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Volumn 46, Issue 2, 2005, Pages 627-635

Phosphorylation and glycosylation of bovine lens MP20

Author keywords

[No Author keywords available]

Indexed keywords

CYANOGEN BROMIDE; GALECTIN 3; LENS PROTEIN; MEMBRANE PROTEIN 20; TRYPSIN; UNCLASSIFIED DRUG;

EID: 13944281684     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.04-0894     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 0023955118 scopus 로고
    • MP17, a fiber-specific intrinsic membrane protein from mammalian eye lens
    • Mulders JW, Voorter CE, Lamers C, et al. MP17, a fiber-specific intrinsic membrane protein from mammalian eye lens. Curr Eye Res. 1988;7:207-219.
    • (1988) Curr Eye Res , vol.7 , pp. 207-219
    • Mulders, J.W.1    Voorter, C.E.2    Lamers, C.3
  • 2
    • 0026786352 scopus 로고
    • The distribution of the fiber cell intrinsic membrane proteins MP20 and connexin46 in the bovine lens
    • Tenbroek E, Arneson M, Jarvis L, Louis C. The distribution of the fiber cell intrinsic membrane proteins MP20 and connexin46 in the bovine lens. J Cell Sci. 1992;103:245-257.
    • (1992) J Cell Sci , vol.103 , pp. 245-257
    • Tenbroek, E.1    Arneson, M.2    Jarvis, L.3    Louis, C.4
  • 3
    • 0141757144 scopus 로고    scopus 로고
    • Insertion of MP20 into lens fibre cell plasma membranes correlates with the formation of an extracellular diffusion barrier
    • Grey AC, Jacobs MD, Gonen T, Kistler J, Donaldson PJ. Insertion of MP20 into lens fibre cell plasma membranes correlates with the formation of an extracellular diffusion barrier. Exp Eye Res. 2003; 77:567-574.
    • (2003) Exp Eye Res , vol.77 , pp. 567-574
    • Grey, A.C.1    Jacobs, M.D.2    Gonen, T.3    Kistler, J.4    Donaldson, P.J.5
  • 4
    • 0001913054 scopus 로고    scopus 로고
    • MP20: The second most abundant lens membrane protein and member of the tetraspanin superfamily, joins the list of ligands of galectin-3
    • Gonen T, Grey AC, Jacobs MD, Donaldson PJ, Kistler J. MP20: the second most abundant lens membrane protein and member of the tetraspanin superfamily, joins the list of ligands of galectin-3. BMC Cell Biol. 2001;2:17.
    • (2001) BMC Cell Biol , vol.2 , pp. 17
    • Gonen, T.1    Grey, A.C.2    Jacobs, M.D.3    Donaldson, P.J.4    Kistler, J.5
  • 5
    • 0031557714 scopus 로고    scopus 로고
    • Identification of a mutation in the MP19 gene, Lim2, in the cataractous mouse mutant To3
    • Steele EC Jr, Kerscher S, Lyon MF, et al. Identification of a mutation in the MP19 gene, Lim2, in the cataractous mouse mutant To3. Mol Vis. 1997;3:5.
    • (1997) Mol Vis , vol.3 , pp. 5
    • Steele Jr., E.C.1    Kerscher, S.2    Lyon, M.F.3
  • 6
    • 0034595482 scopus 로고    scopus 로고
    • Lim2(To3) transgenic mice establish a causative relationship between the mutation identified in the lim2 gene and cataractogenesis in the To3 mouse mutant
    • Steele EC Jr, Wang JH, Lo WK, et al. Lim2(To3) transgenic mice establish a causative relationship between the mutation identified in the lim2 gene and cataractogenesis in the To3 mouse mutant. Mol Vis. 2000;6:85-94.
    • (2000) Mol Vis , vol.6 , pp. 85-94
    • Steele Jr., E.C.1    Wang, J.H.2    Lo, W.K.3
  • 7
    • 0028793694 scopus 로고
    • Epithelial membrane protein-1, peripheral myelin protein 22, and lens membrane protein 20 define a novel gene family
    • Taylor V, Welcher AA, Program AE, Suter U. Epithelial membrane protein-1, peripheral myelin protein 22, and lens membrane protein 20 define a novel gene family. J Biol Chem. 1995;270:28824-28833.
    • (1995) J Biol Chem , vol.270 , pp. 28824-28833
    • Taylor, V.1    Welcher, A.A.2    Program, A.E.3    Suter, U.4
  • 8
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • Morita K, Furuse M, Fujimoto K, Tsukita S. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci USA. 1999;96:511-516.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 9
    • 0035789069 scopus 로고    scopus 로고
    • The mouse lens fiber-cell intrinsic membrane protein MP19 gene (Lim2) and granule membrane protein GMP-17 gene (Nkg7): Isolation and sequence analysis of two neighboring genes
    • Zhou L, Li X, Church RL. The mouse lens fiber-cell intrinsic membrane protein MP19 gene (Lim2) and granule membrane protein GMP-17 gene (Nkg7): isolation and sequence analysis of two neighboring genes. Mol Vis. 2001;7:79-88.
    • (2001) Mol Vis , vol.7 , pp. 79-88
    • Zhou, L.1    Li, X.2    Church, R.L.3
  • 10
    • 0033631414 scopus 로고    scopus 로고
    • The peripheral myelin protein 22 and epithelial membrane protein family
    • Jetten AM, Suter U. The peripheral myelin protein 22 and epithelial membrane protein family. Prog Nucleic Acids Res Mol Biol. 2000; 64:97-129.
    • (2000) Prog Nucleic Acids Res Mol Biol , vol.64 , pp. 97-129
    • Jetten, A.M.1    Suter, U.2
  • 11
    • 0032055044 scopus 로고    scopus 로고
    • Structural arrangement of lens fiber cell plasma membrane protein MP20
    • Arneson ML, Louis CF. Structural arrangement of lens fiber cell plasma membrane protein MP20. Exp Eye Res. 1998;66:495-509.
    • (1998) Exp Eye Res , vol.66 , pp. 495-509
    • Arneson, M.L.1    Louis, C.F.2
  • 12
    • 0027452876 scopus 로고
    • Cloning and expression of a major rat lens membrane protein, MP20
    • Kumar NM, Jarvis LJ, Tenbroek E, Louis CF. Cloning and expression of a major rat lens membrane protein, MP20. Exp Eye Res. 1993;56:35-43.
    • (1993) Exp Eye Res , vol.56 , pp. 35-43
    • Kumar, N.M.1    Jarvis, L.J.2    Tenbroek, E.3    Louis, C.F.4
  • 13
    • 0347930657 scopus 로고    scopus 로고
    • Does lens intrinsic membrane protein MP19 contain a membrane-targeting signal?
    • Chen T, Li X, Yang Y, Erdene AG, Church RL. Does lens intrinsic membrane protein MP19 contain a membrane-targeting signal? Mol Vis. 2003;9:735-746.
    • (2003) Mol Vis , vol.9 , pp. 735-746
    • Chen, T.1    Li, X.2    Yang, Y.3    Erdene, A.G.4    Church, R.L.5
  • 14
    • 0025941909 scopus 로고
    • Age-dependent covalent changes in MP18 from bovine lens membrane
    • Subramanian G, Takemoto L. Age-dependent covalent changes in MP18 from bovine lens membrane. Invest Ophthalmol Vis Sci. 1991;32:2588-2592.
    • (1991) Invest Ophthalmol Vis Sci , vol.32 , pp. 2588-2592
    • Subramanian, G.1    Takemoto, L.2
  • 15
    • 0024364998 scopus 로고
    • Bovine lens 23, 21 and 19 kDa intrinsic membrane proteins have an identical amino-terminal amino acid sequence
    • Rao GN, Gutekunst KA, Church RL. Bovine lens 23, 21 and 19 kDa intrinsic membrane proteins have an identical amino-terminal amino acid sequence. FEBS Lett. 1989;250:483-486.
    • (1989) FEBS Lett , vol.250 , pp. 483-486
    • Rao, G.N.1    Gutekunst, K.A.2    Church, R.L.3
  • 16
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly PJ, Krebs EG. Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem. 1991;266:15555-15558.
    • (1991) J Biol Chem , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 18
    • 0021993133 scopus 로고
    • Phosphorylation of lens fiber cell membrane proteins
    • Garland D, Russell P. Phosphorylation of lens fiber cell membrane proteins. Proc Natl Acad Sci USA. 1985;82:653-657.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 653-657
    • Garland, D.1    Russell, P.2
  • 19
    • 0024358086 scopus 로고
    • Structural organization of the lens fiber cell plasma membrane protein MP18
    • Galvan A, Lampe PD, Hur KC, et al. Structural organization of the lens fiber cell plasma membrane protein MP18. J Biol Chem. 1989;264:19974-19978.
    • (1989) J Biol Chem , vol.264 , pp. 19974-19978
    • Galvan, A.1    Lampe, P.D.2    Hur, K.C.3
  • 20
    • 0022459258 scopus 로고
    • Phosphorylation of lens intrinsic membrane proteins by protein kinase C
    • Lampe PD, Bazzi MD, Nelsestuen GL, Johnson RG. Phosphorylation of lens intrinsic membrane proteins by protein kinase C. Eur J Biochem. 1986;156:351-357.
    • (1986) Eur J Biochem , vol.156 , pp. 351-357
    • Lampe, P.D.1    Bazzi, M.D.2    Nelsestuen, G.L.3    Johnson, R.G.4
  • 22
    • 0018719555 scopus 로고
    • Lens gap junctions: A structural hypothesis for nonregulated low-resistance intercellular pathways
    • Goodenough DJ. Lens gap junctions: a structural hypothesis for nonregulated low-resistance intercellular pathways. Invest Ophthalmol Vis Sci. 1979;18:1104-1122.
    • (1979) Invest Ophthalmol Vis Sci , vol.18 , pp. 1104-1122
    • Goodenough, D.J.1
  • 23
    • 0029156287 scopus 로고
    • Purification and oligomeric state of the major lens fiber cell membrane proteins
    • Jarvis LJ, Louis CF. Purification and oligomeric state of the major lens fiber cell membrane proteins. Curr Eye Res. 1995;14:799-808.
    • (1995) Curr Eye Res , vol.14 , pp. 799-808
    • Jarvis, L.J.1    Louis, C.F.2
  • 24
    • 0028310723 scopus 로고
    • Identification of glycoproteins on nitrocellulose membranes and gels
    • Thornton DJ, Carlstedt I, Sheehan JK. Identification of glycoproteins on nitrocellulose membranes and gels. Methods Mol Biol. 1994;32:119-128.
    • (1994) Methods Mol Biol , vol.32 , pp. 119-128
    • Thornton, D.J.1    Carlstedt, I.2    Sheehan, J.K.3
  • 25
    • 0031887346 scopus 로고    scopus 로고
    • Mass spectrometric analysis of integral membrane proteins: Application to complete mapping of bacteriorhodopsins and rhodopsin
    • Ball LE, Oatis JE Jr, Dharmasiri K, et al. Mass spectrometric analysis of integral membrane proteins: application to complete mapping of bacteriorhodopsins and rhodopsin. Protein Sci. 1998;7:758-764.
    • (1998) Protein Sci , vol.7 , pp. 758-764
    • Ball, L.E.1    Oatis Jr., J.E.2    Dharmasiri, K.3
  • 26
    • 0036127937 scopus 로고    scopus 로고
    • Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • van Montfort BA, Canas B, Duurkens R, Godovac-Zimmermann J, Robillard GT. Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J Mass Spectrom. 2002;37:322-330.
    • (2002) J Mass Spectrom , vol.37 , pp. 322-330
    • Montfort, B.A.1    Canas, B.2    Duurkens, R.3    Godovac-Zimmermann, J.4    Robillard, G.T.5
  • 27
    • 0023804303 scopus 로고
    • Contributions of mass spectrometry to peptide and protein structure
    • Biemann K. Contributions of mass spectrometry to peptide and protein structure. Biomed Environ Mass Spectrom. 1988;16:99-111.
    • (1988) Biomed Environ Mass Spectrom , vol.16 , pp. 99-111
    • Biemann, K.1
  • 28
    • 0345383804 scopus 로고    scopus 로고
    • Protein phosphorylation analysis by electrospray ionization-mass spectrometry
    • Resing KA, Ahn NG. Protein phosphorylation analysis by electrospray ionization-mass spectrometry. Methods Enzymol. 1997;283: 29-44.
    • (1997) Methods Enzymol , vol.283 , pp. 29-44
    • Resing, K.A.1    Ahn, N.G.2
  • 29
    • 0034577985 scopus 로고    scopus 로고
    • Protein C-mannosylation: Facts and questions
    • Furmanek A, Hofsteenge J. Protein C-mannosylation: facts and questions. Acta Biochim Pol. 2000;47:781-789.
    • (2000) Acta Biochim Pol , vol.47 , pp. 781-789
    • Furmanek, A.1    Hofsteenge, J.2
  • 30
    • 0036047046 scopus 로고    scopus 로고
    • C-mannosylation and o-fucosylation of thrombospondin type 1 repeats
    • Gonzalez de Peredo A, Klein D, Macek B, et al. C-mannosylation and o-fucosylation of thrombospondin type 1 repeats. Mol Cell Proteomics. 2002;1:11-18.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 11-18
    • Gonzalez De Peredo, A.1    Klein, D.2    Macek, B.3
  • 31
    • 0024368598 scopus 로고
    • Identifications of an 18,000 Dalton protein in mammalian lens fiber cell membranes
    • Louis CF, Hur KC, Galvan AC, et al. Identifications of an 18,000 Dalton protein in mammalian lens fiber cell membranes. J Biol Chem. 1989;264:19967-19973.
    • (1989) J Biol Chem , vol.264 , pp. 19967-19973
    • Louis, C.F.1    Hur, K.C.2    Galvan, A.C.3
  • 32
    • 0033986513 scopus 로고    scopus 로고
    • Galectin-3 is associated with the plasma membrane of lens fiber cells
    • Gonen T, Donaldson P, Kistler J. Galectin-3 is associated with the plasma membrane of lens fiber cells. Invest Ophthalmol Vis Sci. 2000;41:199-203.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 199-203
    • Gonen, T.1    Donaldson, P.2    Kistler, J.3
  • 33
    • 0028033725 scopus 로고
    • New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us
    • Hofsteenge J, Muller DR, de Beer T, et al. New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us. Biochemistry. 1994;33: 13524-13530.
    • (1994) Biochemistry , vol.33 , pp. 13524-13530
    • Hofsteenge, J.1    Muller, D.R.2    De Beer, T.3
  • 34
    • 9544222719 scopus 로고    scopus 로고
    • Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms
    • Loffler A, Doucey MA, Jansson AM, et al. Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms. Biochemistry. 1996;35:12005-12014.
    • (1996) Biochemistry , vol.35 , pp. 12005-12014
    • Loffler, A.1    Doucey, M.A.2    Jansson, A.M.3
  • 35
    • 0033785743 scopus 로고    scopus 로고
    • Tryptophan-N-glucoside in fruits and fruit juices
    • Diem S, Bergmann J, Herderich M. Tryptophan-N-glucoside in fruits and fruit juices. J Agric Food Chem. 2000;48:4913-4917.
    • (2000) J Agric Food Chem , vol.48 , pp. 4913-4917
    • Diem, S.1    Bergmann, J.2    Herderich, M.3
  • 36
    • 2442519149 scopus 로고    scopus 로고
    • C-Mannosylation of MUC5AC and MUC5B Cys subdomains
    • Perez-Vilar J, Randell SH, Boucher RC. C-Mannosylation of MUC5AC and MUC5B Cys subdomains. Glycobiology. 2004;14: 325-337.
    • (2004) Glycobiology , vol.14 , pp. 325-337
    • Perez-Vilar, J.1    Randell, S.H.2    Boucher, R.C.3
  • 37
    • 0037136406 scopus 로고    scopus 로고
    • Oligosaccharide specificity of galectins: A search by frontal affinity chromatography
    • Hirabayashi J, Hashidate T, Arata Y, et al. Oligosaccharide specificity of galectins: a search by frontal affinity chromatography. Biochim Biophys Acta. 2002;1572:232-254.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 232-254
    • Hirabayashi, J.1    Hashidate, T.2    Arata, Y.3
  • 38
    • 0033914833 scopus 로고    scopus 로고
    • beta-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3
    • Fradin C, Poulain D, Jouault T. beta-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3. Infect Immun. 2000;68:4391-4398.
    • (2000) Infect Immun , vol.68 , pp. 4391-4398
    • Fradin, C.1    Poulain, D.2    Jouault, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.