About: The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix     Goto   Sponge   NotDistinct   Permalink

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  • Background: Myeloperoxidase (MPO) is an abundant hemoprotein expressed by neutrophil granulocytes that is recognized to play an important role in the development of vascular diseases. Upon degranulation from circulating neutrophil granulocytes, MPO binds to the surface of endothelial cells in an electrostatic-dependent manner and undergoes transcytotic migration to the underlying extracellular matrix (ECM). However, the mechanisms governing the binding of MPO to subendothelial ECM proteins, and whether this binding modulates its enzymatic functions are not well understood. Methods: We investigated MPO binding to ECM derived from aortic endothelial cells, aortic smooth muscle cells, and fibroblasts, and to purified ECM proteins, and the modulation of these associations by glycosaminoglycans. The oxidizing and chlorinating potential of MPO upon binding to ECM proteins was tested. observed.
  • Background: Myeloperoxidase (MPO) is an abundant hemoprotein expressed by neutrophil granulocytes that is recognized to play an important role in the development of vascular diseases. Upon degranulation from circulating neutrophil granulocytes, MPO binds to the surface of endothelial cells in an electrostatic-dependent manner and undergoes transcytotic migration to the underlying extracellular matrix (ECM). However, the mechanisms governing the binding of MPO to subendothelial ECM proteins, and whether this binding modulates its enzymatic functions are not well understood. Methods: We investigated MPO binding to ECM derived from aortic endothelial cells, aortic smooth muscle cells, and fibroblasts, and to purified ECM proteins, and the modulation of these associations by glycosaminoglycans. The oxidizing and chlorinating potential of MPO upon binding to ECM proteins was tested. observed. (en)
Title
  • The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix
  • The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix (en)
skos:prefLabel
  • The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix
  • The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix (en)
skos:notation
  • RIV/68081707:_____/13:00399439!RIV14-GA0-68081707
http://linked.open...avai/riv/aktivita
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  • I, P(ED1.100/02/0123), P(GCP305/12/J038), Z(AV0Z50040702)
http://linked.open...iv/cisloPeriodika
  • 10
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  • 97851
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  • RIV/68081707:_____/13:00399439
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  • Endothelium; Enzyme activity; Collagen IV (en)
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  • NL - Nizozemsko
http://linked.open...ontrolniKodProRIV
  • [9AB2127CA9E5]
http://linked.open...i/riv/nazevZdroje
  • Biochimica et Biophysica Acta. General Subjects
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  • 1830
http://linked.open...iv/tvurceVysledku
  • Kubala, Lukáš
  • Kolářová, Hana
  • Víteček, Jan
  • Baldus, S.
  • Klinke, A.
  • Lau, D.
  • Eiserich, J. P.
  • Kremserová, Silvie
  • Chapman, A.L.P.
http://linked.open...ain/vavai/riv/wos
  • 000323854900013
http://linked.open...n/vavai/riv/zamer
issn
  • 0304-4165
number of pages
http://bibframe.org/vocab/doi
  • 10.1016/j.bbagen.2013.05.024
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