메뉴 건너뛰기




Volumn 31, Issue 34, 2011, Pages 12208-12217

MMP2-9 cleavage of dystroglycan alters the size and molecular composition of Schwann cell domains

Author keywords

[No Author keywords available]

Indexed keywords

DYSTROGLYCAN; GELATINASE A; GELATINASE B;

EID: 80051937261     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.0141-11.2011     Document Type: Article
Times cited : (39)

References (73)
  • 1
  • 2
    • 33645869560 scopus 로고    scopus 로고
    • Dystroglycan is selectively cleaved at the parenchymal basement membrane at sites of leukocyte extravasation in experimental autoimmune encephalomyelitis
    • Agrawal S, Anderson P, Durbeej M, van Rooijen N, Ivars F, Opdenakker G, Sorokin LM (2006) Dystroglycan is selectively cleaved at the parenchymal basement membrane at sites of leukocyte extravasation in experimental autoimmune encephalomyelitis. J Exp Med 203:1007-1019.
    • (2006) J Exp Med , vol.203 , pp. 1007-1019
    • Agrawal, S.1    Anderson, P.2    Durbeej, M.3    van Rooijen, N.4    Ivars, F.5    Opdenakker, G.6    Sorokin, L.M.7
  • 3
    • 38949156757 scopus 로고    scopus 로고
    • SEA domain proteolysis determines the functional composition of dystroglycan
    • Akhavan A, Crivelli SN, Singh M, Lingappa VR, Muschler JL (2008) SEA domain proteolysis determines the functional composition of dystroglycan. FASEB J 22:612-621.
    • (2008) FASEB J , vol.22 , pp. 612-621
    • Akhavan, A.1    Crivelli, S.N.2    Singh, M.3    Lingappa, V.R.4    Muschler, J.L.5
  • 4
    • 45549096100 scopus 로고    scopus 로고
    • The ABCA1 cholesterol transporter associates with one of two distinct dystrophinbased scaffolds in Schwann cells
    • Albrecht DE, Sherman DL, Brophy PJ, Froehner SC (2008) The ABCA1 cholesterol transporter associates with one of two distinct dystrophinbased scaffolds in Schwann cells. Glia 56:611-618.
    • (2008) Glia , vol.56 , pp. 611-618
    • Albrecht, D.E.1    Sherman, D.L.2    Brophy, P.J.3    Froehner, S.C.4
  • 5
    • 0031771470 scopus 로고    scopus 로고
    • Angiogenesis and apoptosis are cellular parameters of neoplastic progression in transgenic mouse models of tumorigenesis
    • Bergers G, Hanahan D, Coussens LM (1998) Angiogenesis and apoptosis are cellular parameters of neoplastic progression in transgenic mouse models of tumorigenesis. Int J Dev Biol 42:995-1002.
    • (1998) Int J Dev Biol , vol.42 , pp. 995-1002
    • Bergers, G.1    Hanahan, D.2    Coussens, L.M.3
  • 8
    • 0015577453 scopus 로고
    • Abnormalities of peripheral nerves in murine muscular dystrophy
    • Bradley WG, JenkisonM (1973) Abnormalities of peripheral nerves in murine muscular dystrophy. J Neurol Sci 18:227-247.
    • (1973) J Neurol Sci , vol.18 , pp. 227-247
    • Bradley, W.G.1    Jenkison, M.2
  • 9
    • 33646530740 scopus 로고    scopus 로고
    • Assembly of a perivascular astrocyte protein scaffold at the mammalian blood-brain barrier is dependent on alpha-syntrophin
    • Bragg AD, Amiry-Moghaddam M, Ottersen OP, Adams ME, Froehner SC (2006) Assembly of a perivascular astrocyte protein scaffold at the mammalian blood-brain barrier is dependent on alpha-syntrophin. Glia 53:879-890.
    • (2006) Glia , vol.53 , pp. 879-890
    • Bragg, A.D.1    Amiry-Moghaddam, M.2    Ottersen, O.P.3    Adams, M.E.4    Froehner, S.C.5
  • 11
    • 34249667153 scopus 로고    scopus 로고
    • Cytokine regulation of MMP-9 in peripheral glia: Implications for pathological processes and pain in injured nerve
    • Chattopadhyay S, Myers RR, Janes J, Shubayev V (2007) Cytokine regulation of MMP-9 in peripheral glia: implications for pathological processes and pain in injured nerve. Brain Behav Immun 21:561-568.
    • (2007) Brain Behav Immun , vol.21 , pp. 561-568
    • Chattopadhyay, S.1    Myers, R.R.2    Janes, J.3    Shubayev, V.4
  • 13
    • 3142580944 scopus 로고    scopus 로고
    • The potassium channel Kir4.1 associates with the dystrophin-glycoprotein complex via alpha-syntrophin in glia
    • Connors NC, Adams ME, Froehner SC, Kofuji P (2004) The potassium channel Kir4.1 associates with the dystrophin-glycoprotein complex via alpha-syntrophin in glia. J Biol Chem 279:28387-28392.
    • (2004) J Biol Chem , vol.279 , pp. 28387-28392
    • Connors, N.C.1    Adams, M.E.2    Froehner, S.C.3    Kofuji, P.4
  • 14
    • 0034625470 scopus 로고    scopus 로고
    • Nerve regeneration in Wld(s) mice is normalized by actinomycin D
    • Court F, Alvarez J (2000) Nerve regeneration in Wld(s) mice is normalized by actinomycin D. Brain Res 867:1-8.
    • (2000) Brain Res , vol.867 , pp. 1-8
    • Court, F.1    Alvarez, J.2
  • 15
    • 64849090412 scopus 로고    scopus 로고
    • A laminin-2, dystroglycan, utrophin axis is required for compartmentalization and elongation of myelin segments
    • Court FA, Hewitt JE, Davies K, Patton BL, Uncini A, Wrabetz L, Feltri ML (2009) A laminin-2, dystroglycan, utrophin axis is required for compartmentalization and elongation of myelin segments. J Neurosci 29:3908-3919.
    • (2009) J Neurosci , vol.29 , pp. 3908-3919
    • Court, F.A.1    Hewitt, J.E.2    Davies, K.3    Patton, B.L.4    Uncini, A.5    Wrabetz, L.6    Feltri, M.L.7
  • 19
    • 0031453392 scopus 로고    scopus 로고
    • The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination
    • Einheber S, Zanazzi G, Ching W, Scherer S, Milner TA, Peles E, Salzer JL (1997) The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination. J Cell Biol 139:1495-1506.
    • (1997) J Cell Biol , vol.139 , pp. 1495-1506
    • Einheber, S.1    Zanazzi, G.2    Ching, W.3    Scherer, S.4    Milner, T.A.5    Peles, E.6    Salzer, J.L.7
  • 21
    • 0033836577 scopus 로고    scopus 로고
    • MMP-2 and MMP-9 increase the neuritepromoting potential of schwann cell basal laminae and are upregulated in degenerated nerve
    • Ferguson TA, Muir D (2000) MMP-2 and MMP-9 increase the neuritepromoting potential of schwann cell basal laminae and are upregulated in degenerated nerve. Mol Cell Neurosci 16:157-167.
    • (2000) Mol Cell Neurosci , vol.16 , pp. 157-167
    • Ferguson, T.A.1    Muir, D.2
  • 23
    • 0033757623 scopus 로고    scopus 로고
    • Maturation and maintenance of the neuromuscular synapse: Genetic evidence for roles of the dystrophin-glycoprotein complex
    • Grady RM, Zhou H, Cunningham JM, Henry MD, Campbell KP, Sanes JR (2000) Maturation and maintenance of the neuromuscular synapse: genetic evidence for roles of the dystrophin-glycoprotein complex. Neuron 25:279-293.
    • (2000) Neuron , vol.25 , pp. 279-293
    • Grady, R.M.1    Zhou, H.2    Cunningham, J.M.3    Henry, M.D.4    Campbell, K.P.5    Sanes, J.R.6
  • 24
    • 33747383933 scopus 로고    scopus 로고
    • Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue
    • Haenggi T, Fritschy JM (2006) Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue. Cell Mol Life Sci 63:1614-1631.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1614-1631
    • Haenggi, T.1    Fritschy, J.M.2
  • 26
    • 0000215620 scopus 로고
    • Distribution of nodes and incisures in normal and regenerated nerve fibers
    • Hiscoe HB (1947) Distribution of nodes and incisures in normal and regenerated nerve fibers. Anat Rec 99:447-475.
    • (1947) Anat Rec , vol.99 , pp. 447-475
    • Hiscoe, H.B.1
  • 27
    • 0033976679 scopus 로고    scopus 로고
    • Biosynthesis of dystroglycan: Processing of a precursor propeptide
    • Holt KH, Crosbie RH, Venzke DP, Campbell KP (2000) Biosynthesis of dystroglycan: processing of a precursor propeptide. FEBS Lett 468:79-83.
    • (2000) FEBS Lett , vol.468 , pp. 79-83
    • Holt, K.H.1    Crosbie, R.H.2    Venzke, D.P.3    Campbell, K.P.4
  • 29
    • 0030884231 scopus 로고    scopus 로고
    • Unaltered secretion of beta-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice
    • Itoh T, Ikeda T, Gomi H, Nakao S, Suzuki T, Itohara S (1997) Unaltered secretion of beta-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice. J Biol Chem 272:22389-22392.
    • (1997) J Biol Chem , vol.272 , pp. 22389-22392
    • Itoh, T.1    Ikeda, T.2    Gomi, H.3    Nakao, S.4    Suzuki, T.5    Itohara, S.6
  • 30
    • 0020660891 scopus 로고
    • Quantitative studies of the abnormal axon- Schwann cell relationship in the peripheral motor and sensory nerves of the dystrophic mouse
    • Jaros E, Jenkison M (1983) Quantitative studies of the abnormal axon- Schwann cell relationship in the peripheral motor and sensory nerves of the dystrophic mouse. Brain Res 258:181-196.
    • (1983) Brain Res , vol.258 , pp. 181-196
    • Jaros, E.1    Jenkison, M.2
  • 31
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, Riordan JR (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83:129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 32
    • 4444228394 scopus 로고    scopus 로고
    • Aberrant expression, processing and degradation of dystroglycan in squamous cell carcinomas
    • Jing J, Lien CF, Sharma S, Rice J, Brennan PA, Gó recki DC (2004) Aberrant expression, processing and degradation of dystroglycan in squamous cell carcinomas. Eur J Cancer 40:2143-2151.
    • (2004) Eur J Cancer , vol.40 , pp. 2143-2151
    • Jing, J.1    Lien, C.F.2    Sharma, S.3    Rice, J.4    Brennan, P.A.5    Górecki, D.C.6
  • 34
    • 0028587288 scopus 로고
    • Organization of microtubules in myelinating Schwann cells
    • Kidd GJ, Andrews SB, Trapp BD (1994) Organization of microtubules in myelinating Schwann cells. J Neurocytol 23:801-810.
    • (1994) J Neurocytol , vol.23 , pp. 801-810
    • Kidd, G.J.1    Andrews, S.B.2    Trapp, B.D.3
  • 35
    • 64249172203 scopus 로고    scopus 로고
    • The canonical Notch signaling pathway: Unfolding the activation mechanism
    • Kopan R, Ilagan MX (2009) The canonical Notch signaling pathway: unfolding the activation mechanism. Cell 137:216-233.
    • (2009) Cell , vol.137 , pp. 216-233
    • Kopan, R.1    Ilagan, M.X.2
  • 36
    • 0030442578 scopus 로고    scopus 로고
    • Basement membrane and repair of injury to peripheral nerve: Defining a potential role for macrophages, matrix metalloproteinases, and tissue inhibitor of metalloproteinases-1
    • La Fleur M, Underwood JL, Rappolee DA, Werb Z (1996) Basement membrane and repair of injury to peripheral nerve: defining a potential role for macrophages, matrix metalloproteinases, and tissue inhibitor of metalloproteinases-1. J Exp Med 184:2311-2326.
    • (1996) J Exp Med , vol.184 , pp. 2311-2326
    • la Fleur, M.1    Underwood, J.L.2    Rappolee, D.A.3    Werb, Z.4
  • 37
    • 0017087803 scopus 로고
    • Myodystrophy, a new myopathy on chromosome 8 of the mouse
    • Lane PW, Beamer TC, Myers DD (1976) Myodystrophy, a new myopathy on chromosome 8 of the mouse. J Hered 67:135-138.
    • (1976) J Hered , vol.67 , pp. 135-138
    • Lane, P.W.1    Beamer, T.C.2    Myers, D.D.3
  • 38
    • 67649851014 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy
    • Li H, Mittal A, Makonchuk DY, Bhatnagar S, Kumar A (2009) Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy. Hum Mol Genet 18:2584-2598.
    • (2009) Hum Mol Genet , vol.18 , pp. 2584-2598
    • Li, H.1    Mittal, A.2    Makonchuk, D.Y.3    Bhatnagar, S.4    Kumar, A.5
  • 42
    • 0035223979 scopus 로고    scopus 로고
    • The role of metalloprotease in pathogenesis of nervous system diseases (in Polish)
    • Mirowska D, Członkowska A (2001) The role of metalloprotease in pathogenesis of nervous system diseases (in Polish). Neurol Neurochir Pol 35:101-110.
    • (2001) Neurol Neurochir Pol , vol.35 , pp. 101-110
    • Mirowska, D.1    Członkowska, A.2
  • 43
    • 77949455857 scopus 로고    scopus 로고
    • Dystroglycan versatility in cell adhesion: A tale of multiple motifs
    • Moore CJ, Winder SJ (2010) Dystroglycan versatility in cell adhesion: a tale of multiple motifs. Cell Commun Signal 8:3.
    • (2010) Cell Commun Signal , vol.8 , pp. 3
    • Moore, C.J.1    Winder, S.J.2
  • 49
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A, Ewald AJ, Werb Z (2007) Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 8:221-233.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 50
    • 0006554324 scopus 로고
    • London: Bailliere, Tindall and Cox
    • Ramóny Cajal S (1933) Histology. London: Bailliere, Tindall and Cox.
    • (1933) Histology
    • Ramóny Cajal, S.1
  • 55
    • 0141987863 scopus 로고    scopus 로고
    • Polarized domains of myelinated axons
    • Salzer JL (2003) Polarized domains of myelinated axons. Neuron 40:297-318.
    • (2003) Neuron , vol.40 , pp. 297-318
    • Salzer, J.L.1
  • 56
    • 56249104133 scopus 로고    scopus 로고
    • Aberrant expression of beta-dystroglycan may be due to processing by matrix metalloproteinases-2 and-9 in oral squamous cell carcinoma
    • Shang ZJ, Ethunandan M, Górecki DC, Brennan PA (2008) Aberrant expression of beta-dystroglycan may be due to processing by matrix metalloproteinases-2 and-9 in oral squamous cell carcinoma. Oral Oncol 44:1139-1146.
    • (2008) Oral Oncol , vol.44 , pp. 1139-1146
    • Shang, Z.J.1    Ethunandan, M.2    Górecki, D.C.3    Brennan, P.A.4
  • 57
    • 0034681351 scopus 로고    scopus 로고
    • A tripartite nuclear localization signal in the PDZ-domain protein L-periaxin
    • Sherman DL, Brophy PJ (2000) A tripartite nuclear localization signal in the PDZ-domain protein L-periaxin. J Biol Chem 275:4537-4540.
    • (2000) J Biol Chem , vol.275 , pp. 4537-4540
    • Sherman, D.L.1    Brophy, P.J.2
  • 58
    • 0034968820 scopus 로고    scopus 로고
    • Specific disruption of a schwann cell dystrophin-related protein complex in a demyelinating neuropathy
    • Sherman DL, Fabrizi C, Gillespie CS, Brophy PJ (2001) Specific disruption of a schwann cell dystrophin-related protein complex in a demyelinating neuropathy. Neuron 30:677-687.
    • (2001) Neuron , vol.30 , pp. 677-687
    • Sherman, D.L.1    Fabrizi, C.2    Gillespie, C.S.3    Brophy, P.J.4
  • 59
    • 0033621668 scopus 로고    scopus 로고
    • Upregulation and interaction of TNFalpha and gelatinases A and B in painful peripheral nerve injury
    • Shubayev VI, Myers RR (2000) Upregulation and interaction of TNFalpha and gelatinases A and B in painful peripheral nerve injury. Brain Res 855:83-89.
    • (2000) Brain Res , vol.855 , pp. 83-89
    • Shubayev, V.I.1    Myers, R.R.2
  • 62
    • 1242314761 scopus 로고    scopus 로고
    • Regulation of angiogenesis by extracellular matrix
    • Sottile J (2004) Regulation of angiogenesis by extracellular matrix. Biochim Biophys Acta 1654:13-22.
    • (2004) Biochim Biophys Acta , vol.1654 , pp. 13-22
    • Sottile, J.1
  • 67
    • 33750436537 scopus 로고    scopus 로고
    • Dystroglycan loss disrupts polarity and beta-casein induction in mammary epithelial cells by perturbing laminin anchoring
    • Weir ML, Oppizzi ML, Henry MD, Onishi A, Campbell KP, Bissell MJ, Muschler JL (2006) Dystroglycan loss disrupts polarity and beta-casein induction in mammary epithelial cells by perturbing laminin anchoring. J Cell Sci 119:4047-4058.
    • (2006) J Cell Sci , vol.119 , pp. 4047-4058
    • Weir, M.L.1    Oppizzi, M.L.2    Henry, M.D.3    Onishi, A.4    Campbell, K.P.5    Bissell, M.J.6    Muschler, J.L.7
  • 68
    • 0034973979 scopus 로고    scopus 로고
    • Do Schwann cells stop, DR(o)P2, and roll?
    • Wrabetz L, Feltri ML (2001) Do Schwann cells stop, DR(o)P2, and roll? Neuron 30:642-644.
    • (2001) Neuron , vol.30 , pp. 642-644
    • Wrabetz, L.1    Feltri, M.L.2
  • 70
    • 71249161927 scopus 로고    scopus 로고
    • IL-1beta induces MMP-9 expression via a Ca 2_-dependent CaMKII/JNK/c-JUN cascade in rat brain astrocytes
    • Wu CY, Hsieh HL, Sun CC, Yang CM (2009) IL-1beta induces MMP-9 expression via a Ca 2_-dependent CaMKII/JNK/c-JUN cascade in rat brain astrocytes. Glia 57:1775-1789.
    • (2009) Glia , vol.57 , pp. 1775-1789
    • Wu, C.Y.1    Hsieh, H.L.2    Sun, C.C.3    Yang, C.M.4
  • 71
    • 0035878554 scopus 로고    scopus 로고
    • Processing of betadystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex
    • Yamada H, Saito F, Fukuta-Ohi H, Zhong D, Hase A, Arai K, Okuyama A, Maekawa R, Shimizu T, Matsumura K (2001) Processing of betadystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex. Hum Mol Genet 10:1563-1569.
    • (2001) Hum Mol Genet , vol.10 , pp. 1563-1569
    • Yamada, H.1    Saito, F.2    Fukuta-Ohi, H.3    Zhong, D.4    Hase, A.5    Arai, K.6    Okuyama, A.7    Maekawa, R.8    Shimizu, T.9    Matsumura, K.10
  • 73
    • 33646835580 scopus 로고    scopus 로고
    • Characterization of the protease activity that cleaves the extracellular domain of beta-dystroglycan
    • Zhong D, Saito F, Saito Y, Nakamura A, Shimizu T, Matsumura K (2006) Characterization of the protease activity that cleaves the extracellular domain of beta-dystroglycan. Biochem Biophys Res Commun 345: 867-871.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 867-871
    • Zhong, D.1    Saito, F.2    Saito, Y.3    Nakamura, A.4    Shimizu, T.5    Matsumura, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.