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Sökning: WFRF:(Arfors K E) > Heparin-binding pro...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004074naa a2200601 4500
001oai:lup.lub.lu.se:13589d7b-0714-4900-89c7-37c5b726ab70
003SwePub
008180827s1999 | |||||||||||000 ||eng|
024a https://lup.lub.lu.se/record/13589d7b-0714-4900-89c7-37c5b726ab702 URI
024a https://doi.org/10.1172/JCI66712 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
100a Olofsson, A Mu Lund University,Lunds universitet,Institutionen för laboratoriemedicin,Medicinska fakulteten,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)medk-mol
2451 0a Heparin-binding protein targeted to mitochondrial compartments protects endothelial cells from apoptosis
264 1c 1999
520 a Neutrophil-borne heparin-binding protein (HBP) is a multifunctional protein involved in the progression of inflammation. HBP is stored in neutrophil granules and released upon stimulation of the cells in proximity to endothelial cells. HBP affects endothelial cells in multiple ways; however, the molecular and cellular mechanisms underlying the interaction of HBP with these cells are unknown. Affinity isolation and enzymatic degradation demonstrated that HBP released from human neutrophils binds to endothelial cell-surface proteoglycans, such as syndecans and glypican. Flow cytometry indicated that a significant fraction of proteoglycan-bound HBP is taken up by the endothelial cells, and we used radiolabeled HBP to determine the internalization rate of surface-bound HBP. Confocal and electron microscopy revealed that internalized HBP is targeted to perinuclear compartments of endothelial cells, where it colocalizes with mitochondria. Western blotting of isolated mitochondria from HBP-treated endothelial cells showed that HBP is present in 2 forms - 28 and 22 kDa. Internalized HBP markedly reduced growth factor deprivation-induced caspase-3 activation and protected endothelial cells from apoptosis, suggesting that uptake and intracellular routing of exogenous HBP to mitochondria contributes to the sustained viability of endothelial cells in the context of locally activated neutrophils.
653 a Antimicrobial Cationic Peptides
653 a Apoptosis/drug effects
653 a Biological Transport
653 a Blood Proteins/metabolism
653 a Carrier Proteins/metabolism
653 a Cells, Cultured
653 a Chromatography, Affinity
653 a Endothelium, Vascular/cytology
653 a Heparin/metabolism
653 a Humans
653 a Kinetics
653 a Leukotriene B4/pharmacology
653 a Mitochondria/metabolism
653 a N-Formylmethionine Leucyl-Phenylalanine/pharmacology
653 a Neutrophils/physiology
653 a Proteoglycans/isolation & purification
653 a Recombinant Proteins/metabolism
653 a Tetradecanoylphorbol Acetate/pharmacology
653 a Umbilical Veins
700a Vestberg, Mu Lund University,Lunds universitet,Immunologi,Forskargrupper vid Lunds universitet,Immunology,Lund University Research Groups4 aut0 (Swepub:lu)infl-mve
700a Herwald, Hu Lund University,Lunds universitet,Institutionen för laboratoriemedicin,Medicinska fakulteten,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)medk-hhe
700a Rygaard, J4 aut
700a David, G4 aut
700a Arfors, K E4 aut
700a Linde, V4 aut
700a Flodgaard, H4 aut
700a Dedio, J4 aut
700a Müller-Esterl, W4 aut
700a Lundgren-Akerlund, Eu Lund University4 aut
710a Institutionen för laboratoriemedicinb Medicinska fakulteten4 org
773t Journal of Clinical Investigationg 104:7, s. 885-894q 104:7<885-894x 0021-9738
856u http://dx.doi.org/10.1172/JCI6671x freey FULLTEXT
8564 8u https://lup.lub.lu.se/record/13589d7b-0714-4900-89c7-37c5b726ab70
8564 8u https://doi.org/10.1172/JCI6671

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