메뉴 건너뛰기




Volumn 374, Issue 1, 2003, Pages 199-206

Pigment-epithelium-derived factor (PEDF) occurs at a physiologically relevant concentration in human blood: Purification and characterization

Author keywords

Angiogenesis; Collagen binding; Plasma; Pyroglutamate; Serpin

Indexed keywords

BIOCHEMISTRY; BLOOD; BLOOD VESSELS; CYTOLOGY; GROWTH KINETICS; NEUROPHYSIOLOGY;

EID: 0042326667     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030313     Document Type: Article
Times cited : (135)

References (37)
  • 2
    • 0035956869 scopus 로고    scopus 로고
    • Prevention of ischemia-induced retinopathy by the natural ocular antiangiogenic agent pigment epithelium-derived factor
    • Stellmach, V., Crawford, S. E., Zhou, W. and Bouck, N. (2001) Prevention of ischemia-induced retinopathy by the natural ocular antiangiogenic agent pigment epithelium-derived factor. Proc. Natl. Acad. Sci. U.S.A. 98, 2593-2597
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2593-2597
    • Stellmach, V.1    Crawford, S.E.2    Zhou, W.3    Bouck, N.4
  • 3
    • 0036104828 scopus 로고    scopus 로고
    • Inducer-stimulated Fas targets activated endothelium for destruction by anti-angiogenic thrombospondin-1 and pigment epithelium-derived factor
    • Volpert, O. V., Zaichuk, T., Zhou, W., Reiher, F., Ferguson, T. A., Stuart, P. M., Amin, M. and Bouck, N. P. (2002) Inducer-stimulated Fas targets activated endothelium for destruction by anti-angiogenic thrombospondin-1 and pigment epithelium-derived factor. Nat. Med. 8, 349-357
    • (2002) Nat. Med. , vol.8 , pp. 349-357
    • Volpert, O.V.1    Zaichuk, T.2    Zhou, W.3    Reiher, F.4    Ferguson, T.A.5    Stuart, P.M.6    Amin, M.7    Bouck, N.P.8
  • 4
    • 0025772716 scopus 로고
    • PEDF: A pigment epithelium-derived factor with potent neuronal differentiative activity
    • Tombran-Tink, J., Chader, G. G. and Johnson, L. V. (1991) PEDF: a pigment epithelium-derived factor with potent neuronal differentiative activity. Exp. Eye. Res. 53, 411-414
    • (1991) Exp. Eye. Res. , vol.53 , pp. 411-414
    • Tombran-Tink, J.1    Chader, G.G.2    Johnson, L.V.3
  • 6
    • 0032125517 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor (PEDF) differentially protects immature but not mature cerebellar granule cells against apaptotic cell death
    • Araki, T., Taniwaki, T., Becerra, S. P., Chader, G. J. and Schwartz, J. P. (1998) Pigment epithelium-derived factor (PEDF) differentially protects immature but not mature cerebellar granule cells against apaptotic cell death. J. Neurosci. Res. 53, 7-15
    • (1998) J. Neurosci. Res. , vol.53 , pp. 7-15
    • Araki, T.1    Taniwaki, T.2    Becerra, S.P.3    Chader, G.J.4    Schwartz, J.P.5
  • 7
    • 0035956928 scopus 로고    scopus 로고
    • PEDF: Raising both hopes and questions in controlling angiogenesis
    • Chader, G. J. (2001) PEDF: Raising both hopes and questions in controlling angiogenesis. Proc. Natl. Acad. Sci U.S.A. 98, 2122-2124
    • (2001) Proc. Natl. Acad. Sci U.S.A. , vol.98 , pp. 2122-2124
    • Chader, G.J.1
  • 8
    • 0027446940 scopus 로고
    • Pigment epithelium-derived factor: Neurotrophic activity and identification as a member of the serine pratease inhibitor gene family
    • Steele, F. R., Chader, G. J., Johnson, L. V. and Tombran-Tink, J. (1993) Pigment epithelium-derived factor: neurotrophic activity and identification as a member of the serine pratease inhibitor gene family. Prac. Natl. Acad. Sci. U.S.A. 90, 1526-1530
    • (1993) Prac. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 1526-1530
    • Steele, F.R.1    Chader, G.J.2    Johnson, L.V.3    Tombran-Tink, J.4
  • 9
    • 0035949561 scopus 로고    scopus 로고
    • Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor
    • Simonovic, M., Gettins, P. G. and Volz, K. (2001) Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor. Proc. Natl. Acad. Sci. U.S.A. 98, 11131-11135
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 11131-11135
    • Simonovic, M.1    Gettins, P.G.2    Volz, K.3
  • 10
    • 0029347070 scopus 로고
    • Identification of pigment epithelium-derived factor in the interphotoreceptor matrix of bovine eyes
    • Wu, Y. Q., Notario, V., Chader, G. J. and Becerra, S. P. (1995) Identification of pigment epithelium-derived factor in the interphotoreceptor matrix of bovine eyes. Protein Expression Purif. 6, 447-456
    • (1995) Protein Expression Purif. , vol.6 , pp. 447-456
    • Wu, Y.Q.1    Notario, V.2    Chader, G.J.3    Becerra, S.P.4
  • 11
    • 0029761958 scopus 로고    scopus 로고
    • Protealytic activity directed toward pigment epithelium-derived factor in vitreous of bovine eyes. Implications of proteolytic processing
    • Wu, Y. Q. and Becerra, S. P. (1996) Protealytic activity directed toward pigment epithelium-derived factor in vitreous of bovine eyes. Implications of proteolytic processing. Invest. Ophthalmol. Vis. Sci. 37, 1984-1993
    • (1996) Invest. Ophthalmol. Vis. Sci. , vol.37 , pp. 1984-1993
    • Wu, Y.Q.1    Becerra, S.P.2
  • 12
    • 0027375798 scopus 로고
    • Overexpression of fetal human pigment epithelium-derived factor in Escherichia coli. A functionally active neurotrophic factor
    • Becerra, S. P., Palmer, I., Kumar, A., Steele, F., Shiloach, J., Natario, V. and Chader, G. J. (1993) Overexpression of fetal human pigment epithelium-derived factor in Escherichia coli. A functionally active neurotrophic factor. J. Biol. Chem. 268, 23148-23156
    • (1993) J. Biol. Chem. , vol.268 , pp. 23148-23156
    • Becerra, S.P.1    Palmer, I.2    Kumar, A.3    Steele, F.4    Shiloach, J.5    Natario, V.6    Chader, G.J.7
  • 14
    • 0030449154 scopus 로고    scopus 로고
    • Recombinant human pigment epithelium-derived factor (PEDF): Characterization of PEDF overexpressed and secreted by eukaryotic cells
    • Stratikos, E., Alberdi, E., Gettins, P. G. and Becerra, S. P. (1996) Recombinant human pigment epithelium-derived factor (PEDF): characterization of PEDF overexpressed and secreted by eukaryotic cells. Protein Sci. 5, 2575-2582
    • (1996) Protein Sci. , vol.5 , pp. 2575-2582
    • Stratikos, E.1    Alberdi, E.2    Gettins, P.G.3    Becerra, S.P.4
  • 15
    • 0029101802 scopus 로고
    • Identification of proteins differentially expressed in quiescent and proliferatively senescent fibroblast cultures
    • DiPaolo, B. R., Pignolo, R. J. and Cristofalo, V. J. (1995) Identification of proteins differentially expressed in quiescent and proliferatively senescent fibroblast cultures. Exp. Cell. Res. 220, 178-185
    • (1995) Exp. Cell. Res. , vol.220 , pp. 178-185
    • DiPaolo, B.R.1    Pignolo, R.J.2    Cristofalo, V.J.3
  • 16
    • 0020010851 scopus 로고
    • Preparation and characterization of the different types of collagen
    • Miller, E. J. and Rhodes, R. K. (1982) Preparation and characterization of the different types of collagen. Methods Enzymol. 82, 33-64
    • (1982) Methods Enzymol. , vol.82 , pp. 33-64
    • Miller, E.J.1    Rhodes, R.K.2
  • 17
    • 0019792891 scopus 로고
    • Analysis of protein and peptide mixtures: Evaluation of three sodium dodecyl sulphate-polyacrylamide gel electrophoresis buffers systems
    • Bury, A. F. (1981) Analysis of protein and peptide mixtures: Evaluation of three sodium dodecyl sulphate-polyacrylamide gel electrophoresis buffers systems. J. Chromatogr. 213, 491-500
    • (1981) J. Chromatogr. , vol.213 , pp. 491-500
    • Bury, A.F.1
  • 18
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 19
    • 0031576218 scopus 로고    scopus 로고
    • Characterization of an epithelial approximately 450-kDa protein that facilitates endocytosis of intrinsic factor-vitamin B12 and binds receptor-associated protein
    • Birn, H., Verroust, P. J., Nexo, E., Hager, H., Jacobsen, C., Christensen, E. I. and Moestrup, S. K. (1997) Characterization of an epithelial approximately 450-kDa protein that facilitates endocytosis of intrinsic factor-vitamin B12 and binds receptor-associated protein. J. Biol. Chem. 272, 26497-26504
    • (1997) J. Biol. Chem. , vol.272 , pp. 26497-26504
    • Birn, H.1    Verroust, P.J.2    Nexo, E.3    Hager, H.4    Jacobsen, C.5    Christensen, E.I.6    Moestrup, S.K.7
  • 20
    • 0025249194 scopus 로고
    • Amino acid analysis
    • Ozols, J. (1990) Amino acid analysis. Methods Enzyme. 182, 587-601
    • (1990) Methods Enzyme. , vol.182 , pp. 587-601
    • Ozols, J.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 24
    • 0034736289 scopus 로고    scopus 로고
    • Structural characterisation at human proteinosis surfactant protein A
    • Berg, T., Leth-Larsen, R., Holmskov, U. and Hojrup, P. (2000) Structural characterisation at human proteinosis surfactant protein A. Biochim. Biophys. Acta 1543, 159-173
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 159-173
    • Berg, T.1    Leth-Larsen, R.2    Holmskov, U.3    Hojrup, P.4
  • 25
    • 0029072698 scopus 로고
    • Fluorophore-assisted carbohydrate electrophoresis technology and applications
    • Hu, G. F. (1995) Fluorophore-assisted carbohydrate electrophoresis technology and applications. J. Chromatogr. A. 705, 89-103
    • (1995) J. Chromatogr. A , vol.705 , pp. 89-103
    • Hu, G.F.1
  • 26
    • 0026201240 scopus 로고
    • Polyacrylamide gel electrophoresis of reducing saccharides labeled with the fluorophore 2-aminoacridone: Subpicomolar detection using an imaging system based on a cooled charge-coupled device
    • Jackson, P. (1991) Polyacrylamide gel electrophoresis of reducing saccharides labeled with the fluorophore 2-aminoacridone: subpicomolar detection using an imaging system based on a cooled charge-coupled device. Anal. Biochem. 196, 238-244
    • (1991) Anal. Biochem. , vol.196 , pp. 238-244
    • Jackson, P.1
  • 27
    • 0030569057 scopus 로고    scopus 로고
    • Organization, evolutionary conservation, expression and unusual Alu density of the human gene for pigment epithelium-derived factor, a unique neurotrophic serpin
    • Tombran-Tink, J., Mazuruk, K., Rodriguez, I. R., Chung, D., Linker, T., Englander, E. and Chader, G. J. (1996) Organization, evolutionary conservation, expression and unusual Alu density of the human gene for pigment epithelium-derived factor, a unique neurotrophic serpin. Mol. Vis. 2, 11 (http://www.molvis.org/molvis/)
    • (1996) Mol. Vis. , vol.2 , pp. 11
    • Tombran-Tink, J.1    Mazuruk, K.2    Rodriguez, I.R.3    Chung, D.4    Linker, T.5    Englander, E.6    Chader, G.J.7
  • 28
    • 0032511013 scopus 로고    scopus 로고
    • Isolation, purification, and characterization of a collagen-associated serpin, caspin, produced by murine colon adenocarcinoma cells
    • Kozaki, K., Miyaishi, O., Koiwai, O., Yasui, Y., Kashiwai, A., Nishikawa, Y., Shimizu, S. and Saga, S. (1998) Isolation, purification, and characterization of a collagen-associated serpin, caspin, produced by murine colon adenocarcinoma cells. J. Biol. Chem. 273, 15125-15130
    • (1998) J. Biol. Chem. , vol.273 , pp. 15125-15130
    • Kozaki, K.1    Miyaishi, O.2    Koiwai, O.3    Yasui, Y.4    Kashiwai, A.5    Nishikawa, Y.6    Shimizu, S.7    Saga, S.8
  • 29
    • 0032549956 scopus 로고    scopus 로고
    • Structural and comparative analysis of the mouse gene for pigment epithelium-derived factor (PEDF)
    • Singh, V. K., Chader, G. J. and Rodriguez, I. R. (1998) Structural and comparative analysis of the mouse gene for pigment epithelium-derived factor (PEDF). Mol. Vis. 4, 7 (http://www.malvis.org/molvis/)
    • (1998) Mol. Vis. , vol.4 , pp. 7
    • Singh, V.K.1    Chader, G.J.2    Rodriguez, I.R.3
  • 30
    • 0037160083 scopus 로고    scopus 로고
    • Mapping the type I collagen-binding site on pigment epithelium-derived factor. Implications for its antiangiogenic activity
    • Meyer, C., Notari, L. and Becerra, S. P. (2002) Mapping the type I collagen-binding site on pigment epithelium-derived factor. Implications for its antiangiogenic activity. J. Biol. Chem. 277, 45400-45407
    • (2002) J. Biol. Chem. , vol.277 , pp. 45400-45407
    • Meyer, C.1    Notari, L.2    Becerra, S.P.3
  • 32
    • 0033517356 scopus 로고    scopus 로고
    • Cutaneous wound healing
    • Singer, A. J. and Clark, R. A. (1999) Cutaneous wound healing. N. Engl. J. Med. 341, 738-746
    • (1999) N. Engl. J. Med. , vol.341 , pp. 738-746
    • Singer, A.J.1    Clark, R.A.2
  • 33
    • 0019784255 scopus 로고
    • Pyroglutamic acid. Non-metabolic formation, function in proteins and peptides, and characteristics of the enzymes effecting its removal
    • Abraham, G. N. and Podell, D. N. (1981) Pyroglutamic acid. Non-metabolic formation, function in proteins and peptides, and characteristics of the enzymes effecting its removal. Mol. Cell. Biochem. 38 (Special number), 181-190
    • (1981) N. Mol. Cell. Biochem. , vol.38 , Issue.SPECIAL NUMBER , pp. 181-190
    • Abraham, G.N.1    Podell, D.N.2
  • 34
    • 0028266432 scopus 로고
    • Refined 1.7 Å X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity
    • Mosimann, S. C., Ardelt, W. and James, M. N. (1994) Refined 1.7 Å X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity. J. Mol. Biol. 236, 1141-1153
    • (1994) J. Mol. Biol. , vol.236 , pp. 1141-1153
    • Mosimann, S.C.1    Ardelt, W.2    James, M.N.3
  • 35
    • 0018193575 scopus 로고
    • Cyclic analogues of luteinizing hormone-releasing hormone with significant biological activities
    • Seprodi, J., Coy, D. H., Vilchez-Martinez, J. A., Pedroza, E., Huang, W. Y. and Schally, A. V. (1978) Cyclic analogues of luteinizing hormone-releasing hormone with significant biological activities. J. Med. Chem. 21, 993-995
    • (1978) J. Med. Chem. , vol.21 , pp. 993-995
    • Seprodi, J.1    Coy, D.H.2    Vilchez-Martinez, J.A.3    Pedroza, E.4    Huang, W.Y.5    Schally, A.V.6
  • 36
    • 0036297892 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor exerts apposite effects on endothelial cells of different phenotypes
    • Hutchings, H., Maitre-Boube, M., Tombran-Tink, J. and Plouet, J. (2002) Pigment epithelium-derived factor exerts apposite effects on endothelial cells of different phenotypes. Biochem. Biophys. Res. Commun. 294, 764-769
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 764-769
    • Hutchings, H.1    Maitre-Boube, M.2    Tombran-Tink, J.3    Plouet, J.4
  • 37
    • 0032424256 scopus 로고    scopus 로고
    • Pyroglutamyl peptidase: An overview of the three known enzymatic forms
    • Cummins, P. M. and O'Connor, B. (1998) Pyroglutamyl peptidase: an overview of the three known enzymatic forms. Biochim. Biophys. Acta. 1429, 1-17
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 1-17
    • Cummins, P.M.1    O'Connor, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.