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Volumn 23, Issue 3, 2016, Pages 243-252

Membrane-anchored proteases in endothelial cell biology

Author keywords

ADAM; Angiotensin converting enzyme; Membrane tethered matrix metalloprotease; Membrane anchored serine protease; Pro protein convertase

Indexed keywords

MEMBRANE ANCHORED PROTEASE; PEPTIDE; PROTEIN TYROSINE KINASE; PROTEINASE; UNCLASSIFIED DRUG; SERINE PROTEINASE;

EID: 84959115305     PISSN: 10656251     EISSN: 15317048     Source Type: Journal    
DOI: 10.1097/MOH.0000000000000238     Document Type: Review
Times cited : (15)

References (99)
  • 1
    • 84897850189 scopus 로고    scopus 로고
    • Endothelium and its alterations in cardiovascular diseases: Life style intervention
    • Favero G, Paganelli C, Buffoli B, et al. Endothelium and its alterations in cardiovascular diseases: life style intervention. Biomed Res Int 2014; 2014:801896.
    • (2014) Biomed Res Int , vol.2014 , pp. 801896
    • Favero, G.1    Paganelli, C.2    Buffoli, B.3
  • 2
    • 84858280962 scopus 로고    scopus 로고
    • Proteolytic activation of the epithelial sodium channel and therapeutic application of a serine protease inhibitor for the treatment of salt-sensitive hypertension
    • Kitamura K, Tomita K. Proteolytic activation of the epithelial sodium channel and therapeutic application of a serine protease inhibitor for the treatment of salt-sensitive hypertension. Clin Exp Nephrol 2012; 16:44-48.
    • (2012) Clin Exp Nephrol , vol.16 , pp. 44-48
    • Kitamura, K.1    Tomita, K.2
  • 3
    • 58849147112 scopus 로고    scopus 로고
    • Camostat mesilate inhibits prostasin activity and reduces blood pressure and renal injury in salt-sensitive hypertension
    • Maekawa A, Kakizoe Y, Miyoshi T, et al. Camostat mesilate inhibits prostasin activity and reduces blood pressure and renal injury in salt-sensitive hypertension. J Hypertens 2009; 27:181-189.
    • (2009) J Hypertens , vol.27 , pp. 181-189
    • Maekawa, A.1    Kakizoe, Y.2    Miyoshi, T.3
  • 4
    • 50249083855 scopus 로고    scopus 로고
    • Prostasin: A possible candidate gene for human hypertension
    • Zhu H, Guo D, Li K, et al. Prostasin: a possible candidate gene for human hypertension. Am J Hypertens 2008; 21:1028-1033.
    • (2008) Am J Hypertens , vol.21 , pp. 1028-1033
    • Zhu, H.1    Guo, D.2    Li, K.3
  • 5
    • 84864148752 scopus 로고    scopus 로고
    • Mutations of the serine protease CAP1/Prss8 lead to reduced embryonic viability, skin defects, and decreased ENaC activity
    • Frateschi S, Keppner A, Malsure S, et al. Mutations of the serine protease CAP1/Prss8 lead to reduced embryonic viability, skin defects, and decreased ENaC activity. Am J Pathol 2012; 181:605-615.
    • (2012) Am J Pathol , vol.181 , pp. 605-615
    • Frateschi, S.1    Keppner, A.2    Malsure, S.3
  • 6
    • 77953667958 scopus 로고    scopus 로고
    • ENaC-mediated alveolar fluid clearance and lung fluid balance depend on the channel-activating protease. 1
    • Planes C, Randrianarison NH, Charles RP, et al. ENaC-mediated alveolar fluid clearance and lung fluid balance depend on the channel-activating protease 1. EMBO Mol Med 2010; 2:26-37.
    • (2010) EMBO Mol Med , vol.2 , pp. 26-37
    • Planes, C.1    Randrianarison, N.H.2    Charles, R.P.3
  • 7
    • 23744513344 scopus 로고    scopus 로고
    • The epidermal barrier function is dependent on the serine protease CAP1/Prss8
    • Leyvraz C, Charles RP, Rubera I, et al. The epidermal barrier function is dependent on the serine protease CAP1/Prss8. J Cell Biol 2005; 170:487-496.
    • (2005) J Cell Biol , vol.170 , pp. 487-496
    • Leyvraz, C.1    Charles, R.P.2    Rubera, I.3
  • 8
    • 84896341078 scopus 로고    scopus 로고
    • The serine protease prostasin regulates hepatic insulin sensitivity by modulating TLR4 signalling
    • Uchimura K, Hayata M, Mizumoto T, et al. The serine protease prostasin regulates hepatic insulin sensitivity by modulating TLR4 signalling. Nat Commun 2014; 5:3428.
    • (2014) Nat Commun , vol.5 , pp. 3428
    • Uchimura, K.1    Hayata, M.2    Mizumoto, T.3
  • 9
    • 77749239665 scopus 로고    scopus 로고
    • Membrane-anchored serine protease matriptase regulates epithelial barrier formation and permeability in the intestine
    • Buzza MS, Netzel-Arnett S, Shea-Donohue T, et al. Membrane-anchored serine protease matriptase regulates epithelial barrier formation and permeability in the intestine. Proc Natl Acad Sci U S A 2010; 107:4200-4205.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4200-4205
    • Buzza, M.S.1    Netzel-Arnett, S.2    Shea-Donohue, T.3
  • 10
    • 79955478095 scopus 로고    scopus 로고
    • C-Met-induced epithelial carcinogenesis is initiated by the serine protease matriptase
    • Szabo R, Rasmussen AL, Moyer AB, et al. c-Met-induced epithelial carcinogenesis is initiated by the serine protease matriptase. Oncogene 2011; 30:2003-2016.
    • (2011) Oncogene , vol.30 , pp. 2003-2016
    • Szabo, R.1    Rasmussen, A.L.2    Moyer, A.B.3
  • 11
    • 73549091040 scopus 로고    scopus 로고
    • Epithelial integrity is maintained by a matriptasedependent proteolytic pathway
    • List K, Kosa P, Szabo R, et al. Epithelial integrity is maintained by a matriptasedependent proteolytic pathway. Am J Pathol 2009; 175:1453-1463.
    • (2009) Am J Pathol , vol.175 , pp. 1453-1463
    • List, K.1    Kosa, P.2    Szabo, R.3
  • 12
    • 84904626934 scopus 로고    scopus 로고
    • The role of TMPRSS6/matriptase-2 in iron regulation and anemia
    • Wang CY, Meynard D, Lin HY. The role of TMPRSS6/matriptase-2 in iron regulation and anemia. Front Pharmacol 2014; 5:114.
    • (2014) Front Pharmacol , vol.5 , pp. 114
    • Wang, C.Y.1    Meynard, D.2    Lin, H.Y.3
  • 13
    • 84873059706 scopus 로고    scopus 로고
    • Matriptase-2 inhibits HECV motility and tubule formation in vitro and tumour angiogenesis in vivo
    • Webb SL, Sanders AJ, Mason MD, Jiang WG. Matriptase-2 inhibits HECV motility and tubule formation in vitro and tumour angiogenesis in vivo. Mol Cell Biochem 2013; 375:207-217.
    • (2013) Mol Cell Biochem , vol.375 , pp. 207-217
    • Webb, S.L.1    Sanders, A.J.2    Mason, M.D.3    Jiang, W.G.4
  • 14
    • 84887020390 scopus 로고    scopus 로고
    • Corin: A new player in the regulation of saltwater balance and blood pressure
    • Armaly Z, Assady S, Abassi Z. Corin: a new player in the regulation of saltwater balance and blood pressure. Curr Opin Nephrol Hypertens 2013; 22:713-722.
    • (2013) Curr Opin Nephrol Hypertens , vol.22 , pp. 713-722
    • Armaly, Z.1    Assady, S.2    Abassi, Z.3
  • 15
    • 84893764200 scopus 로고    scopus 로고
    • Corin in natriuretic peptide processing and hypertension
    • Zhou Y, Wu Q. Corin in natriuretic peptide processing and hypertension. Curr Hypertens Rep 2014; 16:415.
    • (2014) Curr Hypertens Rep , vol.16 , pp. 415
    • Zhou, Y.1    Wu, Q.2
  • 16
    • 84862778346 scopus 로고    scopus 로고
    • Role of corin in trophoblast invasion and uterine spiral artery remodelling in pregnancy
    • Cui Y, Wang W, Dong N, et al. Role of corin in trophoblast invasion and uterine spiral artery remodelling in pregnancy. Nature 2012; 484:246-250.
    • (2012) Nature , vol.484 , pp. 246-250
    • Cui, Y.1    Wang, W.2    Dong, N.3
  • 17
    • 0032443652 scopus 로고    scopus 로고
    • Failure of ventral closure and axial rotation in embryos lacking the proprotein convertase Furin
    • Roebroek AJ, Umans L, Pauli IG, et al. Failure of ventral closure and axial rotation in embryos lacking the proprotein convertase Furin. Development 1998; 125:4863-4876.
    • (1998) Development , vol.125 , pp. 4863-4876
    • Roebroek, A.J.1    Umans, L.2    Pauli, I.G.3
  • 18
    • 84866280245 scopus 로고    scopus 로고
    • Loss of endothelial furin leads to cardiac malformation and early postnatal death
    • Kim W, Essalmani R, Szumska D, et al. Loss of endothelial furin leads to cardiac malformation and early postnatal death. Mol Cell Biol 2012; 32:3382-3391.
    • (2012) Mol Cell Biol , vol.32 , pp. 3382-3391
    • Kim, W.1    Essalmani, R.2    Szumska, D.3
  • 19
    • 84879404228 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitors and their effects on the cardiovascular system
    • Solun B, Marcoviciu D, Dicker D. Dipeptidyl peptidase-4 inhibitors and their effects on the cardiovascular system. Curr Cardiol Rep 2013; 15:382.
    • (2013) Curr Cardiol Rep , vol.15 , pp. 382
    • Solun, B.1    Marcoviciu, D.2    Dicker, D.3
  • 20
    • 84946560133 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 regulation of SDF-1/CXCR4 axis: Implications for cardiovascular disease
    • Zhong J, Rajagopalan S. Dipeptidyl peptidase-4 regulation of SDF-1/CXCR4 axis: implications for cardiovascular disease. Front Immunol 2015; 6:477.
    • (2015) Front Immunol , vol.6 , pp. 477
    • Zhong, J.1    Rajagopalan, S.2
  • 21
    • 77951168113 scopus 로고    scopus 로고
    • Genetic deletion or pharmacological inhibition of dipeptidyl peptidase-4 improves cardiovascular outcomes after myocardial infarction in mice
    • Sauve M, Ban K, Momen MA, et al. Genetic deletion or pharmacological inhibition of dipeptidyl peptidase-4 improves cardiovascular outcomes after myocardial infarction in mice. Diabetes 2010; 59:1063-1073.
    • (2010) Diabetes , vol.59 , pp. 1063-1073
    • Sauve, M.1    Ban, K.2    Momen, M.A.3
  • 22
    • 79951677095 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition attenuates blood pressure rising in young spontaneously hypertensive rats
    • Pacheco BP, Crajoinas RO, Couto GK, et al. Dipeptidyl peptidase IV inhibition attenuates blood pressure rising in young spontaneously hypertensive rats. J Hypertens 2011; 29:520-528.
    • (2011) J Hypertens , vol.29 , pp. 520-528
    • Pacheco, B.P.1    Crajoinas, R.O.2    Couto, G.K.3
  • 23
    • 42349114587 scopus 로고    scopus 로고
    • Endothelial sprouting and angiogenesis: Matrix metalloproteinases in the lead
    • van Hinsbergh VW, Koolwijk P. Endothelial sprouting and angiogenesis: matrix metalloproteinases in the lead. Cardiovasc Res 2008; 78:203-212.
    • (2008) Cardiovasc Res , vol.78 , pp. 203-212
    • Van Hinsbergh, V.W.1    Koolwijk, P.2
  • 25
    • 84880174251 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Inflammatory regulators of cell behaviors in vascular formation and remodeling
    • Chen Q, Jin M, Yang F, et al. Matrix metalloproteinases: inflammatory regulators of cell behaviors in vascular formation and remodeling. Mediators Inflamm 2013; 2013:928315.
    • (2013) Mediators Inflamm , vol.2013 , pp. 928315
    • Chen, Q.1    Jin, M.2    Yang, F.3
  • 26
    • 84937723140 scopus 로고    scopus 로고
    • Deficiency of MMP17/MT4-MMP proteolytic activity predisposes to aortic aneurysm in mice
    • Martin-Alonso M, Garcia-Redondo AB, Guo D, et al. Deficiency of MMP17/MT4-MMP proteolytic activity predisposes to aortic aneurysm in mice. Circ Res 2015; 117:e13-e26.
    • (2015) Circ Res , vol.117 , pp. e13-e26
    • Martin-Alonso, M.1    Garcia-Redondo, A.B.2    Guo, D.3
  • 28
    • 77954563151 scopus 로고    scopus 로고
    • ADAM8 is a negative regulator of retinal neovascularization and of the growth of heterotopically injected tumor cells in mice
    • Guaiquil VH, Swendeman S, Zhou W, et al. ADAM8 is a negative regulator of retinal neovascularization and of the growth of heterotopically injected tumor cells in mice. J Mol Med (Berl) 2010; 88:497-505.
    • (2010) J Mol Med (Berl) , vol.88 , pp. 497-505
    • Guaiquil, V.H.1    Swendeman, S.2    Zhou, W.3
  • 29
    • 84893770998 scopus 로고    scopus 로고
    • ADAM8 expression in invasive breast cancer promotes tumor dissemination and metastasis
    • Romagnoli M, Mineva ND, Polmear M, et al. ADAM8 expression in invasive breast cancer promotes tumor dissemination and metastasis. EMBO Mol Med 2014; 6:278-294.
    • (2014) EMBO Mol Med , vol.6 , pp. 278-294
    • Romagnoli, M.1    Mineva, N.D.2    Polmear, M.3
  • 30
    • 66349106575 scopus 로고    scopus 로고
    • ADAM9 is involved in pathological retinal neovascularization
    • Guaiquil V, Swendeman S, Yoshida T, et al. ADAM9 is involved in pathological retinal neovascularization. Mol Cell Biol 2009; 29:2694-2703.
    • (2009) Mol Cell Biol , vol.29 , pp. 2694-2703
    • Guaiquil, V.1    Swendeman, S.2    Yoshida, T.3
  • 31
    • 79961009646 scopus 로고    scopus 로고
    • Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures
    • Glomski K, Monette S, Manova K, et al. Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures. Blood 2011; 118:1163-1174.
    • (2011) Blood , vol.118 , pp. 1163-1174
    • Glomski, K.1    Monette, S.2    Manova, K.3
  • 32
    • 84920097040 scopus 로고    scopus 로고
    • ADAM10 and ADAM17 have opposite roles during sprouting angiogenesis
    • Caolo V, Swennen G, Chalaris A, et al. ADAM10 and ADAM17 have opposite roles during sprouting angiogenesis. Angiogenesis 2015; 18:13-22.
    • (2015) Angiogenesis , vol.18 , pp. 13-22
    • Caolo, V.1    Swennen, G.2    Chalaris, A.3
  • 33
    • 84940757010 scopus 로고    scopus 로고
    • ADAM12: A genetic modifier of preclinical peripheral arterial disease
    • Dokun AO, Chen L, Okutsu M, et al. ADAM12: a genetic modifier of preclinical peripheral arterial disease. Am J Physiol Heart Circ Physiol 2015; 309:H790-H803.
    • (2015) Am J Physiol Heart Circ Physiol , vol.309 , pp. H790-H803
    • Dokun, A.O.1    Chen, L.2    Okutsu, M.3
  • 34
    • 84938771822 scopus 로고    scopus 로고
    • ADAM12 and ADAM17 are essential molecules for hypoxia-induced impairment of neural vascular barrier function
    • Cui D, Arima M, Takubo K, et al. ADAM12 and ADAM17 are essential molecules for hypoxia-induced impairment of neural vascular barrier function. Sci Rep 2015; 5:12796.
    • (2015) Sci Rep , vol.5 , pp. 12796
    • Cui, D.1    Arima, M.2    Takubo, K.3
  • 35
    • 84866625277 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase 15 contributes to atherosclerosis by mediating endothelial barrier dysfunction via Src family kinase activity
    • Sun C, Wu MH, Lee ES, Yuan SY. A disintegrin and metalloproteinase 15 contributes to atherosclerosis by mediating endothelial barrier dysfunction via Src family kinase activity. Arterioscler Thromb Vasc Biol 2012; 32:2444-2451.
    • (2012) Arterioscler Thromb Vasc Biol , vol.32 , pp. 2444-2451
    • Sun, C.1    Wu, M.H.2    Lee, E.S.3    Yuan, S.Y.4
  • 36
    • 84873333125 scopus 로고    scopus 로고
    • ADAM15 deficiency attenuates pulmonary hyperpermeability and acute lung injury in lipopolysaccharide-treated mice
    • Sun C, Beard RS Jr, McLean DL, et al. ADAM15 deficiency attenuates pulmonary hyperpermeability and acute lung injury in lipopolysaccharide-treated mice. Am J Physiol Lung Cell Mol Physiol 2013; 304:L135-L142.
    • (2013) Am J Physiol Lung Cell Mol Physiol , vol.304 , pp. L135-L142
    • Sun, C.1    Beard, R.S.2    McLean, D.L.3
  • 37
    • 84924246465 scopus 로고    scopus 로고
    • Characterization of oxygen-induced retinopathy in mice carrying an inactivating point mutation in the catalytic site of ADAM15
    • Maretzky T, Blobel CP, Guaiquil V. Characterization of oxygen-induced retinopathy in mice carrying an inactivating point mutation in the catalytic site of ADAM15. Invest Ophthalmol Vis Sci 2014; 55:6774-6782.
    • (2014) Invest Ophthalmol Vis Sci , vol.55 , pp. 6774-6782
    • Maretzky, T.1    Blobel, C.P.2    Guaiquil, V.3
  • 38
    • 77950889362 scopus 로고    scopus 로고
    • Pathological neovascularization is reduced by inactivation of ADAM17 in endothelial cells but not in pericytes
    • Weskamp G, Mendelson K, Swendeman S, et al. Pathological neovascularization is reduced by inactivation of ADAM17 in endothelial cells but not in pericytes. Circ Res 2010; 106:932-940.
    • (2010) Circ Res , vol.106 , pp. 932-940
    • Weskamp, G.1    Mendelson, K.2    Swendeman, S.3
  • 39
    • 77954309262 scopus 로고    scopus 로고
    • ADAM33 expression in atherosclerotic lesions and relationship of ADAM33 gene variation with atherosclerosis
    • Holloway JW, Laxton RC, Rose-Zerilli MJ, et al. ADAM33 expression in atherosclerotic lesions and relationship of ADAM33 gene variation with atherosclerosis. Atherosclerosis 2010; 211:224-230.
    • (2010) Atherosclerosis , vol.211 , pp. 224-230
    • Holloway, J.W.1    Laxton, R.C.2    Rose-Zerilli, M.J.3
  • 40
    • 33745831888 scopus 로고    scopus 로고
    • The genetics of asthma: ADAM33 as an example of a susceptibility gene
    • Holgate ST, Yang Y, Haitchi HM, et al. The genetics of asthma: ADAM33 as an example of a susceptibility gene. Proc Am Thorac Soc 2006; 3:440-443.
    • (2006) Proc Am Thorac Soc , vol.3 , pp. 440-443
    • Holgate, S.T.1    Yang, Y.2    Haitchi, H.M.3
  • 41
    • 44649176263 scopus 로고    scopus 로고
    • The soluble form of a disintegrin and metalloprotease 33 promotes angiogenesis: Implications for airway remodeling in asthma
    • Puxeddu I, Pang YY, Harvey A, et al. The soluble form of a disintegrin and metalloprotease 33 promotes angiogenesis: implications for airway remodeling in asthma. J Allergy Clin Immunol 2008; 121:1400-1406.
    • (2008) J Allergy Clin Immunol , vol.121 , pp. 1400-1406
    • Puxeddu, I.1    Pang, Y.Y.2    Harvey, A.3
  • 42
    • 84930169739 scopus 로고    scopus 로고
    • Hypertension: Renin-angiotensin-aldosterone system alterations
    • Te RL, van Esch JH, Roks AJ, et al. Hypertension: renin-angiotensin-aldosterone system alterations. Circ Res 2015; 116:960-975.
    • (2015) Circ Res , vol.116 , pp. 960-975
    • Te, R.L.1    Van Esch, J.H.2    Roks, A.J.3
  • 44
    • 84940841802 scopus 로고    scopus 로고
    • ACE2 and vasoactive peptides: Novel players in cardiovascular/renal remodeling and hypertension
    • Mendoza-Torres E, Oyarzun A, Mondaca-Ruff D, et al. ACE2 and vasoactive peptides: novel players in cardiovascular/renal remodeling and hypertension. Ther Adv Cardiovasc Dis 2015; 9:217-237.
    • (2015) Ther Adv Cardiovasc Dis , vol.9 , pp. 217-237
    • Mendoza-Torres, E.1    Oyarzun, A.2    Mondaca-Ruff, D.3
  • 45
    • 84926509411 scopus 로고    scopus 로고
    • Renin-angiotensin system in the kidney: What is new?
    • Ferrao FM, Lara LS, Lowe J. Renin-angiotensin system in the kidney: what is new? World J Nephrol 2014; 3:64-76.
    • (2014) World J Nephrol , vol.3 , pp. 64-76
    • Ferrao, F.M.1    Lara, L.S.2    Lowe, J.3
  • 46
    • 69949118724 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases
    • Bugge TH, Antalis TM, Wu Q. Type II transmembrane serine proteases. J Biol Chem 2009; 284:23177-23181.
    • (2009) J Biol Chem , vol.284 , pp. 23177-23181
    • Bugge, T.H.1    Antalis, T.M.2    Wu, Q.3
  • 47
    • 84930752520 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases: Their functions and regulations
    • Itoh Y. Membrane-type matrix metalloproteinases: their functions and regulations. Matrix Biol 2015; 44-46:207-223.
    • (2015) Matrix Biol , vol.44-46 , pp. 207-223
    • Itoh, Y.1
  • 48
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals DF, Courtneidge SA. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 2003; 17:7-30.
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 49
    • 78751637146 scopus 로고    scopus 로고
    • Membrane-anchored serine proteases in health and disease
    • Antalis TM, Bugge TH, Wu Q. Membrane-anchored serine proteases in health and disease. Prog Mol Biol Transl Sci 2011; 99:1-50.
    • (2011) Prog Mol Biol Transl Sci , vol.99 , pp. 1-50
    • Antalis, T.M.1    Bugge, T.H.2    Wu, Q.3
  • 50
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas G. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat Rev Mol Cell Biol 2002; 3:753-766.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 753-766
    • Thomas, G.1
  • 51
  • 52
    • 84879192166 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme 2 (ACE2) is a key modulator of the renin angiotensin system in health and disease
    • Tikellis C, Thomas MC. Angiotensin-converting enzyme 2 (ACE2) is a key modulator of the renin angiotensin system in health and disease. Int J Pept 2012; 2012:256294.
    • (2012) Int J Pept , vol.2012 , pp. 256294
    • Tikellis, C.1    Thomas, M.C.2
  • 53
    • 84907898299 scopus 로고    scopus 로고
    • Shedding of epithin/PRSS14 is induced by TGF-beta and mediated by tumor necrosis factor-alpha converting enzyme
    • Lee HS, Park BM, Cho Y, et al. Shedding of epithin/PRSS14 is induced by TGF-beta and mediated by tumor necrosis factor-alpha converting enzyme. Biochem Biophys Res Commun 2014; 452:1084-1090.
    • (2014) Biochem Biophys Res Commun , vol.452 , pp. 1084-1090
    • Lee, H.S.1    Park, B.M.2    Cho, Y.3
  • 54
    • 77954915960 scopus 로고    scopus 로고
    • The cutting edge: Membraneanchored serine protease activities in the pericellular microenvironment
    • Antalis TM, Buzza MS, Hodge KM, et al. The cutting edge: membraneanchored serine protease activities in the pericellular microenvironment. Biochem J 2010; 428:325-346.
    • (2010) Biochem J , vol.428 , pp. 325-346
    • Antalis, T.M.1    Buzza, M.S.2    Hodge, K.M.3
  • 55
    • 0033944447 scopus 로고    scopus 로고
    • Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases
    • Yana I, Weiss SJ. Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases. Mol Biol Cell 2000; 11:2387-2401.
    • (2000) Mol Biol Cell , vol.11 , pp. 2387-2401
    • Yana, I.1    Weiss, S.J.2
  • 57
    • 84929093820 scopus 로고    scopus 로고
    • The functional maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 requires processing at a newly identified proprotein convertase (PC) cleavage site
    • Wong E, Maretzky T, Peleg Y, et al. The functional maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 requires processing at a newly identified proprotein convertase (PC) cleavage site. J Biol Chem 2015; 290:12135-12146.
    • (2015) J Biol Chem , vol.290 , pp. 12135-12146
    • Wong, E.1    Maretzky, T.2    Peleg, Y.3
  • 58
    • 84946549613 scopus 로고    scopus 로고
    • Deletions in the cytoplasmic domain of iRhom1 and iRhom2 promote shedding of the TNF receptor by the protease ADAM17
    • Maney SK, McIlwain DR, Polz R, et al. Deletions in the cytoplasmic domain of iRhom1 and iRhom2 promote shedding of the TNF receptor by the protease ADAM17. Sci Signal 2015; 8:ra109.
    • (2015) Sci Signal , vol.8 , pp. ra109
    • Maney, S.K.1    McIlwain, D.R.2    Polz, R.3
  • 59
    • 84879560367 scopus 로고    scopus 로고
    • A matriptase-prostasin reciprocal zymogen activation complex with unique features: Prostasin as a nonenzymatic co-factor for matriptase activation
    • Friis S, Uzzun SK, Godiksen S, et al. A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a nonenzymatic co-factor for matriptase activation. J Biol Chem 2013; 288:19028-19039.
    • (2013) J Biol Chem , vol.288 , pp. 19028-19039
    • Friis, S.1    Uzzun, S.K.2    Godiksen, S.3
  • 60
    • 84901405942 scopus 로고    scopus 로고
    • The membrane-anchored serine protease prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity
    • Peters DE, Szabo R, Friis S, et al. The membrane-anchored serine protease prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity. J Biol Chem 2014; 289:14740-14749.
    • (2014) J Biol Chem , vol.289 , pp. 14740-14749
    • Peters, D.E.1    Szabo, R.2    Friis, S.3
  • 61
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: Key components in EGFR signalling and development
    • Blobel CP. ADAMs: key components in EGFR signalling and development. Nat Rev Mol Cell Biol 2005; 6:32-43.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 32-43
    • Blobel, C.P.1
  • 62
    • 84866487100 scopus 로고    scopus 로고
    • Ectodomain shedding and ADAMs in development
    • Weber S, Saftig P. Ectodomain shedding and ADAMs in development. Development 2012; 139:3693-3709.
    • (2012) Development , vol.139 , pp. 3693-3709
    • Weber, S.1    Saftig, P.2
  • 63
    • 56749133149 scopus 로고    scopus 로고
    • The ADAMs: Signalling scissors in the tumour microenvironment
    • Murphy G. The ADAMs: signalling scissors in the tumour microenvironment. Nat Rev Cancer 2008; 8:929-941.
    • (2008) Nat Rev Cancer , vol.8 , pp. 929-941
    • Murphy, G.1
  • 64
    • 63649128433 scopus 로고    scopus 로고
    • Regulation of the proteolytic disintegrin metalloproteinases, the 'Sheddases'
    • Murphy G. Regulation of the proteolytic disintegrin metalloproteinases, the 'Sheddases'. Semin Cell Dev Biol 2009; 20:138-145.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 138-145
    • Murphy, G.1
  • 66
    • 84943347613 scopus 로고    scopus 로고
    • MT1-MMP recognition by ERM proteins and its implication in CD44 shedding
    • Terawaki S, Kitano K, Aoyama M, et al. MT1-MMP recognition by ERM proteins and its implication in CD44 shedding. Genes Cells 2015; 20:847-859.
    • (2015) Genes Cells , vol.20 , pp. 847-859
    • Terawaki, S.1    Kitano, K.2    Aoyama, M.3
  • 67
    • 84913592386 scopus 로고    scopus 로고
    • Cytoskeletal confinement of CX3CL1 limits its susceptibility to proteolytic cleavage by ADAM10
    • Wong HS, Jaumouille V, Heit B, et al. Cytoskeletal confinement of CX3CL1 limits its susceptibility to proteolytic cleavage by ADAM10. Mol Biol Cell 2014; 25:3884-3899.
    • (2014) Mol Biol Cell , vol.25 , pp. 3884-3899
    • Wong, H.S.1    Jaumouille, V.2    Heit, B.3
  • 68
    • 0037340473 scopus 로고    scopus 로고
    • Endothelial cell serine proteases expressed during vascular morphogenesis and angiogenesis
    • Aimes RT, Zijlstra A, Hooper JD, et al. Endothelial cell serine proteases expressed during vascular morphogenesis and angiogenesis. Thromb Haemost 2003; 89:561-572.
    • (2003) Thromb Haemost , vol.89 , pp. 561-572
    • Aimes, R.T.1    Zijlstra, A.2    Hooper, J.D.3
  • 69
    • 84922287405 scopus 로고    scopus 로고
    • Proteolytic activation of the protease-activated receptor (PAR)-2 by the glycosylphosphatidylinositol-anchored serine protease testisin
    • Driesbaugh KH, Buzza MS, Martin EW, et al. Proteolytic activation of the protease-activated receptor (PAR)-2 by the glycosylphosphatidylinositol-anchored serine protease testisin. J Biol Chem 2015; 290:3529-3541.
    • (2015) J Biol Chem , vol.290 , pp. 3529-3541
    • Driesbaugh, K.H.1    Buzza, M.S.2    Martin, E.W.3
  • 70
    • 34249307505 scopus 로고    scopus 로고
    • Modulation of tissue factor-factor VIIa signaling by lipid rafts and caveolae
    • Awasthi V, Mandal SK, Papanna V, et al. Modulation of tissue factor-factor VIIa signaling by lipid rafts and caveolae. Arterioscler Thromb Vasc Biol 2007; 27:1447-1455.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 1447-1455
    • Awasthi, V.1    Mandal, S.K.2    Papanna, V.3
  • 71
    • 43749120051 scopus 로고    scopus 로고
    • Lipid raft localization regulates the cleavage specificity of protease activated receptor 1 in endothelial cells
    • Bae JS, Yang L, Rezaie AR. Lipid raft localization regulates the cleavage specificity of protease activated receptor 1 in endothelial cells. J Thromb Haemost 2008; 6:954-961.
    • (2008) J Thromb Haemost , vol.6 , pp. 954-961
    • Bae, J.S.1    Yang, L.2    Rezaie, A.R.3
  • 72
    • 39849104321 scopus 로고    scopus 로고
    • Endothelial adherens and tight junctions in vascular homeostasis, inflammation and angiogenesis
    • Wallez Y, Huber P. Endothelial adherens and tight junctions in vascular homeostasis, inflammation and angiogenesis. Biochim Biophys Acta 2008; 1778:794-809.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 794-809
    • Wallez, Y.1    Huber, P.2
  • 73
    • 42649105392 scopus 로고    scopus 로고
    • Tight junctions contain oligomeric protein assembly critical for maintaining blood-brain barrier integrity in vivo
    • McCaffrey G, Staatz WD, Quigley CA, et al. Tight junctions contain oligomeric protein assembly critical for maintaining blood-brain barrier integrity in vivo. J Neurochem 2007; 103:2540-2555.
    • (2007) J Neurochem , vol.103 , pp. 2540-2555
    • McCaffrey, G.1    Staatz, W.D.2    Quigley, C.A.3
  • 74
    • 66549086638 scopus 로고    scopus 로고
    • Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases
    • Koenen RR, Pruessmeyer J, Soehnlein O, et al. Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases. Blood 2009; 113:4799-4809.
    • (2009) Blood , vol.113 , pp. 4799-4809
    • Koenen, R.R.1    Pruessmeyer, J.2    Soehnlein, O.3
  • 75
    • 77954317110 scopus 로고    scopus 로고
    • ADAM15 regulates endothelial permeability and neutrophil migration via Src/ERK1/2 signalling
    • Sun C, Wu MH, Guo M, et al. ADAM15 regulates endothelial permeability and neutrophil migration via Src/ERK1/2 signalling. Cardiovasc Res 2010; 87:348-355.
    • (2010) Cardiovasc Res , vol.87 , pp. 348-355
    • Sun, C.1    Wu, M.H.2    Guo, M.3
  • 76
    • 84908045063 scopus 로고    scopus 로고
    • MicroRNA-147b regulates vascular endothelial barrier function by targeting ADAM15 expression
    • Chatterjee V, Beard RS Jr, Reynolds JJ, et al. MicroRNA-147b regulates vascular endothelial barrier function by targeting ADAM15 expression. PLoS One 2014; 9:e110286.
    • (2014) PLoS One , vol.9 , pp. e110286
    • Chatterjee, V.1    Beard, R.S.2    Reynolds, J.J.3
  • 77
    • 84894483331 scopus 로고    scopus 로고
    • Control of vascular permeability by atrial natriuretic peptide via a GEF-H1-dependent mechanism
    • Tian X, Tian Y, Gawlak G, et al. Control of vascular permeability by atrial natriuretic peptide via a GEF-H1-dependent mechanism. J Biol Chem 2014; 289:5168-5183.
    • (2014) J Biol Chem , vol.289 , pp. 5168-5183
    • Tian, X.1    Tian, Y.2    Gawlak, G.3
  • 78
    • 84877823830 scopus 로고    scopus 로고
    • ACE2, angiotensin-(1-7) and Mas receptor axis in inflammation and fibrosis
    • Simoes e Silva AC, Silveira KD, Ferreira AJ, et al. ACE2, angiotensin-(1-7) and Mas receptor axis in inflammation and fibrosis. Br J Pharmacol 2013; 169:477-492.
    • (2013) Br J Pharmacol , vol.169 , pp. 477-492
    • Simoes-E-Silva, A.C.1    Silveira, K.D.2    Ferreira, A.J.3
  • 79
    • 84925486259 scopus 로고    scopus 로고
    • ACE2 and Ang-(1-7) protect endothelial cell function and prevent early atherosclerosis by inhibiting inflammatory response
    • Zhang YH, Zhang YH, Dong XF, et al. ACE2 and Ang-(1-7) protect endothelial cell function and prevent early atherosclerosis by inhibiting inflammatory response. Inflamm Res 2015; 64:253-260.
    • (2015) Inflamm Res , vol.64 , pp. 253-260
    • Zhang, Y.H.1    Zhang, Y.H.2    Dong, X.F.3
  • 80
    • 84952001288 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of HGF/Met in the cardiovascular system
    • Gallo S, Sala V, Gatti S, Crepaldi T. Cellular and molecular mechanisms of HGF/Met in the cardiovascular system. Clin Sci (Lond) 2015; 129:1173-1193.
    • (2015) Clin Sci (Lond) , vol.129 , pp. 1173-1193
    • Gallo, S.1    Sala, V.2    Gatti, S.3    Crepaldi, T.4
  • 81
    • 1442358746 scopus 로고    scopus 로고
    • Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
    • Sahin U, Weskamp G, Kelly K, et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J Cell Biol 2004; 164:769-779.
    • (2004) J Cell Biol , vol.164 , pp. 769-779
    • Sahin, U.1    Weskamp, G.2    Kelly, K.3
  • 82
    • 0032515018 scopus 로고    scopus 로고
    • An essential role for ectodomain shedding in mammalian development
    • Peschon JJ, Slack JL, Reddy P, et al. An essential role for ectodomain shedding in mammalian development. Science 1998; 282:1281-1284.
    • (1998) Science , vol.282 , pp. 1281-1284
    • Peschon, J.J.1    Slack, J.L.2    Reddy, P.3
  • 83
    • 0037507267 scopus 로고    scopus 로고
    • Defective valvulogenesis in HBEGF and TACE-null mice is associated with aberrant BMP signaling
    • Jackson LF, Qiu TH, Sunnarborg SW, et al. Defective valvulogenesis in HBEGF and TACE-null mice is associated with aberrant BMP signaling. EMBO J 2003; 22:2704-2716.
    • (2003) EMBO J , vol.22 , pp. 2704-2716
    • Jackson, L.F.1    Qiu, T.H.2    Sunnarborg, S.W.3
  • 84
    • 33745714456 scopus 로고    scopus 로고
    • ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors
    • Ohtsu H, Dempsey PJ, Eguchi S. ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors. Am J Physiol Cell Physiol 2006; 291:C1-C10.
    • (2006) Am J Physiol Cell Physiol , vol.291 , pp. C1-C10
    • Ohtsu, H.1    Dempsey, P.J.2    Eguchi, S.3
  • 85
    • 84927924551 scopus 로고    scopus 로고
    • Heterotrimeric G proteins directly regulate MMP14/membrane type-1 matrix metalloprotease: A novel mechanism for GPCREGFR transactivation
    • Overland AC, Insel PA. Heterotrimeric G proteins directly regulate MMP14/membrane type-1 matrix metalloprotease: a novel mechanism for GPCREGFR transactivation. J Biol Chem 2015; 290:9941-9947.
    • (2015) J Biol Chem , vol.290 , pp. 9941-9947
    • Overland, A.C.1    Insel, P.A.2
  • 86
    • 0032582686 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins
    • Hiraoka N, Allen E, Apel IJ, et al. Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins. Cell 1998; 95:365-377.
    • (1998) Cell , vol.95 , pp. 365-377
    • Hiraoka, N.1    Allen, E.2    Apel, I.J.3
  • 87
    • 0037017385 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) regulate fibrin-invasive activity via MT1-MMP-dependent and -independent processes
    • Hotary KB, Yana I, Sabeh F, et al. Matrix metalloproteinases (MMPs) regulate fibrin-invasive activity via MT1-MMP-dependent and -independent processes. J Exp Med 2002; 195:295-308.
    • (2002) J Exp Med , vol.195 , pp. 295-308
    • Hotary, K.B.1    Yana, I.2    Sabeh, F.3
  • 88
    • 84937764835 scopus 로고    scopus 로고
    • Fluid shear stress promotes proprotein convertase-dependent activation of MT1-MMP
    • Kang H, Duran CL, Abbey CA, et al. Fluid shear stress promotes proprotein convertase-dependent activation of MT1-MMP. Biochem Biophys Res Commun 2015; 460:596-602.
    • (2015) Biochem Biophys Res Commun , vol.460 , pp. 596-602
    • Kang, H.1    Duran, C.L.2    Abbey, C.A.3
  • 89
    • 34249744576 scopus 로고    scopus 로고
    • Crosstalk between neovessels and mural cells directs the site-specific expression of MT1-MMP to endothelial tip cells
    • Yana I, Sagara H, Takaki S, et al. Crosstalk between neovessels and mural cells directs the site-specific expression of MT1-MMP to endothelial tip cells. J Cell Sci 2007; 120:1607-1614.
    • (2007) J Cell Sci , vol.120 , pp. 1607-1614
    • Yana, I.1    Sagara, H.2    Takaki, S.3
  • 90
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • Itoh Y, Takamura A, Ito N, et al. Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J 2001; 20:4782-4793.
    • (2001) EMBO J , vol.20 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3
  • 91
    • 84962945253 scopus 로고    scopus 로고
    • A novel role of endothelium in activation of latent pro-membrane type 1 matrix metalloproteinase and pro-matrix metalloproteinase-2 in rat aorta
    • [Epub ahead of print]
    • Otto S, Deussen A, Zatschler B, et al. A novel role of endothelium in activation of latent pro-membrane type 1 matrix metalloproteinase and pro-matrix metalloproteinase-2 in rat aorta. Cardiovasc Res 2015. [Epub ahead of print]
    • (2015) Cardiovasc Res
    • Otto, S.1    Deussen, A.2    Zatschler, B.3
  • 92
    • 84991444240 scopus 로고    scopus 로고
    • Functional relationship between matrix metalloproteinase-11 and matrix metalloproteinase-14
    • Buache E, Thai R, Wendling C, et al. Functional relationship between matrix metalloproteinase-11 and matrix metalloproteinase-14. Cancer Med 2014; 3:1197-1210.
    • (2014) Cancer Med , vol.3 , pp. 1197-1210
    • Buache, E.1    Thai, R.2    Wendling, C.3
  • 93
    • 2642516344 scopus 로고    scopus 로고
    • Membrane associated proteases and their inhibitors in tumour angiogenesis
    • Noel A, Maillard C, Rocks N, et al. Membrane associated proteases and their inhibitors in tumour angiogenesis. J Clin Pathol 2004; 57:577-584.
    • (2004) J Clin Pathol , vol.57 , pp. 577-584
    • Noel, A.1    Maillard, C.2    Rocks, N.3
  • 94
    • 80051924091 scopus 로고    scopus 로고
    • Characterization of the differential response of endothelial cells exposed to normal and elevated laminar shear stress
    • White SJ, Hayes EM, Lehoux S, et al. Characterization of the differential response of endothelial cells exposed to normal and elevated laminar shear stress. J Cell Physiol 2011; 226:2841-2848.
    • (2011) J Cell Physiol , vol.226 , pp. 2841-2848
    • White, S.J.1    Hayes, E.M.2    Lehoux, S.3
  • 95
    • 79955497166 scopus 로고    scopus 로고
    • Sema3E-PlexinD1 signaling selectively suppresses disoriented angiogenesis in ischemic retinopathy in mice
    • Fukushima Y, Okada M, Kataoka H, et al. Sema3E-PlexinD1 signaling selectively suppresses disoriented angiogenesis in ischemic retinopathy in mice. J Clin Invest 2011; 121:1974-1985.
    • (2011) J Clin Invest , vol.121 , pp. 1974-1985
    • Fukushima, Y.1    Okada, M.2    Kataoka, H.3
  • 96
    • 27744549126 scopus 로고    scopus 로고
    • Microarray analysis of endothelial differentially expressed genes in liver of cirrhotic rats
    • Tugues S, Morales-Ruiz M, Fernandez-Varo G, et al. Microarray analysis of endothelial differentially expressed genes in liver of cirrhotic rats. Gastroenterology 2005; 129:1686-1695.
    • (2005) Gastroenterology , vol.129 , pp. 1686-1695
    • Tugues, S.1    Morales-Ruiz, M.2    Fernandez-Varo, G.3
  • 97
    • 77954669022 scopus 로고    scopus 로고
    • Microarray analysis of retinal endothelial tip cells identifies CXCR4 as a mediator of tip cell morphology and branching
    • Strasser GA, Kaminker JS, Tessier-Lavigne M. Microarray analysis of retinal endothelial tip cells identifies CXCR4 as a mediator of tip cell morphology and branching. Blood 2010; 115:5102-5110.
    • (2010) Blood , vol.115 , pp. 5102-5110
    • Strasser, G.A.1    Kaminker, J.S.2    Tessier-Lavigne, M.3
  • 98
    • 33646231757 scopus 로고    scopus 로고
    • Subtractive transcriptomics: Establishing polarity drives in vitro human endothelial morphogenesis
    • Glesne DA, Zhang W, Mandava S, et al. Subtractive transcriptomics: establishing polarity drives in vitro human endothelial morphogenesis. Cancer Res 2006; 66:4030-4040.
    • (2006) Cancer Res , vol.66 , pp. 4030-4040
    • Glesne, D.A.1    Zhang, W.2    Mandava, S.3
  • 99
    • 84883679792 scopus 로고    scopus 로고
    • Mesenchymal stem/progenitors and other endometrial cell types from women with polycystic ovary syndrome (PCOS) display inflammatory and oncogenic potential
    • Piltonen TT, Chen J, Erikson DW, et al. Mesenchymal stem/progenitors and other endometrial cell types from women with polycystic ovary syndrome (PCOS) display inflammatory and oncogenic potential. J Clin Endocrinol Metab 2013; 98:3765-3775.
    • (2013) J Clin Endocrinol Metab , vol.98 , pp. 3765-3775
    • Piltonen, T.T.1    Chen, J.2    Erikson, D.W.3


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