynaptic portions of muscle fibre BL, and in the BLs of satellite cells that ensheath neurons in sympathetic and sensory ganglia. This HSPG is not detectable in the neuropil of the brain and spinal cord. Neurons, Schwann cells and fibroblasts cultured alone do not assemble a BL or accumulate immunocytochemically detectable amounts of this HSPG, but it is present in BLs assembled in myotube and in Schwann cell-neuron cultures. Thus, this HSPG is a component of most, if not all, BLs in the PNS.
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PMID:Basal lamina-associated heparan sulphate proteoglycan in the rat PNS: characterization and localization using monoclonal antibodies. 294 Mar 43

The heparan sulfate proteoglycan (HSPGs) is a components of the extracellular matrix of skeletal muscle that is concentrated at the neuromuscular junction (NMJ). Recent studies have suggested that HSPG, together with its bound peptide growth factors, plays important roles in autocrine or paracrine types of regulation of cell growth and differentiation. Heparin-binding growth-associated molecule (HB-GAM; also known as pleiotrophin, or p18) is a newly discovered HSPG-bound factor that is expressed at high levels in the developing CNS and PNS. In this study, we examined the role of this factor in NMJ development by examining its relationship to the formation of ACh receptor (AChR) clusters. Using an antibody against recombinant rat brain HB-GAM, we found that this protein is present prominently on the surface of cultured Xenopus myotomal muscle cells by immunocytochemistry. It is associated with HSPGs as evidenced by the fact that heparin and heparinase treatment greatly diminished the antibody labeling. HB-GAM is concentrated at preexisting AChR hot spots as well as at those induced by polystyrene beads. In addition, this molecule is also concentrated at AChR clusters induced by spinal cord neurons in nerve-muscle cocultures. To assess its function in synaptic induction, we applied recombinant HB-GAM-coated beads to cultured muscle cells to effect its focal presentation. Over 70% of these beads induced the formation of AChR clusters as shown by fluorescent alpha-bungarotoxin labeling. Furthermore, bath application of HB-GAM inhibited the nerve-induced formation of AChR clusters. Thus, HB-GAM is an endogenous muscle-derived factor that may be a component of the molecular mechanism in postsynaptic induction.
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PMID:The role of heparin-binding growth-associated molecule (HB-GAM) in the postsynaptic induction in cultured muscle cells. 772 43

The distribution of anionic microdomains has been described in cerebral vessels and more recently in capillaries of peripheral nerve. Evidence is accumulating that these sites play a role in the barrier function of vascular endothelia in the PNS and CNS. The chemical nature of anionic sites has been at least partly determined for cerebral vessels but not in peripheral nerve. This study reports our preliminary investigations to determine the nature of endothelial anionic sites in sciatic nerve. The effects of digestion of ultra-thin sections of nerve with a battery of proteolytic and glycolytic enzymes (papain, trypsin, proteinase K, hyaluronidase, heparinase, heparitinase and neuraminidase) on the distribution of anionic sites was determined using the label, cationic colloidal gold. Papain, a proteolytic enzyme of broad specificity, succeeded in removing the majority of cationic colloidal gold-binding sites on the luminal surface of vascular endothelia. In contrast trypsin and proteinase K were less effective, reflecting their narrower specificity. Hyaluronidase, heparinase and heparitinase did not significantly affect cationic colloidal gold-labelling. However, a considerable reduction in cationic colloidal gold-binding occurred following neuraminidase digestion. These results suggest that, as in cerebral vessels, sialic acid-containing glycoproteins are largely responsible for the negatively charged domains on the luminal membrane of endothelial cells in peripheral nerve.
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PMID:Molecular characterization of anionic sites on the luminal front of endoneurial capillaries in sciatic nerve. 817 16