메뉴 건너뛰기




Volumn 389, Issue 2, 2005, Pages 249-257

A short guided tour through functional and structural features of saposin-like proteins

Author keywords

Antimicrobial activity; Innate immunity; Lipid metabolism; Lipid binding; Membrane interaction; Saposin like protein

Indexed keywords

CELL CULTURE; CELLS; GENES; LIPIDS; MICROORGANISMS;

EID: 22544463623     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050051     Document Type: Review
Times cited : (167)

References (100)
  • 1
    • 0029126584 scopus 로고
    • Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
    • Munford, R. S., Sheppard, P. O. and O'Hara, P. J. (1995) Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure. J. Lipid Res. 36, 1653-1663
    • (1995) J. Lipid Res. , vol.36 , pp. 1653-1663
    • Munford, R.S.1    Sheppard, P.O.2    O'Hara, P.J.3
  • 2
    • 0028353499 scopus 로고
    • Acid sphingomyelinase possesses a domain homologous to its activator proteins: Saposins B and D
    • Ponting, C. P. (1994) Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D. Protein Sci. 3, 359-361
    • (1994) Protein Sci. , vol.3 , pp. 359-361
    • Ponting, C.P.1
  • 3
    • 0026661998 scopus 로고
    • Acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides, has phospholipase, lysophospholipase, diacylglycerollipase, and acyltransferase activities in vitro
    • Munford, R. S. and Hunter, J. P. (1992) Acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides, has phospholipase, lysophospholipase, diacylglycerollipase, and acyltransferase activities in vitro. J. Biol. Chem. 267, 10116-10121
    • (1992) J. Biol. Chem. , vol.267 , pp. 10116-10121
    • Munford, R.S.1    Hunter, J.P.2
  • 4
    • 0026768211 scopus 로고
    • Saposins: Structure, function, distribution, and molecular genetics
    • Kishimoto, Y., Hiraiwa, M. and O'Brien, J. S. (1992) Saposins: structure, function, distribution, and molecular genetics. J. Lipid Res. 33, 1255-1267
    • (1992) J. Lipid Res. , vol.33 , pp. 1255-1267
    • Kishimoto, Y.1    Hiraiwa, M.2    O'Brien, J.S.3
  • 5
    • 0034939951 scopus 로고    scopus 로고
    • Sphingolipid activator proteins: Proteins with complex functions in lipid degradation and skin biogenesis
    • Schuette, C. G., Pierstorff, B., Huettler, S. and Sandhoff, K. (2001) Sphingolipid activator proteins: proteins with complex functions in lipid degradation and skin biogenesis. Glycobiology 11, 81R-90R
    • (2001) Glycobiology , vol.11
    • Schuette, C.G.1    Pierstorff, B.2    Huettler, S.3    Sandhoff, K.4
  • 6
    • 0026347862 scopus 로고
    • Pulmonary surfactant protein B (SP-B): Structure-function relationships
    • Cochrane, C. G. and Revak, S. D. (1991) Pulmonary surfactant protein B (SP-B): structure-function relationships. Science 254, 566-568
    • (1991) Science , vol.254 , pp. 566-568
    • Cochrane, C.G.1    Revak, S.D.2
  • 7
    • 0031127454 scopus 로고    scopus 로고
    • Granulysin, a new human cytolytic granule-associated protein with possible involvement in cell-mediated cytotoxicity
    • Pena, S. V. and Krensky, A. M. (1997) Granulysin, a new human cytolytic granule-associated protein with possible involvement in cell-mediated cytotoxicity. Semin. Immunol. 9, 117-125
    • (1997) Semin. Immunol. , vol.9 , pp. 117-125
    • Pena, S.V.1    Krensky, A.M.2
  • 8
    • 0026705846 scopus 로고
    • Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene
    • Schnabel, D., Schröder, M., Fürst, W., Klein, A., Hurwitz, R., Zenk, T., Weber, J., Harzer, K., Paton, B. C., Poulos, A. et al. (1992) Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene. J. Biol. Chem. 267, 3312-3315
    • (1992) J. Biol. Chem. , vol.267 , pp. 3312-3315
    • Schnabel, D.1    Schröder, M.2    Fürst, W.3    Klein, A.4    Hurwitz, R.5    Zenk, T.6    Weber, J.7    Harzer, K.8    Paton, B.C.9    Poulos, A.10
  • 9
    • 0025743034 scopus 로고
    • Sulfatide activator protein: Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease
    • Holtschmidt, H., Sandhoff, K., Kwon, H. Y., Harzer, K., Nakano, T. and Suzuki, K. (1991) Sulfatide activator protein: alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease. J. Biol. Chem. 266, 7556-7560
    • (1991) J. Biol. Chem. , vol.266 , pp. 7556-7560
    • Holtschmidt, H.1    Sandhoff, K.2    Kwon, H.Y.3    Harzer, K.4    Nakano, T.5    Suzuki, K.6
  • 12
    • 0024435444 scopus 로고
    • Activator protein deficient Gaucher's disease: A second patient with the newly identified lipid storage disorder
    • Christomanou, H., Chabas, A., Pampols, T. and Guardiola, A. (1989) Activator protein deficient Gaucher's disease: a second patient with the newly identified lipid storage disorder. Klin. Wochenschr. 67, 999-1003
    • (1989) Klin. Wochenschr. , vol.67 , pp. 999-1003
    • Christomanou, H.1    Chabas, A.2    Pampols, T.3    Guardiola, A.4
  • 13
    • 0025762364 scopus 로고
    • Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease
    • Schnabel, D., Schröder, M. and Sandhoff, K. (1991) Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease. FEBS Lett. 284, 57-59
    • (1991) FEBS Lett. , vol.284 , pp. 57-59
    • Schnabel, D.1    Schröder, M.2    Sandhoff, K.3
  • 14
    • 0037180829 scopus 로고    scopus 로고
    • Hydrophobic surfactant proteins in lung function and disease
    • Whitsett, J. A. and Weaver, T. E. (2002) Hydrophobic surfactant proteins in lung function and disease. N. Engl. J. Med. 347, 2141-2148
    • (2002) N. Engl. J. Med. , vol.347 , pp. 2141-2148
    • Whitsett, J.A.1    Weaver, T.E.2
  • 16
    • 0027466161 scopus 로고
    • Brief report: Deficiency of pulmonary surfactant protein B in congenital alveolar proteinosis
    • Nogee, L. M., de Mello, D. E., Dehner, L. P. and Colten, H. R. (1993) Brief report: deficiency of pulmonary surfactant protein B in congenital alveolar proteinosis. N. Engl. J. Med. 328, 406-410
    • (1993) N. Engl. J. Med. , vol.328 , pp. 406-410
    • Nogee, L.M.1    De Mello, D.E.2    Dehner, L.P.3    Colten, H.R.4
  • 17
    • 0037762571 scopus 로고    scopus 로고
    • Biosynthesis and degradation of mammalian glycosphingolipids
    • Sandhoff, K. and Kolter, T. (2003) Biosynthesis and degradation of mammalian glycosphingolipids. Philos. Trans. R. Soc. London Ser. B 358, 847-861
    • (2003) Philos. Trans. R. Soc. London Ser. B , vol.358 , pp. 847-861
    • Sandhoff, K.1    Kolter, T.2
  • 18
    • 0025787230 scopus 로고
    • Glycosphingolipid specificity of the human sulfatide activator protein
    • Vogel, A., Schwarzmann, G. and Sandhoff, K. (1991) Glycosphingolipid specificity of the human sulfatide activator protein. Eur. J. Biochem. 200, 591-597
    • (1991) Eur. J. Biochem. , vol.200 , pp. 591-597
    • Vogel, A.1    Schwarzmann, G.2    Sandhoff, K.3
  • 19
    • 0019513677 scopus 로고
    • Mechanism of activation of glucocerebrosidase by co-β-glucosidase (glucosidase activator protein)
    • Berent, S. L. and Radin, N. S. (1981) Mechanism of activation of glucocerebrosidase by co-β-glucosidase (glucosidase activator protein). Biochim. Biophys. Acta 664, 572-582
    • (1981) Biochim. Biophys. Acta , vol.664 , pp. 572-582
    • Berent, S.L.1    Radin, N.S.2
  • 21
    • 0020482329 scopus 로고
    • A protein activator of galactosylceramide β-galactosidase
    • Wenger, D. A., Sattler, M. and Roth, S. (1982) A protein activator of galactosylceramide β-galactosidase. Biochim. Biophys. Acta 712, 639-649
    • (1982) Biochim. Biophys. Acta , vol.712 , pp. 639-649
    • Wenger, D.A.1    Sattler, M.2    Roth, S.3
  • 24
    • 0028275240 scopus 로고
    • Sphingolipid activator protein D (sap-D) stimulates the lysosomal degradation of ceramide in vivo
    • Klein, A., Henseler, M., Klein, C., Suzuki, K., Harzer, K. and Sandhoff, K. (1994) Sphingolipid activator protein D (sap-D) stimulates the lysosomal degradation of ceramide in vivo. Biochem. Biophys. Res. Commun. 200, 1440-1448
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 1440-1448
    • Klein, A.1    Henseler, M.2    Klein, C.3    Suzuki, K.4    Harzer, K.5    Sandhoff, K.6
  • 26
    • 0037518438 scopus 로고    scopus 로고
    • Physiological relevance of sphingolipid activator proteins in cultured human fibroblasts
    • Sadeghlar, F., Remmel, N., Breiden, B., Klingenstein, R., Schwarzmann, G. and Sandhoff, K. (2003) Physiological relevance of sphingolipid activator proteins in cultured human fibroblasts. Biochimie 85, 439-448
    • (2003) Biochimie , vol.85 , pp. 439-448
    • Sadeghlar, F.1    Remmel, N.2    Breiden, B.3    Klingenstein, R.4    Schwarzmann, G.5    Sandhoff, K.6
  • 27
    • 0027181185 scopus 로고
    • Binding of cerebrosides and sulfatides to saposins A-D
    • Soeda, S., Hiraiwa, M., O'Brien, J. S. and Kishimoto, Y. (1993) Binding of cerebrosides and sulfatides to saposins A-D. J. Biol. Chem. 268, 18519-18523
    • (1993) J. Biol. Chem. , vol.268 , pp. 18519-18523
    • Soeda, S.1    Hiraiwa, M.2    O'Brien, J.S.3    Kishimoto, Y.4
  • 28
    • 0029417339 scopus 로고
    • H-dependent conformational properties of saposins and their interactions with phospholipid membranes
    • Vaccaro, A. M., Ciaffoni, F., Tatti, M., Salvioli, R., Barca, A., Tognozzi, D. and Scerch, C. (1995) pH-dependent conformational properties of saposins and their interactions with phospholipid membranes. J. Biol. Chem. 270, 30576-30580
    • (1995) J. Biol. Chem. , vol.270 , pp. 30576-30580
    • Vaccaro, A.M.1    Ciaffoni, F.2    Tatti, M.3    Salvioli, R.4    Barca, A.5    Tognozzi, D.6    Scerch, C.7
  • 30
    • 1642504446 scopus 로고    scopus 로고
    • Fusogenic domain and lysines in saposin C
    • Qi, X. and Chu, Z. (2004) Fusogenic domain and lysines in saposin C. Arch. Biochem. Biophys. 424, 210-218
    • (2004) Arch. Biochem. Biophys. , vol.424 , pp. 210-218
    • Qi, X.1    Chu, Z.2
  • 31
    • 0037834892 scopus 로고    scopus 로고
    • Phospholipid vesicle fusion induced by saposin C
    • Wang, Y., Grabowski, G. A. and Qi, X. (2003) Phospholipid vesicle fusion induced by saposin C. Arch. Biochem. Biophys. 415, 43-53
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 43-53
    • Wang, Y.1    Grabowski, G.A.2    Qi, X.3
  • 32
    • 7644235520 scopus 로고    scopus 로고
    • Direct AFM observation of saposin C-induced membrane domains in lipid bilayers: From simple to complex lipid mixtures
    • You, H. X., Qi, X. and Yu, L. (2004) Direct AFM observation of saposin C-induced membrane domains in lipid bilayers: from simple to complex lipid mixtures. Chem. Phys. Lipids 132, 15-22
    • (2004) Chem. Phys. Lipids , vol.132 , pp. 15-22
    • You, H.X.1    Qi, X.2    Yu, L.3
  • 33
    • 0042569070 scopus 로고    scopus 로고
    • Interaction of saposin D with membranes: Effect of anionic phospholipids and sphingolipids
    • Ciaffoni, F., Tatti, M., Salvioli, R. and Vaccaro, A. M. (2003) Interaction of saposin D with membranes: effect of anionic phospholipids and sphingolipids. Biochem. J. 373, 785-792
    • (2003) Biochem. J. , vol.373 , pp. 785-792
    • Ciaffoni, F.1    Tatti, M.2    Salvioli, R.3    Vaccaro, A.M.4
  • 35
    • 0026634092 scopus 로고
    • Effects of surfactant apolipoproteins on liposome structure: Implications for tubular myelin formation
    • Poulain, F. R., Allen, L., Williams, M. C., Hamilton, R. L. and Hawgood, S. (1992) Effects of surfactant apolipoproteins on liposome structure: implications for tubular myelin formation. Am. J. Physiol. 262, L730-L739
    • (1992) Am. J. Physiol. , vol.262
    • Poulain, F.R.1    Allen, L.2    Williams, M.C.3    Hamilton, R.L.4    Hawgood, S.5
  • 36
    • 0030029465 scopus 로고    scopus 로고
    • Kinetics of phospholipid membrane fusion induced by surfactant apoproteins A and B
    • Poulain, F. R., Nir, S. and Hawgood, S. (1996) Kinetics of phospholipid membrane fusion induced by surfactant apoproteins A and B. Biochim. Biophys. Acta 1278, 169-175
    • (1996) Biochim. Biophys. Acta , vol.1278 , pp. 169-175
    • Poulain, F.R.1    Nir, S.2    Hawgood, S.3
  • 37
    • 0001759382 scopus 로고    scopus 로고
    • Analysis of binding and membrane destabilization of phospholipid membranes by surfactant apoprotein B
    • Chang, R., Nir, S. and Poulain, F. R. (1998) Analysis of binding and membrane destabilization of phospholipid membranes by surfactant apoprotein B. Biochim. Biophys. Acta 1371, 254-264
    • (1998) Biochim. Biophys. Acta , vol.1371 , pp. 254-264
    • Chang, R.1    Nir, S.2    Poulain, F.R.3
  • 38
    • 0031569218 scopus 로고    scopus 로고
    • Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins
    • Pena, S. V., Hanson, D. A., Carr, B. A., Goralski, T. J. and Krensky, A. M. (1997) Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins. J. Immunol. 158, 2680-2688
    • (1997) J. Immunol. , vol.158 , pp. 2680-2688
    • Pena, S.V.1    Hanson, D.A.2    Carr, B.A.3    Goralski, T.J.4    Krensky, A.M.5
  • 39
    • 0029061894 scopus 로고
    • NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity
    • Andersson, M., Gunne, H., Agerberth, B., Boman, A., Bergman, T., Sillard, R., Jornvall, H., Mutt, V., Olsson, B., Wigzell, H. et al. (1995) NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity. EMBO J. 14, 1615-1625
    • (1995) EMBO J. , vol.14 , pp. 1615-1625
    • Andersson, M.1    Gunne, H.2    Agerberth, B.3    Boman, A.4    Bergman, T.5    Sillard, R.6    Jornvall, H.7    Mutt, V.8    Olsson, B.9    Wigzell, H.10
  • 40
    • 0037111316 scopus 로고    scopus 로고
    • CD8 T cell-mediated killing of Cryptococcus neoformans requires granulysin and is dependent on CD4 T cells and IL-15
    • Ma, L. L., Spurrell, J. C., Wang, J. F., Neely, G. G., Epelman, S., Krensky, A. M. and Mody, C. H. (2002) CD8 T cell-mediated killing of Cryptococcus neoformans requires granulysin and is dependent on CD4 T cells and IL-15. J. Immunol. 169, 5787-5795
    • (2002) J. Immunol. , vol.169 , pp. 5787-5795
    • Ma, L.L.1    Spurrell, J.C.2    Wang, J.F.3    Neely, G.G.4    Epelman, S.5    Krensky, A.M.6    Mody, C.H.7
  • 41
    • 0037308713 scopus 로고    scopus 로고
    • NK-lysin and its shortened analog NK-2 exhibit potent activities against Trypanosoma cruzi
    • Jacobs, T., Bruhn, H., Gaworski, I., Fleischer, B. and Leippe, M. (2003) NK-lysin and its shortened analog NK-2 exhibit potent activities against Trypanosoma cruzi. Antimicrob. Agents Chemother. 47, 607-613
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 607-613
    • Jacobs, T.1    Bruhn, H.2    Gaworski, I.3    Fleischer, B.4    Leippe, M.5
  • 44
    • 4444360018 scopus 로고    scopus 로고
    • γ δ 5 T cells inhibit in vitro growth of the asexual blood stages of Plasmodium talciparum by a granule exocytosis-dependent cytotoxic pathway that requires granulysin
    • Farouk, S. E., Mincheva-Nilsson, L., Krensky, A. M., Dieli, F. and Troye-Blomberg, M. (2004) γ δ 5 T cells inhibit in vitro growth of the asexual blood stages of Plasmodium talciparum by a granule exocytosis-dependent cytotoxic pathway that requires granulysin. Eur. J. Immunol. 34, 2248-2256
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2248-2256
    • Farouk, S.E.1    Mincheva-Nilsson, L.2    Krensky, A.M.3    Dieli, F.4    Troye-Blomberg, M.5
  • 45
    • 0033572639 scopus 로고    scopus 로고
    • Identification of an anti-mycobacterial domain in NK-lysin and granulysin
    • Andreu, D., Carreno, C., Linde, C., Boman, H. G. and Andersson, M. (1999) Identification of an anti-mycobacterial domain in NK-lysin and granulysin. Biochem. J. 344, 845-849
    • (1999) Biochem. J. , vol.344 , pp. 845-849
    • Andreu, D.1    Carreno, C.2    Linde, C.3    Boman, H.G.4    Andersson, M.5
  • 48
    • 0042430267 scopus 로고    scopus 로고
    • Intracellular mediators of granulysin-induced cell death
    • Okada, S., Li, Q., Whitin, J. C., Clayberger, C. and Krensky, A. M. (2003) Intracellular mediators of granulysin-induced cell death. J. Immunol. 171, 2556-2562
    • (2003) J. Immunol. , vol.171 , pp. 2556-2562
    • Okada, S.1    Li, Q.2    Whitin, J.C.3    Clayberger, C.4    Krensky, A.M.5
  • 50
    • 0028073698 scopus 로고
    • Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: Isolation, primary structure, and pore formation in bacterial cytoplasmic membranes
    • Leippe, M., Andrä, J., Nickel, R., Tannich, E. and Müller-Eberhard, H. J. (1994) Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes. Mol. Microbiol. 14, 895-904
    • (1994) Mol. Microbiol. , vol.14 , pp. 895-904
    • Leippe, M.1    Andrä, J.2    Nickel, R.3    Tannich, E.4    Müller-Eberhard, H.J.5
  • 51
    • 0030950248 scopus 로고    scopus 로고
    • Amoebapores
    • Leippe, M. (1997) Amoebapores. Parasitol. Today 13, 178-183
    • (1997) Parasitol. Today , vol.13 , pp. 178-183
    • Leippe, M.1
  • 52
    • 0028880453 scopus 로고
    • Ancient weapons: NK-lysin, is a mammalian homolog to pore-forming peptides of a protozoan parasite
    • Leippe, M. (1995) Ancient weapons: NK-lysin, is a mammalian homolog to pore-forming peptides of a protozoan parasite. Cell 83, 17-18
    • (1995) Cell , vol.83 , pp. 17-18
    • Leippe, M.1
  • 53
    • 0242637041 scopus 로고    scopus 로고
    • Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals: A comparative functional analysis
    • Bruhn, H., Riekens, B., Berninghausen, O. and Leippe, M. (2003) Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals: a comparative functional analysis. Biochem. J. 375, 737-744
    • (2003) Biochem. J. , vol.375 , pp. 737-744
    • Bruhn, H.1    Riekens, B.2    Berninghausen, O.3    Leippe, M.4
  • 54
    • 0031033595 scopus 로고    scopus 로고
    • Calcium-independent cytolysis of target cells induced by Entamoeba histolytica
    • Berninghausen, O. and Leippe, M. (1997) Calcium-independent cytolysis of target cells induced by Entamoeba histolytica. Arch. Med. Res. 28, 158-160
    • (1997) Arch. Med. Res. , vol.28 , pp. 158-160
    • Berninghausen, O.1    Leippe, M.2
  • 55
    • 0242467808 scopus 로고    scopus 로고
    • A virulence attenuated amoebapore-less mutant of Entamoeba histolytica and its interaction with host cells
    • Bujanover, S., Katz, U., Bracha, R. and Mirelman, D. (2003) A virulence attenuated amoebapore-less mutant of Entamoeba histolytica and its interaction with host cells. Int. J. Parasitol. 33, 1655-1663
    • (2003) Int. J. Parasitol. , vol.33 , pp. 1655-1663
    • Bujanover, S.1    Katz, U.2    Bracha, R.3    Mirelman, D.4
  • 56
    • 0037721200 scopus 로고    scopus 로고
    • Transcriptional silencing of an amoebapore gene in Entamoeba histolytica: Molecular analysis and effect on pathogenicity
    • Bracha, R., Nuchamowitz, Y. and Mirelman, D. (2003) Transcriptional silencing of an amoebapore gene in Entamoeba histolytica: molecular analysis and effect on pathogenicity. Eukaryotic Cell 2, 295-305
    • (2003) Eukaryotic Cell , vol.2 , pp. 295-305
    • Bracha, R.1    Nuchamowitz, Y.2    Mirelman, D.3
  • 57
    • 0037391712 scopus 로고    scopus 로고
    • Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes
    • Andre, J., Herbst, R. and Leippe, M. (2003) Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes. Dev. Comp. Immunol. 27, 291-304
    • (2003) Dev. Comp. Immunol. , vol.27 , pp. 291-304
    • Andre, J.1    Herbst, R.2    Leippe, M.3
  • 58
    • 0042026495 scopus 로고    scopus 로고
    • Interaction of amoebapores and NK-lysin with symmetric phospholipid and asymmetric lipopolysaccharide/phospholipid bilayers
    • Gutsmann, T., Riekens, B., Bruhn, H., Wiese, A., Seydel, U. and Leippe, M. (2003) Interaction of amoebapores and NK-lysin with symmetric phospholipid and asymmetric lipopolysaccharide/phospholipid bilayers. Biochemistry 42, 9804-9812
    • (2003) Biochemistry , vol.42 , pp. 9804-9812
    • Gutsmann, T.1    Riekens, B.2    Bruhn, H.3    Wiese, A.4    Seydel, U.5    Leippe, M.6
  • 59
    • 0033978798 scopus 로고    scopus 로고
    • A novel member of the NK-lysin protein family is developmentally regulated and secreted by Fasciola hepatica
    • Reed, M. B., Strugnell, R. A., Panaccio, M. and Spithill, T. W. (2000) A novel member of the NK-lysin protein family is developmentally regulated and secreted by Fasciola hepatica. Mol. Biochem. Parasitol. 105, 297-303
    • (2000) Mol. Biochem. Parasitol. , vol.105 , pp. 297-303
    • Reed, M.B.1    Strugnell, R.A.2    Panaccio, M.3    Spithill, T.W.4
  • 60
    • 0037668642 scopus 로고    scopus 로고
    • Molecular cloning of a member of the Fasciola hepatica saposin-like protein family
    • Espino, A. M. and Hillyer, G. V. (2003) Molecular cloning of a member of the Fasciola hepatica saposin-like protein family. J. Parasitol. 89, 545-552
    • (2003) J. Parasitol. , vol.89 , pp. 545-552
    • Espino, A.M.1    Hillyer, G.V.2
  • 62
    • 2942702023 scopus 로고    scopus 로고
    • Antimicrobial and pore-forming peptides of free-living and potentially highly pathogenic Naegleria fowleri are released from the same precursor molecule
    • Herbst, R., Marciano-Cabral, F. and Leippe, M. (2004) Antimicrobial and pore-forming peptides of free-living and potentially highly pathogenic Naegleria fowleri are released from the same precursor molecule. J. Biol. Chem. 279, 25955-25958
    • (2004) J. Biol. Chem. , vol.279 , pp. 25955-25958
    • Herbst, R.1    Marciano-Cabral, F.2    Leippe, M.3
  • 63
  • 64
    • 0345291179 scopus 로고    scopus 로고
    • Amoebapore homologs of Caenorhabditis elegans
    • Banyai, L. and Patthy, L. (1998) Amoebapore homologs of Caenorhabditis elegans. Biochim. Biophys. Acta 1429, 259-264
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 259-264
    • Banyai, L.1    Patthy, L.2
  • 66
    • 0034623993 scopus 로고    scopus 로고
    • The saposin-like domain of the plant aspartic proteinase precursor is a potent inducer of vesicle leakage
    • Egas, C., Lavoura, N., Resende, R., Brito, R. M., Pires, E., de Lima, M. C. and Faro, C. (2000) The saposin-like domain of the plant aspartic proteinase precursor is a potent inducer of vesicle leakage. J. Biol. Chem. 275, 38190-38196
    • (2000) J. Biol. Chem. , vol.275 , pp. 38190-38196
    • Egas, C.1    Lavoura, N.2    Resende, R.3    Brito, R.M.4    Pires, E.5    De Lima, M.C.6    Faro, C.7
  • 67
    • 0033565640 scopus 로고    scopus 로고
    • Crystal structure of plant aspartic proteinase prophytepsin: Inactivation and vacuolar targeting
    • Kervinen, J., Tobin, G. J., Costa, J., Waugh, D. S., Wlodawer, A. and Zdanov, A. (1999) Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting. EMBO J. 18, 3947-3955
    • (1999) EMBO J. , vol.18 , pp. 3947-3955
    • Kervinen, J.1    Tobin, G.J.2    Costa, J.3    Waugh, D.S.4    Wlodawer, A.5    Zdanov, A.6
  • 68
    • 0034808250 scopus 로고    scopus 로고
    • A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum
    • Tormakangas, K., Hadlington, J. L., Pimpl, P., Hillmer, S., Brandizzi, F., Teeri, T. H. and Denecke, J. (2001) A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum. Plant Cell 13, 2021-2032
    • (2001) Plant Cell , vol.13 , pp. 2021-2032
    • Tormakangas, K.1    Hadlington, J.L.2    Pimpl, P.3    Hillmer, S.4    Brandizzi, F.5    Teeri, T.H.6    Denecke, J.7
  • 69
    • 0027955997 scopus 로고
    • A saposin-like domain influences the intracellular localization, stability, and catalytic activity of human acyloxyacyl hydrolase
    • Staab, J. F., Ginkel, D. L., Rosenberg, G. B. and Munford, R. S. (1994) A saposin-like domain influences the intracellular localization, stability, and catalytic activity of human acyloxyacyl hydrolase. J. Biol. Chem. 269, 23736-23742
    • (1994) J. Biol. Chem. , vol.269 , pp. 23736-23742
    • Staab, J.F.1    Ginkel, D.L.2    Rosenberg, G.B.3    Munford, R.S.4
  • 70
    • 0035801644 scopus 로고    scopus 로고
    • Purification, cloning and characterization of a GPI inositol deacylase from Trypanosoma brucei
    • Guther, M. L., Leal, S., Morrice, N. A., Cross, G. A. and Ferguson, M. A. (2001) Purification, cloning and characterization of a GPI inositol deacylase from Trypanosoma brucei. EMBO J. 20, 4923-4934
    • (2001) EMBO J. , vol.20 , pp. 4923-4934
    • Guther, M.L.1    Leal, S.2    Morrice, N.A.3    Cross, G.A.4    Ferguson, M.A.5
  • 71
    • 12144281320 scopus 로고    scopus 로고
    • Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase
    • Kölzer, M., Ferlinz, K., Bartelsen, O., Locatelli-Hoops, S., Lang, F. and Sandhoff, K. (2004) Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase. Biol. Chem. 385, 1193-1195
    • (2004) Biol. Chem. , vol.385 , pp. 1193-1195
    • Kölzer, M.1    Ferlinz, K.2    Bartelsen, O.3    Locatelli-Hoops, S.4    Lang, F.5    Sandhoff, K.6
  • 72
    • 0035801842 scopus 로고    scopus 로고
    • Novel putative saposin-like proteins of Entamoeba histolytica different from amoebapores
    • Bruhn, H. and Leippe, M. (2001) Novel putative saposin-like proteins of Entamoeba histolytica different from amoebapores. Biochim. Biophys. Acta 1514, 14-20
    • (2001) Biochim. Biophys. Acta , vol.1514 , pp. 14-20
    • Bruhn, H.1    Leippe, M.2
  • 73
    • 0033180415 scopus 로고    scopus 로고
    • A cell-counting factor regulating structure size in Dictyostelium
    • Brock, D. A. and Gomer, R. H. (1999) A cell-counting factor regulating structure size in Dictyostelium. Genes Dev. 13, 1960-1969
    • (1999) Genes Dev. , vol.13 , pp. 1960-1969
    • Brock, D.A.1    Gomer, R.H.2
  • 74
    • 6344231664 scopus 로고    scopus 로고
    • A cell number counting factor regulates Akt/protein kinase B to regulate Dictyostelium discoideum group size
    • Gao, T., Knecht, D., Tang, L., Hatton, R. D. and Gomer, R. H. (2004) A cell number counting factor regulates Akt/protein kinase B to regulate Dictyostelium discoideum group size. Eukaryotic Cell 3, 1176-1184
    • (2004) Eukaryotic Cell , vol.3 , pp. 1176-1184
    • Gao, T.1    Knecht, D.2    Tang, L.3    Hatton, R.D.4    Gomer, R.H.5
  • 77
    • 1142263116 scopus 로고    scopus 로고
    • Saposins facilitate CD1d-restricted presentation of an exogenous lipid antigen to T cells
    • Kang, S. J. and Cresswell, P. (2004) Saposins facilitate CD1d-restricted presentation of an exogenous lipid antigen to T cells. Nat. Immunol. 5, 175-181
    • (2004) Nat. Immunol. , vol.5 , pp. 175-181
    • Kang, S.J.1    Cresswell, P.2
  • 79
    • 0033179450 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase and Akt protein kinase mediate IGF-I- and prosaptide-induced survival in Schwann cells
    • Campana, W. M., Darin, S. J. and O'Brien, J. S. (1999) Phosphatidylinositol 3-kinase and Akt protein kinase mediate IGF-I- and prosaptide-induced survival in Schwann cells. J. Neurosci. Res. 57, 332-341
    • (1999) J. Neurosci. Res. , vol.57 , pp. 332-341
    • Campana, W.M.1    Darin, S.J.2    O'Brien, J.S.3
  • 80
    • 0035127922 scopus 로고    scopus 로고
    • Prosaposin treatment induces PC12 entry in the S phase of the cell cycle and prevents apoptosis: Activation of ERKs and sphingosine kinase
    • Misasi, R., Sorice, M., Di Marzio, L., Campana, W. M., Molinari, S., Cifone, M. G., Pavan, A., Pontieri, G. M. and O'Brien, J. S. (2001) Prosaposin treatment induces PC12 entry in the S phase of the cell cycle and prevents apoptosis: activation of ERKs and sphingosine kinase. FASEB J. 15, 467-474
    • (2001) FASEB J. , vol.15 , pp. 467-474
    • Misasi, R.1    Sorice, M.2    Di Marzio, L.3    Campana, W.M.4    Molinari, S.5    Cifone, M.G.6    Pavan, A.7    Pontieri, G.M.8    O'Brien, J.S.9
  • 81
    • 0029988531 scopus 로고    scopus 로고
    • Prosaposin and prosaptide, a peptide from prosaposin, induce an increase in ganglioside content on NS20Y neuroblastoma cells
    • Misasi, R., Sorice, M., Carson, G. S., Griggi, T., Lenti, L., Pontieri, G. M. and O'Brien, J. S. (1996) Prosaposin and prosaptide, a peptide from prosaposin, induce an increase in ganglioside content on NS20Y neuroblastoma cells. Glycoconj. J. 13, 195-202
    • (1996) Glycoconj. J. , vol.13 , pp. 195-202
    • Misasi, R.1    Sorice, M.2    Carson, G.S.3    Griggi, T.4    Lenti, L.5    Pontieri, G.M.6    O'Brien, J.S.7
  • 83
    • 13644260925 scopus 로고    scopus 로고
    • Saposin C promotes survival and prevents apoptosis via PI3K/Akt-dependent pathway in prostate cancer cells
    • Lee, T. J., Sartor, O., Luftig, R. B. and Koochekpour, S. (2004) Saposin C promotes survival and prevents apoptosis via PI3K/Akt-dependent pathway in prostate cancer cells. Mol. Cancer 3, 31
    • (2004) Mol. Cancer , vol.3 , pp. 31
    • Lee, T.J.1    Sartor, O.2    Luftig, R.B.3    Koochekpour, S.4
  • 84
    • 0042818023 scopus 로고    scopus 로고
    • MSAP is a novel MIR-interacting protein that enhances neurite outgrowth and increases myosin regulatory light chain
    • Bornhauser, B. C., Olsson, P. A. and Lindholm, D. (2003) MSAP is a novel MIR-interacting protein that enhances neurite outgrowth and increases myosin regulatory light chain. J. Biol. Chem. 278, 35412-35420
    • (2003) J. Biol. Chem. , vol.278 , pp. 35412-35420
    • Bornhauser, B.C.1    Olsson, P.A.2    Lindholm, D.3
  • 85
    • 0033522237 scopus 로고    scopus 로고
    • Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank
    • Yokoyama-Kobayashi, M., Yamaguchi, T., Sekine, S. and Kato, S. (1999) Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank. Gene 228, 161-167
    • (1999) Gene , vol.228 , pp. 161-167
    • Yokoyama-Kobayashi, M.1    Yamaguchi, T.2    Sekine, S.3    Kato, S.4
  • 87
    • 4143050395 scopus 로고    scopus 로고
    • The trafficking of prosaposin (SGP-1) and GM2AP to the lysosomes of TM4 Sertoli cells is mediated by sortilin and monomeric adaptor proteins
    • Hassan, A. J., Zeng, J., Ni, X. and Morales, C. R. (2004) The trafficking of prosaposin (SGP-1) and GM2AP to the lysosomes of TM4 Sertoli cells is mediated by sortilin and monomeric adaptor proteins. Mol. Reprod. Dev. 68, 476-483
    • (2004) Mol. Reprod. Dev. , vol.68 , pp. 476-483
    • Hassan, A.J.1    Zeng, J.2    Ni, X.3    Morales, C.R.4
  • 88
    • 0345732689 scopus 로고    scopus 로고
    • The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin
    • Lefrancois, S., Zeng, J., Hassan, A. J., Canuel, M. and Morales, C. R. (2003) The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin. EMBO J. 22, 6430-6437
    • (2003) EMBO J. , vol.22 , pp. 6430-6437
    • Lefrancois, S.1    Zeng, J.2    Hassan, A.J.3    Canuel, M.4    Morales, C.R.5
  • 92
    • 0347625853 scopus 로고    scopus 로고
    • Solution structure of human saposin C: PH-dependent interaction with phospholipid vesicles
    • de Alba, E., Weiler, S. and Tjandra, N. (2003) Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles. Biochemistry 42, 14729-14740
    • (2003) Biochemistry , vol.42 , pp. 14729-14740
    • De Alba, E.1    Weiler, S.2    Tjandra, N.3
  • 95
    • 0032738115 scopus 로고    scopus 로고
    • Molecular electroporation: A unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin
    • Miteva, M., Andersson, M., Karshikoff, A. and Otting, G. (1999) Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin. FEBS Lett. 462, 155-158
    • (1999) FEBS Lett. , vol.462 , pp. 155-158
    • Miteva, M.1    Andersson, M.2    Karshikoff, A.3    Otting, G.4
  • 96
    • 0028072978 scopus 로고
    • Pore-forming peptide of Entamoeba histolytica: Significance of positively charged amino acid residues for its mode of action
    • Andra, J. and Leippe, M. (1994) Pore-forming peptide of Entamoeba histolytica: significance of positively charged amino acid residues for its mode of action. FEBS Lett. 354, 97-102
    • (1994) FEBS Lett. , vol.354 , pp. 97-102
    • Andra, J.1    Leippe, M.2
  • 97
    • 0034633634 scopus 로고    scopus 로고
    • Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin
    • Gonzalez, C., Langdon, G. M., Bruix, M., Galvez, A., Valdivia, E., Maqueda, M. and Rico, M. (2000) Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin. Proc. Natl. Acad. Sci. U.S.A. 97, 11221-11226
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11221-11226
    • Gonzalez, C.1    Langdon, G.M.2    Bruix, M.3    Galvez, A.4    Valdivia, E.5    Maqueda, M.6    Rico, M.7
  • 98
    • 0035862297 scopus 로고    scopus 로고
    • Monolayer characteristics of bacteriocin AS-48, pH effect and interactions with dipalmitoyl phosphatidic acid at the air-water interface
    • Abriouel, H., Sanchez-Gonzalez, J., Maqueda, M., Galvez, A., Valdivia, E. and Jose Galvez-Ruiz, M. (2001) Monolayer characteristics of bacteriocin AS-48, pH effect and interactions with dipalmitoyl phosphatidic acid at the air-water interface. J. Colloid Interface Sci. 233, 306-312
    • (2001) J. Colloid Interface Sci. , vol.233 , pp. 306-312
    • Abriouel, H.1    Sanchez-Gonzalez, J.2    Maqueda, M.3    Galvez, A.4    Valdivia, E.5    Jose Galvez-Ruiz, M.6
  • 100
    • 4444351828 scopus 로고    scopus 로고
    • Paradise lost and paradigm found
    • Lehrer, R. I. (2004) Paradise lost and paradigm found. Nat. Immunol. 5, 775-776
    • (2004) Nat. Immunol. , vol.5 , pp. 775-776
    • Lehrer, R.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.