메뉴 건너뛰기




Volumn 35, Issue 1, 2003, Pages 90-96

Mutations associated with neutropenia in dogs and humans disrupt intracellular transport of neutrophil elastase

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; LEUKOCYTE ELASTASE; MEMBRANE PROTEIN;

EID: 0041353534     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/ng1224     Document Type: Article
Times cited : (150)

References (29)
  • 1
    • 0002346723 scopus 로고    scopus 로고
    • Leukocyte elastase
    • ed. Woessner, J.F., Academic, San Diego
    • Bieth, J.G. Leukocyte elastase, in Handbook of Proteolytic Enzymes (ed. Woessner, J.F) 54-60 (Academic, San Diego, 1998).
    • (1998) Handbook of Proteolytic Enzymes , pp. 54-60
    • Bieth, J.G.1
  • 2
    • 0032757863 scopus 로고    scopus 로고
    • Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis
    • Horwitz, M., Benson, K.F., Person, R.E., Aprikyan, A.G. & Dale, D.C. Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis. Nat. Genet. 23, 433-436 (1999).
    • (1999) Nat. Genet. , vol.23 , pp. 433-436
    • Horwitz, M.1    Benson, K.F.2    Person, R.E.3    Aprikyan, A.G.4    Dale, D.C.5
  • 3
    • 0034307655 scopus 로고    scopus 로고
    • Mutations in the gene encoding neutrophil elastase in congenital and cyclic neutropenia
    • Dale, D.C. et al. Mutations in the gene encoding neutrophil elastase in congenital and cyclic neutropenia. Blood 96, 2317-2322 (2000).
    • (2000) Blood , vol.96 , pp. 2317-2322
    • Dale, D.C.1
  • 4
    • 0035957966 scopus 로고    scopus 로고
    • Characterization of mutant neutrophil elastase in severe congenital neutropenia
    • Li, F.Q. & Horwitz, M. Characterization of mutant neutrophil elastase in severe congenital neutropenia. J. Biol. Chem. 276, 14230-14241 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 14230-14241
    • Li, F.Q.1    Horwitz, M.2
  • 5
    • 0023137167 scopus 로고
    • Cyclic hormonogenesis in gray collie dogs: Interactions of hematopoietic and endocrine systems
    • Lothrop, C.D. Jr. et al. Cyclic hormonogenesis in gray collie dogs: interactions of hematopoietic and endocrine systems. Endocrinology 120, 1027-1032 (1987).
    • (1987) Endocrinology , vol.120 , pp. 1027-1032
    • Lothrop C.D., Jr.1
  • 6
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor
    • Dell'Angelica, E.C., Shotelersuk, V., Aguilar, R.C., Gahl, W.A. & Bonifacino, J.S. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor. Mol. Cell 3, 11-21 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 11-21
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 7
    • 0036157244 scopus 로고    scopus 로고
    • Nonsense mutations in ADTB3A cause complete deficiency of the β3A subunit of adaptor complex-3 and severe Hermansky-Pudlak syndrome type 2
    • Huizing, M. et al. Nonsense mutations in ADTB3A cause complete deficiency of the β3A subunit of adaptor complex-3 and severe Hermansky-Pudlak syndrome type 2. Pediatr. Res. 51, 150-158 (2002).
    • (2002) Pediatr. Res. , vol.51 , pp. 150-158
    • Huizing, M.1
  • 8
    • 0037139604 scopus 로고    scopus 로고
    • Genetic analyses of adaptin function from yeast to mammals
    • Boehm, M. & Bonifacino, J.S. Genetic analyses of adaptin function from yeast to mammals. Gene 286, 175-186 (2002).
    • (2002) Gene , vol.286 , pp. 175-186
    • Boehm, M.1    Bonifacino, J.S.2
  • 9
    • 0030926547 scopus 로고    scopus 로고
    • Characterization of the adaptor-related protein complex, AP-3
    • Simpson, F., Peden, A.A., Christopoulou, L. & Robinson, M.S. Characterization of the adaptor-related protein complex, AP-3. J. Cell Biol. 137, 835-845 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 835-845
    • Simpson, F.1    Peden, A.A.2    Christopoulou, L.3    Robinson, M.S.4
  • 10
    • 0033620656 scopus 로고    scopus 로고
    • Molecular bases for the recognition of tyrosine-based sorting signals
    • Bonifacino, J.S. & Dell'Angelica, E.C. Molecular bases for the recognition of tyrosine-based sorting signals. J. Cell Biol. 145, 923-926 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 923-926
    • Bonifacino, J.S.1    Dell'Angelica, E.C.2
  • 11
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site
    • Rapoport, I., Chen, Y.C., Cupers, P., Shoelson, S.E. & Kirchhausen, T. Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J. 17, 2148-2155 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2148-2155
    • Rapoport, I.1    Chen, Y.C.2    Cupers, P.3    Shoelson, S.E.4    Kirchhausen, T.5
  • 12
    • 0032587547 scopus 로고    scopus 로고
    • The β3A subunit gene (Ap3b1) of the AP-3 adaptor complex is altered in the mouse hypopigmentation mutant pearl, a model for Hermansky-Pudlak syndrome and night blindness
    • Feng, L. et al. The β3A subunit gene (Ap3b1) of the AP-3 adaptor complex is altered in the mouse hypopigmentation mutant pearl, a model for Hermansky-Pudlak syndrome and night blindness. Hum. Mol. Genet. 8, 323-330 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 323-330
    • Feng, L.1
  • 13
    • 0035918168 scopus 로고    scopus 로고
    • Signal-binding specificity of the μ4 subunit of the adaptor protein complex AP-4
    • Aguilar, R.C. et al. Signal-binding specificity of the μ4 subunit of the adaptor protein complex AP-4. J. Biol. Chem. 276, 13145-13152 (2001)
    • (2001) J. Biol. Chem. , vol.276 , pp. 13145-13152
    • Aguilar, R.C.1
  • 14
    • 0029073056 scopus 로고
    • Carboxyl-terminal prodomain-deleted human leukocyte elastase and cathepsin G are efficiently targeted to granules and enzymatically activated in the rat basophilic/mast cell line RBL
    • Gullberg, U. et al. Carboxyl-terminal prodomain-deleted human leukocyte elastase and cathepsin G are efficiently targeted to granules and enzymatically activated in the rat basophilic/mast cell line RBL. J. Biol. Chem. 270, 12912-12918 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12912-12918
    • Gullberg, U.1
  • 15
    • 0033386292 scopus 로고    scopus 로고
    • Distinct granule populations in human neutrophils and lysosomal organelles identified by immuno-electron microscopy
    • Bainton, D.F. Distinct granule populations in human neutrophils and lysosomal organelles identified by immuno-electron microscopy. J. Immunol. Methods 232, 153-168 (1999).
    • (1999) J. Immunol. Methods , vol.232 , pp. 153-168
    • Bainton, D.F.1
  • 16
    • 0037215566 scopus 로고    scopus 로고
    • Role of neutrophil elastase in bone marrow failure syndromes: Molecular enetic revival of the chalone hypothesis
    • Horwitz, M. et al. Role of neutrophil elastase in bone marrow failure syndromes: molecular genetic revival of the chalone hypothesis. Curr. Opin. Hematol. 10, 49-54 (2003).
    • (2003) Curr. Opin. Hematol. , vol.10 , pp. 49-54
    • Horwitz, M.1
  • 17
    • 0034471359 scopus 로고    scopus 로고
    • Defective organellar membrane protein trafficking in Ap3b1-deficient cells
    • Yang, W., Li, C., Ward, D.M., Kaplan, J. & Mansour, S. L. Defective organellar membrane protein trafficking in Ap3b1-deficient cells. J. Cell Sci. 113, 4077-4086 (2000),
    • (2000) J. Cell Sci. , vol.113 , pp. 4077-4086
    • Yang, W.1    Li, C.2    Ward, D.M.3    Kaplan, J.4    Mansour, S.L.5
  • 18
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Moller, S., Croning, M.D. & Apweiler, R. Evaluation of methods for the prediction of membrane spanning regions. Bioinformatics 17, 646-653 (2001).
    • (2001) Bioinformatics , vol.17 , pp. 646-653
    • Moller, S.1    Croning, M.D.2    Apweiler, R.3
  • 19
    • 0028865394 scopus 로고
    • Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases
    • Owen, C.A., Campbell, M.A., Sanres, P.L., Boukedes, S.S. & Campbell, E.J. Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J. Cell Biol. 131, 775-789 (1995).
    • (1995) J. Cell Biol. , vol.131 , pp. 775-789
    • Owen, C.A.1    Campbell, M.A.2    Sanres, P.L.3    Boukedes, S.S.4    Campbell, E.J.5
  • 20
    • 0020665462 scopus 로고
    • Identification of elastases associated with purified plasma membranes isolated from human monocytes and lymphocytes
    • Fuks, A., Zucker-Franklin, D. & Franklin, E. C. Identification of elastases associated with purified plasma membranes isolated from human monocytes and lymphocytes. Biochim. Biophys. Acta 755, 195-203 (1983).
    • (1983) Biochim. Biophys. Acta , vol.755 , pp. 195-203
    • Fuks, A.1    Zucker-Franklin, D.2    Franklin, E.C.3
  • 21
    • 0028890305 scopus 로고
    • Human coagulation factor V is activated to the functional cofactor by elastase and cathepsin G expressed at the monocyte surface
    • Allen, D.H. & Tracy, P.B. Human coagulation factor V is activated to the functional cofactor by elastase and cathepsin G expressed at the monocyte surface. J. Biol. Chem. 270, 1408-1415 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 1408-1415
    • Allen, D.H.1    Tracy, P.B.2
  • 22
    • 0033961661 scopus 로고    scopus 로고
    • Activation of progelatinase B by membranes of human polymorphonuclear granulocytes
    • Kolkenbrock, H., Zimmermann, J., Burmester, G.R. & Ulbrich, N. Activation of progelatinase B by membranes of human polymorphonuclear granulocytes. Biol. Chem. 381, 49-55 (2000).
    • (2000) Biol. Chem. , vol.381 , pp. 49-55
    • Kolkenbrock, H.1    Zimmermann, J.2    Burmester, G.R.3    Ulbrich, N.4
  • 23
    • 0036337530 scopus 로고    scopus 로고
    • Processing of the human transferrin receptor at distinct positions within the stalk region by neutrophil elastase and cathepsin G
    • Kaup, M. et al. Processing of the human transferrin receptor at distinct positions within the stalk region by neutrophil elastase and cathepsin G. Biol. Chem. 383, 1011-1020 (2002).
    • (2002) Biol. Chem. , vol.383 , pp. 1011-1020
    • Kaup, M.1
  • 24
    • 0018864175 scopus 로고
    • Elastase-like enzymes in human neutrophils localized by ultrastructural cytochemistry
    • Clark, J.M., Vaughan, D.W., Aiken, B.M. & Kagan, H.M. Elastase-like enzymes in human neutrophils localized by ultrastructural cytochemistry. J. Cell Biol. 84, 102-119 (1980).
    • (1980) J. Cell Biol. , vol.84 , pp. 102-119
    • Clark, J.M.1    Vaughan, D.W.2    Aiken, B.M.3    Kagan, H.M.4
  • 25
    • 0037377019 scopus 로고    scopus 로고
    • Selective plasma membrane permeabilization by freeze-thawing and immunofluorescence epitope access to determine the topology of intracellular membrane proteins
    • Mardones, G. & Gonzalez, A. Selective plasma membrane permeabilization by freeze-thawing and immunofluorescence epitope access to determine the topology of intracellular membrane proteins. J. Immunol. Methods 275, 169-177 (2003).
    • (2003) J. Immunol. Methods , vol.275 , pp. 169-177
    • Mardones, G.1    Gonzalez, A.2
  • 26
    • 0030587395 scopus 로고    scopus 로고
    • Subcellular localization of the small GTPase Rab 5a in resting and stimulated human neutrophils
    • Vita, F., Soranzo, M.R., Borelli, V., Bertoncin, P. & Zabucchi, G. Subcellular localization of the small GTPase Rab5a in resting and stimulated human neutrophils. Exp. Cell Res. 227, 367-373 (1996).
    • (1996) Exp. Cell Res. , vol.227 , pp. 367-373
    • Vita, F.1    Soranzo, M.R.2    Borelli, V.3    Bertoncin, P.4    Zabucchi, G.5
  • 27
    • 0027420678 scopus 로고
    • Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: Identification of a distinct gelatinase-containing granule subset by combined immunocytochemistry and subcellular fractionation
    • Kjeldsen, L., Bainton, D.F., Sengelov, H. & Borregaard, N. Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: identification of a distinct gelatinase-containing granule subset by combined immunocytochemistry and subcellular fractionation. Blood 82, 3183-3191 (1993).
    • (1993) Blood , vol.82 , pp. 3183-3191
    • Kjeldsen, L.1    Bainton, D.F.2    Sengelov, H.3    Borregaard, N.4
  • 28
    • 0036890399 scopus 로고    scopus 로고
    • The cytochrome P450 superfamily: Biochemistry, evolution and drug metabolism in humans
    • Danielson, P.B. The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans. Curr. Drug Metab. 3, 561-597 (2002).
    • (2002) Curr. Drug Metab. , vol.3 , pp. 561-597
    • Danielson, P.B.1
  • 29
    • 0024387776 scopus 로고
    • Mammalian β-glucuronidase: Genetics, molecular biology, and cell biology
    • Paigen, K. Mammalian β-glucuronidase: genetics, molecular biology, and cell biology. Prog. Nucleic Acid Res. Mol. Biol. 37, 155-205 (1989).
    • (1989) Prog. Nucleic Acid Res. Mol. Biol. , vol.37 , pp. 155-205
    • Paigen, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.