Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes
about
MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cellsStudies in mice reveal a role for anthrax toxin receptors in matrix metalloproteinase function and extracellular matrix homeostasisIn vitro and in vivo anti-angiogenic activities of Panduratin AAnthrax toxin receptor 2 functions in ECM homeostasis of the murine reproductive tract and promotes MMP activityVideo-rate bioluminescence imaging of matrix metalloproteinase-2 secreted from a migrating cellDomain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activationHomophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion.Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)Expression of membrane-type 1 matrix metalloproteinase in rheumatoid synovial cellsActivation of pro-(matrix metalloproteinase-2) (pro-MMP-2) by thrombin is membrane-type-MMP-dependent in human umbilical vein endothelial cells and generates a distinct 63 kDa active speciesTIMP-2 is required for efficient activation of proMMP-2 in vivoExpression of gelatinases A and B in the ovary of the medaka fish Oryzias latipes.Membrane type 1 matrix metalloproteinase and gelatinase A synergistically degrade type 1 collagen in a cell model.Shedding of membrane type 1 matrix metalloproteinase in a human breast carcinoma cell line.Activation and localization of matrix metalloproteinase-2 and -9 in the skeletal muscle of the muscular dystrophy dog (CXMDJ).DA-Raf-dependent inhibition of the Ras-ERK signaling pathway in type 2 alveolar epithelial cells controls alveolar formation.The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversityHuman membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts.Matrix turnover.Cisplatin and PI3kinase inhibition decrease invasion and migration of human ovarian carcinoma cells and regulate matrix-metalloproteinase expression.TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains.Matrix metalloproteinases in arthritic diseaseTumor cell invasion of von Hippel Lindau renal cell carcinoma cells is mediated by membrane type-1 matrix metalloproteinase.Selective regulation of MMP and TIMP mRNA levels in tree shrew sclera during minus lens compensation and recoveryMembrane-type 1 matrix metalloprotease (MT1-MMP) enables invasive migration of glioma cells in central nervous system white matterExpression of matrix metalloproteinases during rat skin wound healing: evidence that membrane type-1 matrix metalloproteinase is a stromal activator of pro-gelatinase AMMP-2 release and activation in ovarian carcinoma: the role of fibroblasts.Targeting a single function of the multifunctional matrix metalloprotease MT1-MMP: impact on lymphangiogenesisLoss of TIMP3 enhances interstitial nephritis and fibrosis.URG11 promotes gastric cancer growth and invasion by activation of beta-catenin signalling pathway.Modulation of the membrane type 1 matrix metalloproteinase cytoplasmic tail enhances tumor cell invasion and proliferation in three-dimensional collagen matrices.Coordinate action of membrane-type matrix metalloproteinase-1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion.Tissue inhibitor of metalloproteinases (TIMPs) in heart failure.Melanoma biomolecules: independently identified but functionally intertwined.Matrix metalloproteinases are involved in cardiovascular diseases.The canonical methionine 392 of matrix metalloproteinase 2 (gelatinase A) is not required for catalytic efficiency or structural integrity: probing the role of the methionine-turn in the metzincin metalloprotease superfamily.Panduratin A, a possible inhibitor in metastasized A549 cells through inhibition of NF-kappa B translocation and chemoinvasion.CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain.Tissue inhibitor of metalloproteinase-2 regulates matrix metalloproteinase-2-mediated endothelial barrier dysfunction and breast cancer cell transmigration through lung microvascular endothelial cells.Individual Timp deficiencies differentially impact pro-MMP-2 activation.
P2860
Q24685496-A0F3689E-29DD-43A9-BE39-3F287C1F8450Q27010122-18936C39-6F7D-4A77-98DC-FF67F9153726Q27301905-3BEA29B8-677C-400B-AA5A-A8CA9691AF37Q27304959-833789A1-EFBD-4D6C-816D-D288717EA538Q27318583-F8C3CFF2-F26D-40C9-9F52-3F106DA9D4EBQ28138867-452B73C8-B228-4B03-95F8-842B68455980Q28215016-75CB72B2-449B-4EC7-9D5F-CC3C7DB7FEE5Q28258413-EFF7D941-4D28-4291-95C2-E9E6CEFD4839Q28362611-16A630F5-17DE-4837-9D31-2A3637275C06Q28367213-57ABB758-3BD6-4565-86B9-B11CCADFFF87Q28512714-5FEA6159-6F27-444D-AEB7-0F90ABE98CBEQ30886690-21FFC9C3-0DCE-4F48-850D-D644DE78205BQ32148378-5B9E3892-3017-4273-B51B-6D64F7A8B309Q33179117-47C4AB09-C078-494F-8A78-F2DDC7469F82Q33289231-DB3A5EAB-EAC3-4CD5-80EF-98EF5B2F6C48Q33730583-E8B00187-0B54-4552-B0C6-1E4317CB45CBQ33786342-C680B942-DAE3-4575-B3E9-B76D7FB6470EQ33872971-4F49AEB8-415E-4963-96C2-E8B61AF5F033Q34094562-92B6F1F5-6311-49C3-9242-883F7E8D1F4FQ34402615-1220E24C-7DF5-4814-8C07-F3406711FA02Q34545340-4601304B-1527-441B-A888-E839C0170952Q34731104-EB05FA7F-30B5-4464-8F55-BEB5320482A5Q35574224-15920293-AF4D-4F06-8156-ABED9F5BA38EQ36004724-D1E2F40F-DBBB-404F-A615-5057AB4DFD24Q36255730-CAF14CE5-381C-4A08-BA6A-68455A217C5CQ36274038-666C11DC-FE9A-4940-B801-B8E41B8E917DQ36617945-747CDDD6-B7BB-4515-B482-7782BCD1CCD5Q36760245-82574C83-A0EC-43E7-B85B-2D56635B9DCFQ37211116-C4391E2C-E9F7-4463-B473-8A29111DDE7CQ37296321-63AC6E2C-2D7B-40F0-B922-72328E1C9125Q37338942-4362A49D-3F56-4A8E-B0AA-279B45A02196Q37690802-5D9326C6-A52D-4ADC-BE4A-E4C8AD159FB5Q37895982-E8E80F5F-341E-412F-A67F-CF31998D6C60Q38143977-8ED7EB88-97AD-41B0-B43E-BC39C2F3E20EQ38224193-DCCA0B5F-4830-4644-AE3D-38E780D2FA27Q38345793-34E7227C-BF29-490A-8E3D-B58AE25BA99BQ39120218-D39944D4-2D97-4E8D-9D47-1EBEE1E012F2Q39647831-F6C988DD-A203-4203-AB94-731C7BDA71EEQ39689348-09E13E94-942D-464B-93A0-C4AF76BC0483Q40318346-6E7A61E4-64FC-4BBA-83C0-9A3CE6F52229
P2860
Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes
description
1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1995
@ast
im Dezember 1995 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1995/12/22)
@sk
vědecký článek publikovaný v roce 1995
@cs
wetenschappelijk artikel (gepubliceerd op 1995/12/22)
@nl
наукова стаття, опублікована в грудні 1995
@uk
name
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@ast
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@en
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@nl
type
label
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@ast
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@en
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@nl
prefLabel
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@ast
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@en
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@nl
P2093
P2860
P356
P1476
Intermolecular autolytic cleav ...... gelatinase A by cell membranes
@en
P2093
J. J. Reynolds
M. J. Butler
R. V. Ward
S. J. Atkinson
P2860
P304
30479–30485
P356
10.1074/JBC.270.51.30479
P407
P577
1995-12-22T00:00:00Z