Search Results - "Matsas, R"

Mirk/Dyrk1B controls ventral spinal cord development via Shh pathway by Kokkorakis, N., Douka, K., Nalmpanti, A., Politis, P. K., Zagoraiou, L., Matsas, R., Gaitanou, M.

“…Cross-talk between Mirk/Dyrk1B kinase and Sonic hedgehog (Shh)/Gli pathway affects physiology and pathology. Here, we reveal a novel role for Dyrk1B in…”
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Schwann cell transplantation for CNS repair by Lavdas, A A, Papastefanaki, F, Thomaidou, D, Matsas, R

“…Demyelination occurs in several central nervous system (CNS) disorders, including multiple sclerosis, viral infection and spinal cord injury and can result in…”
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Grafts of Schwann cells engineered to express PSA-NCAM promote functional recovery after spinal cord injury by Papastefanaki, Florentia, Chen, Jian, Lavdas, Alexandros A., Thomaidou, Dimitra, Schachner, Melitta, Matsas, Rebecca

“…Schwann cells (SCs) are among the most attractive cellular candidates for the development of remyelination therapies for CNS lesions. Yet, their integration in…”
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Schwann cells genetically engineered to express PSA show enhanced migratory potential without impairment of their myelinating ability in vitro by Lavdas, Alexandros A, Franceschini, Isabelle, Dubois-Dalcq, Monique, Matsas, Rebecca

“…Schwann cells, the myelin‐forming cells of the PNS, are attractive candidates for remyelination therapy as they can remyelinate CNS axons. Yet their…”
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The beneficial effect of genetically engineered Schwann cells with enhanced motility in peripheral nerve regeneration: review by Gravvanis, A I, Lavdas, A A, Papalois, A, Tsoutsos, D A, Matsas, R

“…The importance of Schwann cells in promoting nerve regeneration across a conduit has been extensively reported in the literature, and Schwann cell motility has…”
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Management of infants with Pierre Robin sequence by Matsas, R, Thomson, A, Goodacre, T

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The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11 by Matsas, R, Kenny, A J, Turner, A J

“…Endopeptidase-24.11 (EC 3.4.24.11), purified to homogeneity from pig kidney, was shown to hydrolyse a wide range of neuropeptides, including enkephalins,…”
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Early expression of the BM88 antigen during neuronal differentiation of P19 embryonal carcinoma cells by Boutou, E., Hurel, C., Matsas, R.

“…Previous studies have shown that the BM88 antigen, a neuron‐specific molecule, promotes the differentiation of mouse neuroblastoma cells [23] (Mamalaki A.,…”
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Substance P and [Leu]enkephalin are Hydrolyzed by an Enzyme in Pig Caudate Synaptic Membranes That is Identical with the Endopeptidase of Kidney Microvilli by Matsas, Rebecca, Fulcher, Ian S., Kenny, A. John, Turner, Anthony J.

“…The hydrolysis of [Leu]enkephalin and substance P by purified pig kidney endopeptidase (EC 3.4.24.11) and synaptic membranes prepared from pig caudate nuclei…”
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An immunohistochemical study of endopeptidase-24.11 ("enkephalinase") in the pig nervous system by Matsas, R, Kenny, A J, Turner, A J

“…Endopeptidase-24.11, a plasma membrane ectoenzyme with the ability to hydrolyse a variety of neuropeptides, has been localized in the pig nervous system by an…”
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Characterization and localization of the BM88 antigen in the developing and adult rat brain by Patsavoudi, E, Merkouri, E, Thomaidou, D, Sandillon, F, Alonso, G, Matsas, R

“…Monoclonal antibody BM88 identifies a neuron-specific antigen (BM88 antigen) present in the central and peripheral nervous system of the pig (Patsavoudi et…”
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Monoclonal antibody BM89 recognizes a novel cell surface glycoprotein of the L2/HNK-1 family in the developing mammalian nervous system by Merkouri, E, Matsas, R

“…A monoclonal antibody, BM89, obtained with Triton X-114-treated pig synaptic membranes as an immunogen, recognizes a neuronal antigen in the newborn porcine…”
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Endopeptidase-24.11 is suppressed in myelin-forming but not in non-myelin-forming Schwann cells during development of the rat sciatic nerve by Kioussi, C, Crine, P, Matsas, R

“…Endopeptidase-24.11, which is identical with the common acute lymphoblastic leukemia antigen (CALLA), is a cell surface zinc metalloprotease that has the…”
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Purification and characterization of neuron-specific surface antigen defined by monoclonal antibody BM88 by Patsavoudi, E, Hurel, C, Matsas, R

“…Monoclonal antibody BM88 recognizes a neurospecific surface antigen in the CNS and the PNS. In the present study, the antigen recognized by BM88 was…”
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The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N by Matsas, R, Stephenson, S L, Hryszko, J, Kenny, A J, Turner, A J

“…The property of solutions of Triton X-114 to separate into detergent-rich and detergent-poor phases at 30 degrees C has been exploited to investigate the…”
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Purification of endopeptidase-24.11 ('enkephalinase') from pig brain by immunoadsorbent chromatography by Relton, J M, Gee, N S, Matsas, R, Turner, A J, Kenny, A J

“…Membrane preparations from striatum of pig brain contain endopeptidase activity towards iodoinsulin B-chain. Only 50% of the hydrolysis of insulin B-chain is…”
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Neuron- and myelin-specific monoclonal antibodies recognizing cell-surface antigens of the central and peripheral nervous system by Patsavoudi, E, Hurel, C, Matsas, R

“…Immunohistochemical screening of monoclonal antibodies raised against Triton X-114-treated synaptic membranes revealed two monoclonal antibodies, namely BM88…”
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The metabolism of neuropeptides. Endopeptidase-24.11 in human synaptic membrane preparations hydrolyses substance P by Matsas, R, Rattray, M, Kenny, A J, Turner, A J

“…Synaptic membrane preparations from human striatum and human diencephalon were shown to contain a phosphoramidon-sensitive metalloendopeptidase that appeared…”
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Kidney neutral endopeptidase and the hydrolysis of enkephalin by synaptic membranes show similar sensitivity to inhibitors by Fulcher, I S, Matsas, R, Turner, A J, Kenny, A J

“…Neutral endopeptidase (EC 3.4.24.11) from pig kidney hydrolyses [125I]iodo-insulin B-chain and leucine-enkephalin. Both activities were equally sensitive to…”
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Endopeptidase-24.11 is striosomally ordered in pig brain and, in contrast to aminopeptidase N and peptidyl dipeptidase A ('angiotensin converting enzyme'), is a marker for a set of striatal efferent fibres by Barnes, K, Matsas, R, Hooper, N M, Turner, A J, Kenny, A J

“…Endopeptidase-24.11 (sometimes referred to as 'enkephalinase') is a key cell-surface enzyme in the metabolism of neuropeptides. A previous immunohistochemical…”
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