Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor.
about
Inhibition of platelet adhesion and aggregation by a defined region (Gly-486-Lys-502) of high molecular weight kininogenInduction of apoptosis in vascular cells by plasminogen activator inhibitor-1 and high molecular weight kininogen correlates with their anti-adhesive propertiesOrganization, evolution and functions of the human and mouse Ly6/uPAR family genesThe hyaluronan-binding serine protease from human plasma cleaves HMW and LMW kininogen and releases bradykininThe urokinase receptor (uPAR) and the uPAR-associated protein (uPARAP/Endo180): membrane proteins engaged in matrix turnover during tissue remodelingA plasma kallikrein-dependent plasminogen cascade required for adipocyte differentiationA monoclonal antibody to high-molecular weight kininogen is therapeutic in a rodent model of reactive arthritisIdentification of cytokeratin 1 as a binding protein and presentation receptor for kininogens on endothelial cellsNovel pathogenic mechanism and therapeutic approaches to angioedema associated with C1 inhibitor deficiency.Upregulation of tissue factor in monocytes by cleaved high molecular weight kininogen is dependent on TNF-alpha and IL-1betaThe high-molecular-weight kininogen domain 5 is an intrinsically unstructured protein and its interaction with ferritin is metal mediated.High molecular weight kininogen binds phosphatidylserine and opsonizes urokinase plasminogen activator receptor-mediated efferocytosis.Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator.Bradykinin metabolism and hypotensive transfusion reactions.The antiangiogenic activity of cleaved high molecular weight kininogen is mediated through binding to endothelial cell tropomyosinRole of the light chain of high molecular weight kininogen in adhesion, cell-associated proteolysis and angiogenesis.The hemostatic system and angiogenesis in malignancy.The plasma kallikrein-kinin system counterbalances the renin-angiotensin systemVitronectin accumulates in the interstitium but minimally impacts fibrogenesis in experimental chronic kidney diseaseHigh molecular weight kininogen activates B2 receptor signaling pathway in human vascular endothelial cellsUrokinase and its receptors in chronic kidney disease.Cross-talk between the complement and the kinin system in vascular permeability.Structure-function studies using deletion mutants identify domains of gC1qR/p33 as potential therapeutic targets for vascular permeability and inflammation.Endothelial-cell apoptosis induced by cleaved high-molecular-weight kininogen (HKa) is matrix dependent and requires the generation of reactive oxygen species.The contribution of gC1qR/p33 in infection and inflammationStructural basis of interaction between urokinase-type plasminogen activator and its receptorGenetically altered animal models in the kallikrein-kinin system.Assembly, activation, and physiologic influence of the plasma kallikrein/kinin system.The inhibitory effect of HKa in endothelial cell tube formation is mediated by disrupting the uPA-uPAR complex and inhibiting its signaling and internalization.Domain 2 of uPAR regulates single-chain urokinase-mediated angiogenesis through β1-integrin and VEGFR2Soluble gC1qR is an autocrine signal that induces B1R expression on endothelial cells.Urokinase plasminogen activator system as a potential target for cancer therapy.Effect of His-Gly-Lys motif derived from domain 5 of high molecular weight kininogen on suppression of cancer metastasis both in vitro and in vivo.Tc-99m Glu-Cys-Gly-His-Gly-Lys (ECG-HGK), a novel Tc-99m labeled hexapeptide for molecular tumor imaging.Activation of the kinin-forming cascade on the surface of endothelial cells.High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells.Cigarette Smoke and the Induction of Urokinase Plasminogen Activator Receptor In Vivo: Selective Contribution of Isoforms to Bronchial Epithelial Phenotype.Novel role for p56/Lck in regulation of endothelial cell survival and angiogenesis.Rac mediates cytoskeletal rearrangements and increased cell motility induced by urokinase-type plasminogen activator receptor binding to vitronectin.Cleaved high molecular weight kininogen inhibits tube formation of endothelial progenitor cells via suppression of matrix metalloproteinase 2.
P2860
Q24294902-2B66322E-6179-467C-B89A-D497D0D463FBQ24300523-9A800633-9BD8-445E-A207-64B4CFB5CD7AQ28071700-C6936CDF-C710-454B-B234-4C5EF6846B9FQ28216096-47636256-7EA1-438B-BE03-385A8CE612F7Q28257803-47CC2EE6-3A44-430A-9279-E0CB0EB453E0Q28357136-A86CB7DF-7B04-407C-AF7F-8AB39FA3E7EAQ28572406-68DB077F-DC36-4688-9CBE-0E8856E61A06Q32081348-D44D858F-BB22-4A4A-8EDC-FECA29292F4DQ33560367-4703E8D1-C326-4B2A-A630-7B0B512F3B53Q33655925-F51B6B8C-D093-4919-A445-3EA15541270CQ33977801-7C146510-B0C8-446C-A3A9-1931B4879218Q34053623-52B6707A-1ACC-4089-B10B-0A0C7CEA2D2DQ34112923-1295760F-7C67-40D4-95C9-D7DC36F534C8Q34132135-8E1B9483-2191-4D52-8E81-FF8A22DAF597Q34155709-C133C721-7BC6-4910-836B-AC6FB4BF2985Q34189968-DD290DF7-7AA2-48C1-AD5C-6BDEFF7C87EDQ34425462-30C91398-010E-46AC-A859-D3C2A35B2234Q34603054-BE9DA52F-5A3D-4687-ADEA-14DE69218245Q34979663-A7078C7A-EA0B-4298-9DEC-F757D6F5590AQ35107342-CCA7D22A-8777-4CA8-8A50-87FDB8C0E8F7Q35124141-F7ACAF19-8B5F-4407-9F3C-ECC2CF177F6FQ35182755-09B0F641-34DE-400A-81F2-443E8FA5930BQ35691775-82DCD747-CA04-4487-8617-D971C5B0C276Q35849729-491E50C9-9F25-49A1-93F5-DEF6AF6028DFQ36026773-084883B3-3223-405F-9D13-8E2596BA5F36Q36237711-95DE44E7-C0E1-4353-91CD-5B00345CBB7AQ36404457-15FB995B-547E-4A5A-9206-58A4317B727CQ36492944-304C9183-2F4B-423D-978E-398F84D23E6CQ36805290-99CE4AD8-6D97-40D2-A316-27A6E505C6BEQ37093692-353F0C43-68C8-4F26-9C61-027E7A1DDB6AQ37423077-903F9405-2C49-4B03-815B-D8D295DDD91FQ37630593-CD38B52D-A1DA-4059-9770-67917397EB9CQ38350114-24FD7456-82C0-4E04-8998-98FA6564D0FEQ38795579-9448BD4D-7823-43A4-85E0-7D7F5BB83CC4Q40819973-6FDA1849-7AF4-4A60-BBA5-D508E072AB9FQ40874868-8BA15038-342C-4E99-BFCC-7CE5CA6B7D43Q41608839-D7BF5E9D-CA78-470B-8B2B-E6C96A2347DAQ41641926-C8C31B97-3820-4B1F-9B1D-9AFD4F3251B2Q41812511-E6BB6B28-50C7-42D7-879B-063AB0DD3818Q41855551-D5F5C2D6-00EC-4338-9609-2D8E1A0C3A24
P2860
Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on September 1997
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Binding of high molecular weig ...... d 3 of the urokinase receptor.
@en
Binding of high molecular weig ...... d 3 of the urokinase receptor.
@nl
type
label
Binding of high molecular weig ...... d 3 of the urokinase receptor.
@en
Binding of high molecular weig ...... d 3 of the urokinase receptor.
@nl
prefLabel
Binding of high molecular weig ...... d 3 of the urokinase receptor.
@en
Binding of high molecular weig ...... d 3 of the urokinase receptor.
@nl
P2093
P2860
P356
P1476
Binding of high molecular weig ...... d 3 of the urokinase receptor.
@en
P2093
K R McCrae
R A Pixley
R W Colman
S Najamunnisa
P2860
P304
P356
10.1172/JCI119669
P407
P577
1997-09-01T00:00:00Z