Matrilysin is expressed by lipid-laden macrophages at sites of potential rupture in atherosclerotic lesions and localizes to areas of versican deposition, a proteoglycan substrate for the enzyme.
about
Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysmsVersican degradation and vascular diseaseMatrix metalloproteinases in lung biologyMonocyte matrix metalloproteinase production in Type 2 diabetes and controls--a cross sectional studyInsights from Selective Non-phosphinic Inhibitors of MMP-12 Tailored to Fit with an S1' Loop Canonical ConformationMacrophage metalloelastase, MMP-12, cleaves human apolipoprotein(a) in the linker region between kringles IV-4 and IV-5. Potential relevance to lipoprotein(a) biologyAntimicrobial peptides are expressed and produced in healthy and inflamed human synovial membranesVersican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4Extra-cellular matrix in vascular networksAcrolein activates matrix metalloproteinases by increasing reactive oxygen species in macrophagesRadiolabelled probes for imaging of atherosclerotic plaques.A model to explain specific cellular communications and cellular harmony:- a hypothesis of coupled cells and interactive coupling molecules.Atherosclerosis and matrix metalloproteinases: experimental molecular MR imaging in vivoAllele-specific regulation of matrix metalloproteinase-3 gene by transcription factor NFkappaBUrine matrix metalloproteinase-7 and risk of kidney disease progression and mortality in type 2 diabetes.Sputum hyaluronan and versican in severe eosinophilic asthma.Matrix metalloproteinases in repair.Overexpression of urokinase by plaque macrophages causes histological features of plaque rupture and increases vascular matrix metalloproteinase activity in aged apolipoprotein e-null miceDual-wavelength multifrequency photothermal wave imaging combined with optical coherence tomography for macrophage and lipid detection in atherosclerotic plaques using gold nanoparticles.MMP-7 mediates cleavage of N-cadherin and promotes smooth muscle cell apoptosis.The multiple, complex roles of versican and its proteolytic turnover by ADAMTS proteases during embryogenesis.A novel MMP12 locus is associated with large artery atherosclerotic stroke using a genome-wide age-at-onset informed approachThe extracellular matrix can regulate vascular cell migration, proliferation, and survival: relationships to vascular disease.Therapeutic potential of matrix metalloproteinase inhibitors in atherosclerosis.Divergent effects of matrix metalloproteinases 3, 7, 9, and 12 on atherosclerotic plaque stability in mouse brachiocephalic arteries.Macrophage expression of active MMP-9 induces acute plaque disruption in apoE-deficient miceFocal cerebral ischemia induces active proteases that degrade microvascular matrix.Diet-induced obesity and reduced skin cancer susceptibility in matrix metalloproteinase 19-deficient miceNitroglycerin alters matrix remodeling proteins in THP-1 human macrophages and plasma metalloproteinase activity in rats.Accumulation and loss of extracellular matrix during shear stress-mediated intimal growth and regression in baboon vascular grafts.A selective matrix metalloproteinase-12 inhibitor retards atherosclerotic plaque development in apolipoprotein E-knockout mice.Matrix metalloproteinases and atherosclerotic plaque instability.Deficiency of cathepsin S reduces atherosclerosis in LDL receptor-deficient miceThe role of matrix metalloproteinases in vascular disease.Identification of candidate genes involved in coronary artery calcification by transcriptome sequencing of cell lines.Parallel expression of macrophage metalloelastase (MMP-12) in duodenal and skin lesions of patients with dermatitis herpetiformisLevels of Circulating MMCN-151, a Degradation Product of Mimecan, Reflect Pathological Extracellular Matrix Remodeling in Apolipoprotein E Knockout MiceProteolytic cleavage of versican and involvement of ADAMTS-1 in VEGF-A/VPF-induced pathological angiogenesis.Increased collagenase activity in macrophages from bronchial lavage as a diagnostic marker of non-small cell lung cancer.Expression and localization of matrix metalloproteinase-12 in the aorta of cholesterol-fed rabbits: relationship to lesion development
P2860
Q24564318-5D22C791-E229-4F9A-9249-AE95D0152F7EQ24600539-FB08EC52-D0DD-42B4-AA06-BC8BF6F494D2Q24791682-5E73ECE2-CFCD-447C-A226-88055310101BQ24806823-0F1FD92B-88C1-4FF7-8D0B-41CFDC94AD56Q27664274-8E5E8A5C-7B6C-4C68-BFDD-B7D955CDF59DQ28140467-867A0A4E-549E-4394-B957-17AC56524B13Q28206744-2CFA528A-B612-4BA0-B63A-C0B6982E02AFQ28207975-F4BFB589-DD9D-4358-A2C1-D43F60E8E362Q28261826-92F0610F-7E3B-4C3A-A7CF-D50882EF6D94Q28754552-C5B5D7F0-9C47-40D3-AF63-D9806BF80AD9Q30577193-417295E5-89CE-4B12-8D2A-38C61A189A60Q30599952-1A418D04-4F59-4FB7-8BA2-7D0AAAAFA60BQ33410205-F836C9B6-2EAE-4352-9E91-44F305617296Q33548692-DA02F2B9-57E8-4525-B47C-949A114CD2AEQ33559001-95D98304-701D-4543-9349-A810DB069BA0Q33760636-3F32F292-5314-458A-90B1-B255AEAF0C18Q33815962-25CC1A0F-AE3F-4E3F-8C3F-4E3A519F9E1FQ33858160-627A67F0-657D-4F03-BB1A-B7B7BE32E8A9Q33901369-DE2E67FE-825D-4842-8D37-B6899C980F1AQ33906860-2743D557-C8F4-4216-ACF4-9E64FFDD7A70Q33925634-2004EC3D-D570-41E9-9A10-17941ABF6C20Q33981695-D8126C50-22FF-435A-9842-63496172486DQ34022649-49E2231E-14A2-4063-AFAC-E4EAB3C9D8B5Q34074837-2A8EB686-1A62-4C4E-9D1C-879EED47979EQ34098485-D023B4FB-FC3C-464B-9924-CFDCF2740894Q34236802-4B656784-7B00-4E87-9B73-3DAC594B3168Q34301092-751D0B73-D0FF-4F21-8F8F-506EDECA7A88Q34346225-3427981F-87DA-4AF9-8757-5D4C5F1FA430Q34574503-1E3D572D-F3AF-4A48-A513-834C9CA1A364Q34576649-EB00727C-2D80-43A1-A8BF-993BC61556E7Q34585560-CADE34C3-04D2-495B-835D-7AC6B35A4CE1Q34655385-F2163216-8EE7-46DC-B8B2-D54285A821CBQ34967612-441CCEB9-EDE1-4BF7-BD27-3AA788BA799CQ34981650-9E5CFC42-CF92-4C31-B1C4-B5A5CFD9EF97Q35120692-0CCB7376-3B56-4458-A77E-5E650F5D097CQ35363095-41A73115-D773-4863-860C-8ABB497CAE31Q35440249-EED0C11E-A63C-435D-A622-7E0207531810Q35441108-85090C66-105C-4062-B0E4-C7A1369148EEQ35535722-CAA33243-8C94-48A9-AF6A-3D9DB80FE6C9Q35753125-3FE2870D-E136-4FC8-B984-E3FDC11BB0B6
P2860
Matrilysin is expressed by lipid-laden macrophages at sites of potential rupture in atherosclerotic lesions and localizes to areas of versican deposition, a proteoglycan substrate for the enzyme.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on September 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Matrilysin is expressed by lip ...... ycan substrate for the enzyme.
@en
Matrilysin is expressed by lip ...... ycan substrate for the enzyme.
@nl
type
label
Matrilysin is expressed by lip ...... ycan substrate for the enzyme.
@en
Matrilysin is expressed by lip ...... ycan substrate for the enzyme.
@nl
prefLabel
Matrilysin is expressed by lip ...... ycan substrate for the enzyme.
@en
Matrilysin is expressed by lip ...... ycan substrate for the enzyme.
@nl
P2093
P2860
P356
P1476
Matrilysin is expressed by lip ...... ycan substrate for the enzyme.
@en
P2093
H G Welgus
S A Wickline
S D Shapiro
S Potter-Perigo
P2860
P304
P356
10.1073/PNAS.93.18.9748
P407
P577
1996-09-01T00:00:00Z