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Volumn 11, Issue 1, 2014, Pages

Proteomic analysis of human osteoarthritis synovial fluid

(23)  Balakrishnan, Lavanya a,b   Nirujogi, Raja Sekhar a,c   Ahmad, Sartaj a,d   Bhattacharjee, Mitali a,e   Manda, Srikanth S a,c   Renuse, Santosh a,e   Kelkar, Dhanashree S a,e   Subbannayya, Yashwanth a,f   Raju, Rajesh a   Goel, Renu a,b   Thomas, Joji Kurian a,e   Kaur, Navjyot g   Dhillon, Mukesh g   Tankala, Shantal Gupta g   Jois, Ramesh h   Vasdev, Vivek i   Ramachandra, Y L b   Sahasrabuddhe, Nandini A a   Prasad, T S Keshava a,c,d   Mohan, Sujatha j   more..


Author keywords

Body fluid; Cartilage; Glycosylation; Joint destruction

Indexed keywords

ATTRACTIN; DICKKOPF 1 PROTEIN; FIBRILLIN 1; FIBULIN; FIBULIN 1; GLYCOPROTEIN; LECTIN; MICROSOMAL AMINOPEPTIDASE; OSTEOPONTIN; PROTEIN ADAMDEC1; PROTEIN AFM; PROTEIN CD84; PROTEIN MXRA5; PROTEIN OCG; PROTEIN SPON2; PROTEIN SPP2; PROTEIN VSN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 84903756945     PISSN: 15426416     EISSN: 15590275     Source Type: Journal    
DOI: 10.1186/1559-0275-11-6     Document Type: Article
Times cited : (118)

References (82)
  • 6
    • 67649518014 scopus 로고    scopus 로고
    • Proteomics: Addressing the challenges of osteoarthritis
    • De Ceuninck F, Berenbaum F: Proteomics: Addressing the challenges of osteoarthritis. Drug Discov Today 2009, 14:661-667.
    • (2009) Drug Discov Today , vol.14 , pp. 661-667
    • De Ceuninck, F.1    Berenbaum, F.2
  • 7
    • 77949938199 scopus 로고    scopus 로고
    • Proteomics role in the search for improved diagnosis, prognosis and treatment of osteoarthritis
    • Ruiz-Romero C, Blanco FJ: Proteomics role in the search for improved diagnosis, prognosis and treatment of osteoarthritis. Osteoarthritis Cartilage 2010, 18:500-509.
    • (2010) Osteoarthritis Cartilage , vol.18 , pp. 500-509
    • Ruiz-Romero, C.1    Blanco, F.J.2
  • 9
    • 33750364830 scopus 로고    scopus 로고
    • The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins
    • Adachi J, Kumar C, Zhang Y, Olsen JV, Mann M: The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins. Genome Biol 2006, 7:R80.
    • (2006) Genome Biol , vol.7
    • Adachi, J.1    Kumar, C.2    Zhang, Y.3    Olsen, J.V.4    Mann, M.5
  • 11
    • 33748754288 scopus 로고    scopus 로고
    • Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors
    • de Souza GA, Godoy LM, Mann M: Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors. Genome Biol 2006, 7:R72.
    • (2006) Genome Biol , vol.7
    • De Souza, G.A.1    Godoy, L.M.2    Mann, M.3
  • 15
    • 33745104040 scopus 로고    scopus 로고
    • Large-scale and high-confidence proteomic analysis of human seminal plasma
    • Pilch B, Mann M: Large-scale and high-confidence proteomic analysis of human seminal plasma. Genome Biol 2006, 7:R40.
    • (2006) Genome Biol , vol.7
    • Pilch, B.1    Mann, M.2
  • 16
    • 0042513861 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis of synovial fluid: Method for detecting candidate protein markers for osteoarthritis
    • DOI 10.1007/s00776-003-0657-3
    • Yamagiwa H, Sarkar G, Charlesworth MC, McCormick DJ, Bolander ME: Two-dimensional gel electrophoresis of synovial fluid: method for detecting candidate protein markers for osteoarthritis. J Orthop Sci 2003, 8:482-490. (Pubitemid 37012058)
    • (2003) Journal of Orthopaedic Science , vol.8 , Issue.4 , pp. 482-490
    • Yamagiwa, H.1    Sarkar, G.2    Charlesworth, M.C.3    McCormick, D.J.4    Bolander, M.E.5
  • 23
    • 75549085083 scopus 로고    scopus 로고
    • Human protein reference database and human proteinpedia as discovery tools for systems biology
    • Prasad TS, Kandasamy K, Pandey A: Human Protein Reference Database and Human Proteinpedia as discovery tools for systems biology. Methods Mol Biol 2009, 577:67-79.
    • (2009) Methods Mol Biol , vol.577 , pp. 67-79
    • Prasad, T.S.1    Kandasamy, K.2    Pandey, A.3
  • 26
    • 77956011441 scopus 로고    scopus 로고
    • Aggrecan and cartilage oligomeric matrix protein in serum and synovial fluid of patients with knee osteoarthritis
    • El-Arman MM, El-Fayoumi G, El-Shal E, El-Boghdady I, El-Ghaweet A: Aggrecan and cartilage oligomeric matrix protein in serum and synovial fluid of patients with knee osteoarthritis. Hss J 2010, 6:171-176.
    • (2010) Hss J , vol.6 , pp. 171-176
    • El-Arman, M.M.1    El-Fayoumi, G.2    El-Shal, E.3    El-Boghdady, I.4    El-Ghaweet, A.5
  • 27
    • 84865293224 scopus 로고    scopus 로고
    • Serum levels of cartilage oligomeric matrix protein in the diagnosis of knee osteoarthritis
    • Li H, Wang D, Wu ZQ, Zhong JM, Yuan YJ: Serum levels of cartilage oligomeric matrix protein in the diagnosis of knee osteoarthritis. Zhongguo Gu Shang 2012, 25:380-383.
    • (2012) Zhongguo Gu Shang , vol.25 , pp. 380-383
    • Li, H.1    Wang, D.2    Wu, Z.Q.3    Zhong, J.M.4    Yuan, Y.J.5
  • 28
    • 0026699536 scopus 로고
    • Fibronectin fragments in osteoarthritic synovial fluid
    • Xie DL, Meyers R, Homandberg GA: Fibronectin fragments in osteoarthritic synovial fluid. J Rheumatol 1992, 19:1448-1452.
    • (1992) J Rheumatol , vol.19 , pp. 1448-1452
    • Xie, D.L.1    Meyers, R.2    Homandberg, G.A.3
  • 30
    • 77956371758 scopus 로고    scopus 로고
    • Increased friction coefficient and superficial zone protein expression in patients with advanced osteoarthritis
    • Neu CP, Reddi AH, Komvopoulos K, Schmid TM, Di Cesare PE: Increased friction coefficient and superficial zone protein expression in patients with advanced osteoarthritis. Arthritis Rheum 2010, 62:2680-2687.
    • (2010) Arthritis Rheum , vol.62 , pp. 2680-2687
    • Neu, C.P.1    Reddi, A.H.2    Komvopoulos, K.3    Schmid, T.M.4    Di Cesare, P.E.5
  • 32
    • 0035853783 scopus 로고    scopus 로고
    • Identification and characterization of asporin A novel member of the leucine-rich repeat protein family closely related to decorin and biglycan
    • Lorenzo P, Aspberg A, Onnerfjord P, Bayliss MT, Neame PJ, Heinegard D: Identification and characterization of asporin. a novel member of the leucine-rich repeat protein family closely related to decorin and biglycan. J Biol Chem 2001, 276:12201-12211.
    • (2001) J Biol Chem , vol.276 , pp. 12201-12211
    • Lorenzo, P.1    Aspberg, A.2    Onnerfjord, P.3    Bayliss, M.T.4    Neame, P.J.5    Heinegard, D.6
  • 35
    • 70349772632 scopus 로고    scopus 로고
    • Asporin competes with decorin for collagen binding, binds calcium and promotes osteoblast collagen mineralization
    • Kalamajski S, Aspberg A, Lindblom K, Heinegard D, Oldberg A: Asporin competes with decorin for collagen binding, binds calcium and promotes osteoblast collagen mineralization. Biochem J 2009, 423:53-59.
    • (2009) Biochem J , vol.423 , pp. 53-59
    • Kalamajski, S.1    Aspberg, A.2    Lindblom, K.3    Heinegard, D.4    Oldberg, A.5
  • 38
    • 0032508461 scopus 로고    scopus 로고
    • Nidogen-2: A new basement membrane protein with diverse binding properties
    • DOI 10.1006/jmbi.1998.2004
    • Kohfeldt E, Sasaki T, Gohring W, Timpl R: Nidogen-2: A new basement membrane protein with diverse binding properties. J Mol Biol 1998, 282:99-109. (Pubitemid 28418662)
    • (1998) Journal of Molecular Biology , vol.282 , Issue.1 , pp. 99-109
    • Kohfeldt, E.1    Sasaki, T.2    Gohring, W.3    Timpl, R.4
  • 39
    • 43949105154 scopus 로고    scopus 로고
    • Nidogen-1 and nidogen-2 in healthy human cartilage and in late-stage osteoarthritis cartilage
    • DOI 10.1002/art.23480
    • Kruegel J, Sadowski B, Miosge N: Nidogen-1 and nidogen-2 in healthy human cartilage and in late-stage osteoarthritis cartilage. Arthritis Rheum 2008, 58:1422-1432. (Pubitemid 351705931)
    • (2008) Arthritis and Rheumatism , vol.58 , Issue.5 , pp. 1422-1432
    • Kruegel, J.1    Sadowski, B.2    Miosge, N.3
  • 40
    • 0026017887 scopus 로고
    • Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells
    • Shapiro LH, Ashmun RA, Roberts WM, Look AT: Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells. J Biol Chem 1991, 266:11999-12007. (Pubitemid 21907048)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.18 , pp. 11999-12007
    • Shapiro, L.H.1    Ashmun, R.A.2    Mark Roberts, W.3    Thomas Look, A.4
  • 41
    • 33749449024 scopus 로고    scopus 로고
    • Aminopeptidase N (APN/CD13) is selectively expressed in vascular endothelial cells and plays multiple roles in angiogenesis
    • DOI 10.1016/j.canlet.2005.11.051, PII S0304383505010827
    • Fukasawa K, Fujii H, Saitoh Y, Koizumi K, Aozuka Y, Sekine K, Yamada M, Saiki I, Nishikawa K: Aminopeptidase N (APN/CD13) is selectively expressed in vascular endothelial cells and plays multiple roles in angiogenesis. Cancer Lett 2006, 243:135-143. (Pubitemid 44508648)
    • (2006) Cancer Letters , vol.243 , Issue.1 , pp. 135-143
    • Fukasawa, K.1    Fujii, H.2    Saitoh, Y.3    Koizumi, K.4    Aozuka, Y.5    Sekine, K.6    Yamada, M.7    Saiki, I.8    Nishikawa, K.9
  • 44
    • 0036326359 scopus 로고    scopus 로고
    • The ADAMDEC1 (decysin) gene structure: Evolution by duplication in a metalloprotease gene cluster on Chromosome 8p12
    • DOI 10.1007/s00251-002-0430-3
    • Bates EE, Fridman WH, Mueller CG: The ADAMDEC1 (decysin) gene structure: evolution by duplication in a metalloprotease gene cluster on chromosome 8p12. Immunogenetics 2002, 54:96-105. (Pubitemid 34809705)
    • (2002) Immunogenetics , vol.54 , Issue.2 , pp. 96-105
    • Bates, E.E.1    Fridman, W.H.2    Mueller, C.G.3
  • 45
    • 0346851877 scopus 로고    scopus 로고
    • Inverse regulation of the ADAM-family members, decysin and MADDAM/ADAM19 during monocyte differentiation
    • DOI 10.1111/j.1365-2567.2003.01754.x
    • Fritsche J, Muller A, Hausmann M, Rogler G, Andreesen R, Kreutz M: Inverse regulation of the ADAM-family members, decysin and MADDAM/ADAM19 during monocyte differentiation. Immunology 2003, 110:450-457. (Pubitemid 37521875)
    • (2003) Immunology , vol.110 , Issue.4 , pp. 450-457
    • Fritsche, J.1    Muller, A.2    Hausmann, M.3    Rogler, G.4    Andreesen, R.5    Kreutz, M.6
  • 46
    • 0028819610 scopus 로고
    • Isolation and molecular cloning of a novel bone phosphoprotein related in sequence to the cystatin family of thiol protease inhibitors
    • Hu B, Coulson L, Moyer B, Price PA: Isolation and molecular cloning of a novel bone phosphoprotein related in sequence to the cystatin family of thiol protease inhibitors. J Biol Chem 1995, 270:431-436.
    • (1995) J Biol Chem , vol.270 , pp. 431-436
    • Hu, B.1    Coulson, L.2    Moyer, B.3    Price, P.A.4
  • 47
    • 0037483052 scopus 로고    scopus 로고
    • Biochemical characterization of the serum fetuin-mineral complex
    • DOI 10.1074/jbc.M300739200
    • Price PA, Nguyen TM, Williamson MK: Biochemical characterization of the serum fetuin-mineral complex. J Biol Chem 2003, 278:22153-22160. (Pubitemid 36792626)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 22153-22160
    • Price, P.A.1    Nguyen, T.M.T.2    Williamson, M.K.3
  • 48
    • 77955892561 scopus 로고    scopus 로고
    • Carboxy terminus of secreted phosphoprotein-24 kDa (spp24) is essential for full inhibition of BMP-2 activity
    • Brochmann EJ, Simon RJ, Jawien J, Behnam K, Sintuu C, Wang JC, Murray SS: Carboxy terminus of secreted phosphoprotein-24 kDa (spp24) is essential for full inhibition of BMP-2 activity. J Orthop Res 2010, 28:1200-1207.
    • (2010) J Orthop Res , vol.28 , pp. 1200-1207
    • Brochmann, E.J.1    Simon, R.J.2    Jawien, J.3    Behnam, K.4    Sintuu, C.5    Wang, J.C.6    Murray, S.S.7
  • 50
    • 33646695439 scopus 로고    scopus 로고
    • Role of adhesion molecules in synovial inflammation
    • DOI 10.1097/01.bor.0000218948.42730.39, PII 0000228120060500000010
    • Agarwal SK, Brenner MB: Role of adhesion molecules in synovial inflammation. Curr Opin Rheumatol 2006, 18:268-276. (Pubitemid 43740379)
    • (2006) Current Opinion in Rheumatology , vol.18 , Issue.3 , pp. 268-276
    • Agarwal, S.K.1    Brenner, M.B.2
  • 51
    • 30344487286 scopus 로고    scopus 로고
    • Molecular and cellular characterization of SEL-OB/SVEP1 in osteogenic cells in vivo and in vitro
    • DOI 10.1002/jcp.20497
    • Shur I, Socher R, Hameiri M, Fried A, Benayahu D: Molecular and cellular characterization of SEL-OB/SVEP1 in osteogenic cells in vivo and in vitro. J Cell Physiol 2006, 206:420-427. (Pubitemid 43062811)
    • (2006) Journal of Cellular Physiology , vol.206 , Issue.2 , pp. 420-427
    • Shur, I.1    Socher, R.2    Hameiri, M.3    Fried, A.4    Benayahu, D.5
  • 53
    • 0032479281 scopus 로고    scopus 로고
    • Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix
    • DOI 10.1074/jbc.273.27.16723
    • Sommarin Y, Wendel M, Shen Z, Hellman U, Heinegard D: Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix. J Biol Chem 1998, 273:16723-16729. (Pubitemid 28311696)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.27 , pp. 16723-16729
    • Sommarin, Y.1    Wendel, M.2    Shen, Z.3    Hellman, U.4    Heinegard, D.5
  • 54
    • 0033939602 scopus 로고    scopus 로고
    • Expression of the small leucine-rich proteoglycan osteoadherin/ osteomodulin in human dental pulp and developing rat teeth
    • DOI 10.1016/S8756-3282(00)00310-0, PII S8756328200003100
    • Buchaille R, Couble ML, Magloire H, Bleicher F: Expression of the small leucine-rich proteoglycan osteoadherin/osteomodulin in human dental pulp and developing rat teeth. Bone 2000, 27:265-270. (Pubitemid 30458820)
    • (2000) Bone , vol.27 , Issue.2 , pp. 265-270
    • Buchaille, R.1    Couble, M.L.2    Magloire, H.3    Bleicher, F.4
  • 55
    • 55249114587 scopus 로고    scopus 로고
    • Osteoadherin is upregulated by mature osteoblasts and enhances their in vitro differentiation and mineralization
    • Rehn AP, Cerny R, Sugars RV, Kaukua N, Wendel M: Osteoadherin is upregulated by mature osteoblasts and enhances their in vitro differentiation and mineralization. Calcif Tissue Int 2008, 82:454-464.
    • (2008) Calcif Tissue Int , vol.82 , pp. 454-464
    • Rehn, A.P.1    Cerny, R.2    Sugars, R.V.3    Kaukua, N.4    Wendel, M.5
  • 59
    • 79960936183 scopus 로고    scopus 로고
    • Ex vivo soft-laser treatment inhibits the synovial expression of vimentin and alpha-enolase, potential autoantigens in rheumatoid arthritis
    • Balint G, Barabas K, Zeitler Z, Bakos J, Kekesi KA, Pethes A, Nagy E, Lakatos T, Balint PV, Szekanecz Z: Ex vivo soft-laser treatment inhibits the synovial expression of vimentin and alpha-enolase, potential autoantigens in rheumatoid arthritis. Phys Ther 2011, 91:665-674.
    • (2011) Phys Ther , vol.91 , pp. 665-674
    • Balint, G.1    Barabas, K.2    Zeitler, Z.3    Bakos, J.4    Kekesi, K.A.5    Pethes, A.6    Nagy, E.7    Lakatos, T.8    Balint, P.V.9    Szekanecz, Z.10
  • 63
    • 77449156495 scopus 로고    scopus 로고
    • Identification of glycoproteins in human cerebrospinal fluid
    • Hwang HJ, Quinn T, Zhang J: Identification of glycoproteins in human cerebrospinal fluid. Methods Mol Biol 2009, 566:263-276.
    • (2009) Methods Mol Biol , vol.566 , pp. 263-276
    • Hwang, H.J.1    Quinn, T.2    Zhang, J.3
  • 67
    • 0030744877 scopus 로고    scopus 로고
    • Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an α-helical coiled coil
    • DOI 10.1016/S0014-5793(97)00664-9, PII S0014579397006649
    • Nielsen BB, Kastrup JS, Rasmussen H, Holtet TL, Graversen JH, Etzerodt M, Thogersen HC, Larsen IK: Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil. FEBS Lett 1997, 412:388-396. (Pubitemid 27321289)
    • (1997) FEBS Letters , vol.412 , Issue.2 , pp. 388-396
    • Nielsen, B.B.1    Kastrup, J.S.2    Rasmussen, H.3    Holtet, T.L.4    Graversen, J.H.5    Etzerodt, M.6    Thogersen, H.C.7    Larsen, I.K.8
  • 70
    • 84863564753 scopus 로고    scopus 로고
    • Association of CDX1 binding site of periostin gene with bone mineral density and vertebral fracture risk
    • Xiao SM, Gao Y, Cheung CL, Bow CH, Lau KS, Sham PC, Tan KC, Kung AW: Association of CDX1 binding site of periostin gene with bone mineral density and vertebral fracture risk. Osteoporos Int 2012, 23:1877-1887.
    • (2012) Osteoporos Int , vol.23 , pp. 1877-1887
    • Xiao, S.M.1    Gao, Y.2    Cheung, C.L.3    Bow, C.H.4    Lau, K.S.5    Sham, P.C.6    Tan, K.C.7    Kung, A.W.8
  • 71
    • 27944445973 scopus 로고    scopus 로고
    • Microarray analysis of differential gene expression in temporomandibular joint condylar cartilage after experimentally induced osteoarthritis
    • DOI 10.1016/j.joca.2005.03.010, PII S1063458405000968
    • Meng J, Ma X, Ma D, Xu C: Microarray analysis of differential gene expression in temporomandibular joint condylar cartilage after experimentally induced osteoarthritis. Osteoarthritis Cartilage 2005, 13:1115-1125. (Pubitemid 41672509)
    • (2005) Osteoarthritis and Cartilage , vol.13 , Issue.12 , pp. 1115-1125
    • Meng, J.1    Ma, X.2    Ma, D.3    Xu, C.4
  • 74
    • 40649095957 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture
    • DOI 10.1038/nprot.2008.2, PII NPROT.2008.2
    • Harsha HC, Molina H, Pandey A: Quantitative proteomics using stable isotope labeling with amino acids in cell culture. Nat Protoc 2008, 3:505-516. (Pubitemid 351372235)
    • (2008) Nature Protocols , vol.3 , Issue.3 , pp. 505-516
    • Harsha, H.C.1    Molina, H.2    Pandey, A.3
  • 76
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • DOI 10.1038/nprot.2007.261, PII NPROT.2007.261
    • Rappsilber J, Mann M, Ishihama Y: Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc 2007, 2:1896-1906. (Pubitemid 47308128)
    • (2007) Nature Protocols , vol.2 , Issue.8 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 78
    • 69749114144 scopus 로고    scopus 로고
    • Evaluation of several MS/MS search algorithms for analysis of spectra derived from electron transfer dissociation experiments
    • Kandasamy K, Pandey A, Molina H: Evaluation of several MS/MS search algorithms for analysis of spectra derived from electron transfer dissociation experiments. Anal Chem 2009, 81:7170-7180.
    • (2009) Anal Chem , vol.81 , pp. 7170-7180
    • Kandasamy, K.1    Pandey, A.2    Molina, H.3
  • 80
    • 79951536939 scopus 로고    scopus 로고
    • Collision energy optimization of b- And y-ions for multiple reaction monitoring mass spectrometry
    • Holstein Sherwood CA, Gafken PR, Martin DB: Collision energy optimization of b- And y-ions for multiple reaction monitoring mass spectrometry. J Proteome Res 2011, 10:231-240.
    • (2011) J Proteome Res , vol.10 , pp. 231-240
    • Holstein Sherwood, C.A.1    Gafken, P.R.2    Martin, D.B.3


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