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Volumn 42, Issue , 2013, Pages 63-69

Peptidomic analysis of human reflex tear fluid

Author keywords

Endogenous peptide; MALDI TOF TOF; Peptidomics; Polymeric immunoglobulin receptor; Proline rich protein 4; Tear

Indexed keywords

PEPTIDE;

EID: 84875361063     PISSN: 01969781     EISSN: 18735169     Source Type: Journal    
DOI: 10.1016/j.peptides.2012.11.018     Document Type: Article
Times cited : (20)

References (56)
  • 1
    • 80054730423 scopus 로고    scopus 로고
    • Clinical application of urinary proteomics/peptidomics
    • A. Albalat, H. Mischak, and W. Mullen Clinical application of urinary proteomics/peptidomics Expert Rev Proteomics 8 2011 615 629
    • (2011) Expert Rev Proteomics , vol.8 , pp. 615-629
    • Albalat, A.1    Mischak, H.2    Mullen, W.3
  • 2
    • 0021687267 scopus 로고
    • Inhibition of apatite crystal growth by the amino-terminal segment of human salivary acidic proline-rich proteins
    • T. Aoba, E.C. Moreno, and D.I. Hay Inhibition of apatite crystal growth by the amino-terminal segment of human salivary acidic proline-rich proteins Calcif Tissue Int 36 1984 651 658
    • (1984) Calcif Tissue Int , vol.36 , pp. 651-658
    • Aoba, T.1    Moreno, E.C.2    Hay, D.I.3
  • 3
    • 23244461889 scopus 로고    scopus 로고
    • -/- mice abrogates the development of allergic lung inflammation
    • -/- mice abrogates the development of allergic lung inflammation J Immunol 175 2005 1276 1285
    • (2005) J Immunol , vol.175 , pp. 1276-1285
    • Arnaboldi, P.M.1    Behr, M.J.2    Mucosal, M.D.W.3
  • 6
    • 0034856707 scopus 로고    scopus 로고
    • Peptidomics of the pars intercerebralis-corpus cardiacum complex of the migratory locust, Locusta migratoria
    • E. Clynen, G. Baggerman, D. Veelaert, A. Cerstiaens, D. Van der Horst, and L. Harthoorn Peptidomics of the pars intercerebralis-corpus cardiacum complex of the migratory locust, Locusta migratoria Eur J Biochem 268 2001 1929 1939
    • (2001) Eur J Biochem , vol.268 , pp. 1929-1939
    • Clynen, E.1    Baggerman, G.2    Veelaert, D.3    Cerstiaens, A.4    Van Der Horst, D.5    Harthoorn, L.6
  • 7
    • 18144424749 scopus 로고    scopus 로고
    • The evolution of neuroendocrine peptides
    • J.M. Conlon, and D. Larhammar The evolution of neuroendocrine peptides Gen Comp Endocrinol 142 2005 53 59
    • (2005) Gen Comp Endocrinol , vol.142 , pp. 53-59
    • Conlon, J.M.1    Larhammar, D.2
  • 8
    • 33748294174 scopus 로고    scopus 로고
    • Peptidomics for cancer diagnosis: Present and future
    • E.P. Diamandis Peptidomics for cancer diagnosis: present and future J Proteome Res 5 2006 2079 2082
    • (2006) J Proteome Res , vol.5 , pp. 2079-2082
    • Diamandis, E.P.1
  • 9
    • 0029131474 scopus 로고
    • A major human lacrimal gland mRNA encodes a new proline-rich protein family member
    • D.P. Dickinson, and M. Thiesse A major human lacrimal gland mRNA encodes a new proline-rich protein family member Invest Ophthalmol Vis Sci 36 1995 2020 2031
    • (1995) Invest Ophthalmol Vis Sci , vol.36 , pp. 2020-2031
    • Dickinson, D.P.1    Thiesse, M.2
  • 13
    • 30444432702 scopus 로고    scopus 로고
    • Neuropeptide-processing enzymes: Applications for drug discovery
    • L.D. Fricker Neuropeptide-processing enzymes: applications for drug discovery AAPS J 7 2005 E449 E455
    • (2005) AAPS J , vol.7
    • Fricker, L.D.1
  • 14
    • 77954573017 scopus 로고    scopus 로고
    • Analysis of mouse brain peptides using mass spectrometry-based peptidomics: Implications for novel functions ranging from non-classical neuropeptides to microproteins
    • L.D. Fricker Analysis of mouse brain peptides using mass spectrometry-based peptidomics: implications for novel functions ranging from non-classical neuropeptides to microproteins Mol Biosyst 6 2010 1355
    • (2010) Mol Biosyst , vol.6 , pp. 1355
    • Fricker, L.D.1
  • 15
    • 0034651077 scopus 로고    scopus 로고
    • Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing
    • L.D. Fricker, A.A. McKinzie, J. Sun, E. Curran, Y. Qian, and L. Yan Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing J Neurosci 20 2000 639 648
    • (2000) J Neurosci , vol.20 , pp. 639-648
    • Fricker, L.D.1    McKinzie, A.A.2    Sun, J.3    Curran, E.4    Qian, Y.5    Yan, L.6
  • 16
    • 10644242580 scopus 로고    scopus 로고
    • Characterization of the in vivo forms of lacrimal-specific proline-rich proteins in human tear fluid
    • K.Y.C. Fung, C. Morris, S. Sathe, R. Sack, and M.W. Duncan Characterization of the in vivo forms of lacrimal-specific proline-rich proteins in human tear fluid Proteomics 4 2004 3953 3959
    • (2004) Proteomics , vol.4 , pp. 3953-3959
    • Fung, K.Y.C.1    Morris, C.2    Sathe, S.3    Sack, R.4    Duncan, M.W.5
  • 17
    • 77958198450 scopus 로고    scopus 로고
    • Hemopressin and other bioactive peptides from cytosolic proteins: Are these non-classical neuropeptides?
    • J.S. Gelman, and L.D. Fricker Hemopressin and other bioactive peptides from cytosolic proteins: are these non-classical neuropeptides? AAPS J 12 2010 279 289
    • (2010) AAPS J , vol.12 , pp. 279-289
    • Gelman, J.S.1    Fricker, L.D.2
  • 19
    • 0023757544 scopus 로고
    • Adsorbed salivary proline-rich protein 1 and statherin: Receptors for type 1 fimbriae of Actinomyces viscosus T14V-J1 on apatitic surfaces
    • R.J. Gibbons, D.I. Hay, J.O. Cisar, and W.B. Clark Adsorbed salivary proline-rich protein 1 and statherin: receptors for type 1 fimbriae of Actinomyces viscosus T14V-J1 on apatitic surfaces Infect Immun 56 1988 2990 2993
    • (1988) Infect Immun , vol.56 , pp. 2990-2993
    • Gibbons, R.J.1    Hay, D.I.2    Cisar, J.O.3    Clark, W.B.4
  • 20
    • 40749152244 scopus 로고    scopus 로고
    • Investigation of the human tear film proteome using multiple proteomic approaches
    • K.B. Green-Church, K.K. Nichols, N.M. Kleinholz, L. Zhang, and J.J. Nichols Investigation of the human tear film proteome using multiple proteomic approaches Mol Vis 14 2008 456 470
    • (2008) Mol Vis , vol.14 , pp. 456-470
    • Green-Church, K.B.1    Nichols, K.K.2    Kleinholz, N.M.3    Zhang, L.4    Nichols, J.J.5
  • 21
    • 0020491867 scopus 로고
    • Inhibitory action of proline-containing peptides on Xaa-Pro- dipeptidylaminopeptidase
    • M. Harada, K.M. Fukasawa, K. Fukasawa, and T. Nagatsu Inhibitory action of proline-containing peptides on Xaa-Pro-dipeptidylaminopeptidase Biochim Biophys Acta 705 1982 288 290
    • (1982) Biochim Biophys Acta , vol.705 , pp. 288-290
    • Harada, M.1    Fukasawa, K.M.2    Fukasawa, K.3    Nagatsu, T.4
  • 22
    • 0030739527 scopus 로고    scopus 로고
    • Human free secretory component is composed of the first 585 amino acid residues of the polymeric immunoglobulin receptor
    • G.J. Hughes, S. Frutiger, L.A. Savoy, A.J. Reason, H.R. Morris, and J.C. Jaton Human free secretory component is composed of the first 585 amino acid residues of the polymeric immunoglobulin receptor FEBS Lett 410 1997 443 446
    • (1997) FEBS Lett , vol.410 , pp. 443-446
    • Hughes, G.J.1    Frutiger, S.2    Savoy, L.A.3    Reason, A.J.4    Morris, H.R.5    Jaton, J.C.6
  • 23
    • 14644422603 scopus 로고    scopus 로고
    • Different isoforms and post-translational modifications of human salivary acidic proline-rich proteins
    • R. Inzitari, T. Cabras, G. Onnis, C. Olmi, A. Mastinu, and M.T. Sanna Different isoforms and post-translational modifications of human salivary acidic proline-rich proteins Proteomics 5 2005 805 815
    • (2005) Proteomics , vol.5 , pp. 805-815
    • Inzitari, R.1    Cabras, T.2    Onnis, G.3    Olmi, C.4    Mastinu, A.5    Sanna, M.T.6
  • 24
    • 23344433145 scopus 로고    scopus 로고
    • The polymeric immunoglobulin receptor: Bridging innate and adaptive immune responses at mucosal surfaces
    • C.S. Kaetzel The polymeric immunoglobulin receptor: bridging innate and adaptive immune responses at mucosal surfaces Immunol Rev 206 2005 83 99
    • (2005) Immunol Rev , vol.206 , pp. 83-99
    • Kaetzel, C.S.1
  • 25
    • 0025731994 scopus 로고
    • Basic proline-rich proteins from human parotid saliva: Relationships of the covalent structures of ten proteins from a single individual
    • D.L. Kauffman, A. Bennick, M. Blum, and P.J. Keller Basic proline-rich proteins from human parotid saliva: relationships of the covalent structures of ten proteins from a single individual Biochemistry 30 1991 3351 3356
    • (1991) Biochemistry , vol.30 , pp. 3351-3356
    • Kauffman, D.L.1    Bennick, A.2    Blum, M.3    Keller, P.J.4
  • 26
    • 79956330137 scopus 로고    scopus 로고
    • Peptidomic analysis of the central nervous system of the protochordate, Ciona intestinalis: Homologs and prototypes of vertebrate peptides and novel peptides
    • T. Kawada, M. Ogasawara, T. Sekiguchi, M. Aoyama, K. Hotta, and K. Oka Peptidomic analysis of the central nervous system of the protochordate, Ciona intestinalis: homologs and prototypes of vertebrate peptides and novel peptides Endocrinology 152 2011 2416 2427
    • (2011) Endocrinology , vol.152 , pp. 2416-2427
    • Kawada, T.1    Ogasawara, M.2    Sekiguchi, T.3    Aoyama, M.4    Hotta, K.5    Oka, K.6
  • 27
    • 0028201394 scopus 로고
    • Analysis and function of the human tear proteins
    • A. Kijlstra, and A. Kuizenga Analysis and function of the human tear proteins Adv Exp Med Biol 350 1994 299 308
    • (1994) Adv Exp Med Biol , vol.350 , pp. 299-308
    • Kijlstra, A.1    Kuizenga, A.2
  • 28
    • 27144557079 scopus 로고    scopus 로고
    • Sex-specific peptides from exocrine glands stimulate mouse vomeronasal sensory neurons
    • H. Kimoto, S. Haga, K. Sato, and K. Touhara Sex-specific peptides from exocrine glands stimulate mouse vomeronasal sensory neurons Nature 437 2005 898 901
    • (2005) Nature , vol.437 , pp. 898-901
    • Kimoto, H.1    Haga, S.2    Sato, K.3    Touhara, K.4
  • 29
    • 35549007215 scopus 로고    scopus 로고
    • Sex- and strain-specific expression and vomeronasal activity of mouse ESP family peptides
    • H. Kimoto, K. Sato, F. Nodari, S. Haga, T.E. Holy, and K. Touhara Sex- and strain-specific expression and vomeronasal activity of mouse ESP family peptides Curr Biol 17 2007 1879 1884
    • (2007) Curr Biol , vol.17 , pp. 1879-1884
    • Kimoto, H.1    Sato, K.2    Nodari, F.3    Haga, S.4    Holy, T.E.5    Touhara, K.6
  • 30
    • 79955061701 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: Signaling pathways and biological functions
    • M. Lal, and M. Caplan Regulated intramembrane proteolysis: signaling pathways and biological functions Physiology (Bethesda) 26 2011 34 44
    • (2011) Physiology (Bethesda) , vol.26 , pp. 34-44
    • Lal, M.1    Caplan, M.2
  • 31
    • 0033855722 scopus 로고    scopus 로고
    • Possible release of an ArgGlyArgProGln pentapeptide with innate immunity properties from acidic proline-rich proteins by proteolytic activity in commensal streptococcus and actinomyces species
    • T. Li, P. Bratt, A.P. Jonsson, M. Ryberg, I. Johansson, and W.J. Griffiths Possible release of an ArgGlyArgProGln pentapeptide with innate immunity properties from acidic proline-rich proteins by proteolytic activity in commensal streptococcus and actinomyces species Infect Immun 68 2000 5425 5429
    • (2000) Infect Immun , vol.68 , pp. 5425-5429
    • Li, T.1    Bratt, P.2    Jonsson, A.P.3    Ryberg, M.4    Johansson, I.5    Griffiths, W.J.6
  • 32
    • 79955663580 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis-lessons from amyloid precursor protein processing
    • S.F. Lichtenthaler, C. Haass, and H. Steiner Regulated intramembrane proteolysis-lessons from amyloid precursor protein processing J Neurochem 117 2011 779 796
    • (2011) J Neurochem , vol.117 , pp. 779-796
    • Lichtenthaler, S.F.1    Haass, C.2    Steiner, H.3
  • 35
    • 78650381240 scopus 로고    scopus 로고
    • Characterization of human neutrophil peptides (α-defensins) in the tears of dry eye patients
    • L.-H. Lo, P.-C. Wu, Y.-C. Wu, and J. Shiea Characterization of human neutrophil peptides (α-defensins) in the tears of dry eye patients Anal Methods 2 2010 1934
    • (2010) Anal Methods , vol.2 , pp. 1934
    • Lo, L.-H.1    Wu, P.-C.2    Wu, Y.-C.3    Shiea, J.4
  • 37
    • 69749094420 scopus 로고    scopus 로고
    • A label-free nano-liquid chromatography-mass spectrometry approach for quantitative serum peptidomics in Crohn's disease patients
    • P. Nanni, F. Levander, G. Roda, A. Caponi, P. James, and A. Roda A label-free nano-liquid chromatography-mass spectrometry approach for quantitative serum peptidomics in Crohn's disease patients J Chromatogr B Analyt Technol Biomed Life Sci 877 2009 3127 3136
    • (2009) J Chromatogr B Analyt Technol Biomed Life Sci , vol.877 , pp. 3127-3136
    • Nanni, P.1    Levander, F.2    Roda, G.3    Caponi, A.4    James, P.5    Roda, A.6
  • 38
    • 52649138959 scopus 로고    scopus 로고
    • Improvements for the visualization of low-molecular weight protein and peptides of human tears using MALDI
    • T. Nguyen-Khuong, A. Fitzgerald, Z. Zhao, M. Willcox, and B.J. Walsh Improvements for the visualization of low-molecular weight protein and peptides of human tears using MALDI Proteomics 8 2008 3424 3432
    • (2008) Proteomics , vol.8 , pp. 3424-3432
    • Nguyen-Khuong, T.1    Fitzgerald, A.2    Zhao, Z.3    Willcox, M.4    Walsh, B.J.5
  • 39
    • 20444460241 scopus 로고    scopus 로고
    • The lacrimal gland transcriptome is an unusually rich source of rare and poorly characterized gene transcripts
    • A.M. Ozyildirim, G.J. Wistow, J. Gao, J. Wang, D.P. Dickinson, and H.F. Frierson The lacrimal gland transcriptome is an unusually rich source of rare and poorly characterized gene transcripts Invest Ophthalmol Vis Sci 46 2005 1572 1580
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 1572-1580
    • Ozyildirim, A.M.1    Wistow, G.J.2    Gao, J.3    Wang, J.4    Dickinson, D.P.5    Frierson, H.F.6
  • 40
    • 0028202179 scopus 로고
    • Structure and function of the tear film
    • P.N. Dilly Structure and function of the tear film Adv Exp Med Biol 350 1994 239 247
    • (1994) Adv Exp Med Biol , vol.350 , pp. 239-247
    • Dilly, P.N.1
  • 42
    • 84863012019 scopus 로고    scopus 로고
    • Extensive characterization of Tupaia belangeri neuropeptidome using an integrated mass spectrometric approach
    • F. Petruzziello, L. Fouillen, H. Wadensten, R. Kretz, P.E. Andren, and G. Rainer Extensive characterization of Tupaia belangeri neuropeptidome using an integrated mass spectrometric approach J Proteome Res 11 2012 886 896
    • (2012) J Proteome Res , vol.11 , pp. 886-896
    • Petruzziello, F.1    Fouillen, L.2    Wadensten, H.3    Kretz, R.4    Andren, P.E.5    Rainer, G.6
  • 43
    • 0037302651 scopus 로고    scopus 로고
    • Novel functions of the polymeric Ig receptor: Well beyond transport of immunoglobulins
    • A. Phalipon, and B. Corthésy Novel functions of the polymeric Ig receptor: well beyond transport of immunoglobulins Trends Immunol 24 2003 55 58
    • (2003) Trends Immunol , vol.24 , pp. 55-58
    • Phalipon, A.1    Corthésy, B.2
  • 44
    • 0035152929 scopus 로고    scopus 로고
    • Reduced epithelial expression of secretory component in small airways correlates with airflow obstruction in chronic obstructive pulmonary disease
    • C. Pilette, V. Godding, R. Kiss, M. Delos, E. Verbeken, and C. Decaestecker Reduced epithelial expression of secretory component in small airways correlates with airflow obstruction in chronic obstructive pulmonary disease Am J Respir Crit Care Med 163 2001 185 194
    • (2001) Am J Respir Crit Care Med , vol.163 , pp. 185-194
    • Pilette, C.1    Godding, V.2    Kiss, R.3    Delos, M.4    Verbeken, E.5    Decaestecker, C.6
  • 45
    • 0027407698 scopus 로고
    • Interferon-gamma induces polymeric immunoglobulin receptor mRNA in human intestinal epithelial cells by a protein synthesis dependent mechanism
    • J.F. Piskurich, J.A. France, C.M. Tamer, C.A. Willmer, C.S. Kaetzel, and D.M. Kaetzel Interferon-gamma induces polymeric immunoglobulin receptor mRNA in human intestinal epithelial cells by a protein synthesis dependent mechanism Mol Immunol 30 1993 413 421
    • (1993) Mol Immunol , vol.30 , pp. 413-421
    • Piskurich, J.F.1    France, J.A.2    Tamer, C.M.3    Willmer, C.A.4    Kaetzel, C.S.5    Kaetzel, D.M.6
  • 46
    • 0024998289 scopus 로고
    • Soluble CD23 containing B cell supernatants induce IgE from peripheral blood B-lymphocytes and costimulate with interleukin-4 in induction of IgE
    • A. Saxon, Z. Ke, L. Bahati, and R.H. Stevens Soluble CD23 containing B cell supernatants induce IgE from peripheral blood B-lymphocytes and costimulate with interleukin-4 in induction of IgE J Allergy Clin Immunol 86 1990 333 344
    • (1990) J Allergy Clin Immunol , vol.86 , pp. 333-344
    • Saxon, A.1    Ke, Z.2    Bahati, L.3    Stevens, R.H.4
  • 48
    • 33748754288 scopus 로고    scopus 로고
    • Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors
    • G.A. de Souza, L.M.F. Godoy, and M. Mann Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors Genome Biol 7 2006 R72
    • (2006) Genome Biol , vol.7 , pp. 72
    • De Souza, G.A.1    Godoy, L.M.F.2    Mann, M.3
  • 49
    • 23944470664 scopus 로고    scopus 로고
    • Peptidomic analysis of human blood specimens: Comparison between plasma specimens and serum by differential peptide display
    • H. Tammen, I. Schulte, R. Hess, C. Menzel, M. Kellmann, and T. Mohring Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display Proteomics 5 2005 3414 3422
    • (2005) Proteomics , vol.5 , pp. 3414-3422
    • Tammen, H.1    Schulte, I.2    Hess, R.3    Menzel, C.4    Kellmann, M.5    Mohring, T.6
  • 50
    • 28444479815 scopus 로고    scopus 로고
    • Molecular evolution of animal antimicrobial peptides: Widespread moderate positive selection
    • J.A. Tennessen Molecular evolution of animal antimicrobial peptides: widespread moderate positive selection J Evol Biol 18 2005 1387 1394
    • (2005) J Evol Biol , vol.18 , pp. 1387-1394
    • Tennessen, J.A.1
  • 51
    • 33750621983 scopus 로고    scopus 로고
    • Serum peptidome patterns that distinguish metastatic thyroid carcinoma from cancer-free controls are unbiased by gender and age
    • J. Villanueva, A.J. Martorella, K. Lawlor, J. Philip, M. Fleisher, and R.J. Robbins Serum peptidome patterns that distinguish metastatic thyroid carcinoma from cancer-free controls are unbiased by gender and age Mol Cell Proteomics 5 2006 1840 1852
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1840-1852
    • Villanueva, J.1    Martorella, A.J.2    Lawlor, K.3    Philip, J.4    Fleisher, M.5    Robbins, R.J.6
  • 52
    • 78649396351 scopus 로고    scopus 로고
    • Finding new posttranslational modifications in salivary proline-rich proteins
    • R. Vitorino, R. Alves, A. Barros, A. Caseiro, R. Ferreira, and M.C. Lobo Finding new posttranslational modifications in salivary proline-rich proteins Proteomics 10 2010 3732 3742
    • (2010) Proteomics , vol.10 , pp. 3732-3742
    • Vitorino, R.1    Alves, R.2    Barros, A.3    Caseiro, A.4    Ferreira, R.5    Lobo, M.C.6
  • 53
    • 14744274048 scopus 로고    scopus 로고
    • Human cerebrospinal fluid peptidomics
    • X. Yuan, and D.M. Desiderio Human cerebrospinal fluid peptidomics J Mass Spectrom 40 2005 176 181
    • (2005) J Mass Spectrom , vol.40 , pp. 176-181
    • Yuan, X.1    Desiderio, D.M.2
  • 54
    • 0034664821 scopus 로고    scopus 로고
    • The polymeric immunoglobulin receptor translocates pneumococci across human nasopharyngeal epithelial cells
    • J.R. Zhang, K.E. Mostov, M.E. Lamm, M. Nanno, S. Shimida, and M. Ohwaki The polymeric immunoglobulin receptor translocates pneumococci across human nasopharyngeal epithelial cells Cell 102 2000 827 837
    • (2000) Cell , vol.102 , pp. 827-837
    • Zhang, J.R.1    Mostov, K.E.2    Lamm, M.E.3    Nanno, M.4    Shimida, S.5    Ohwaki, M.6
  • 55
    • 33745005452 scopus 로고    scopus 로고
    • Analysis of the low molecular weight serum peptidome using ultrafiltration and a hybrid ion trap-Fourier transform mass spectrometer
    • X. Zheng, H. Baker, and W.S. Hancock Analysis of the low molecular weight serum peptidome using ultrafiltration and a hybrid ion trap-Fourier transform mass spectrometer J Chromatogr A 1120 2006 173 184
    • (2006) J Chromatogr A , vol.1120 , pp. 173-184
    • Zheng, X.1    Baker, H.2    Hancock, W.S.3


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