메뉴 건너뛰기




Volumn 182, Issue 10, 2009, Pages 6533-6539

Targeted disruption of the gene encoding the murine small subunit of carboxypeptidase N (CPN1) causes susceptibility to C5a anaphylatoxin-mediated shock

Author keywords

[No Author keywords available]

Indexed keywords

ANTIHISTAMINIC AGENT; ARGININE CARBOXYPEPTIDASE; COBROTOXIN; COMPLEMENT COMPONENT C3A; COMPLEMENT COMPONENT C5A; COMPLEMENT COMPONENT C5A RECEPTOR; HISTAMINE;

EID: 70349465190     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0804207     Document Type: Article
Times cited : (43)

References (46)
  • 1
    • 0346849668 scopus 로고    scopus 로고
    • Carboxypeptidase N: A pleiotropic regulator of inflammation
    • Matthews, K. W., S. L. Mueller-Ortiz, and R. A. Wetsel. 2004. Carboxypeptidase N: a pleiotropic regulator of inflammation. Mol. Immunol. 40: 785-793.
    • (2004) Mol. Immunol. , vol.40 , pp. 785-793
    • Matthews, K.W.1    Mueller-Ortiz, S.L.2    Wetsel, R.A.3
  • 2
    • 0001995439 scopus 로고    scopus 로고
    • Structure and function of mammalian zinc carboxypeptidase
    • N. M. Hooper, ed. Taylor and Francis, London
    • Skidgel, R. A. 1996. Structure and function of mammalian zinc carboxypeptidase. In Zinc Metalloprotease in Health and Disease. N. M. Hooper, ed. Taylor and Francis, London, pp. 241-283.
    • (1996) Zinc Metalloprotease in Health and Disease , pp. 241-283
    • Skidgel, R.A.1
  • 3
    • 36249014859 scopus 로고    scopus 로고
    • Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator
    • Skidgel, R. A., and E. G. Erdos. 2007. Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator. Int. Immunopharmacol. 7: 1888-1899.
    • (2007) Int. Immunopharmacol. , vol.7 , pp. 1888-1899
    • Skidgel, R.A.1    Erdos, E.G.2
  • 4
    • 0020174237 scopus 로고
    • Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase i)
    • Levin, Y., R. A. Skidgel, and E. G. Erdos. 1982. Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase i). Proc. Natl. Acad. Sci. USA 79: 4618-4622.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4618-4622
    • Levin, Y.1    Skidgel, R.A.2    Erdos, E.G.3
  • 5
    • 0000077897 scopus 로고
    • An enzyme in human blood plasma that inactivates bradykinin and kallidins
    • Erdos, E. G., and E. M. Sloane. 1962. An enzyme in human blood plasma that inactivates bradykinin and kallidins. Biochem. Pharmacol. 11: 585-592.
    • (1962) Biochem. Pharmacol. , vol.11 , pp. 585-592
    • Erdos, E.G.1    Sloane, E.M.2
  • 6
    • 0014900566 scopus 로고
    • Anaphylatoxin inactivator of human plasma: Its isolation and characterization as a carboxypeptidase
    • Bokisch, V. A., and H. J. Muller-Eberhard. 1970. Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase. J. Clin. Invest. 49: 2427-2436.
    • (1970) J. Clin. Invest. , vol.49 , pp. 2427-2436
    • Bokisch, V.A.1    Muller-Eberhard, H.J.2
  • 7
    • 0001136044 scopus 로고    scopus 로고
    • Complement anaphylatoxins (C3a, C4a, C5a) and their receptors (C3aR, C5aR/CD88) as therapeutic targets in inflammation
    • J. D. Lambris and V. M. Holers, eds. Humana, Totowa, NJ
    • Wetsel, R. A., J. Kildsgaard, and D. L. Haviland. 2000. Complement anaphylatoxins (C3a, C4a, C5a) and their receptors (C3aR, C5aR/CD88) as therapeutic targets in inflammation. In Contemporary Immunology: Therapeutic Interventions in the Complement System. J. D. Lambris and V. M. Holers, eds. Humana, Totowa, NJ, pp. 113-154.
    • (2000) Contemporary Immunology: Therapeutic Interventions in the Complement System , pp. 113-154
    • Wetsel, R.A.1    Kildsgaard, J.2    Haviland, D.L.3
  • 8
    • 20444383082 scopus 로고    scopus 로고
    • Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1α in the circulation
    • Davis, D. A., K. E. Singer, M. De La Luz Sierra, M. Narazaki, F. Yang, H. M. Fales, R. Yarchoan, and G. Tosato. 2005. Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1α in the circulation. Blood 105: 4561-4568.
    • (2005) Blood , vol.105 , pp. 4561-4568
    • Davis, D.A.1    Singer, K.E.2    De La Luz Sierra, M.3    Narazaki, M.4    Yang, F.5    Fales, H.M.6    Yarchoan, R.7    Tosato, G.8
  • 9
    • 1642366238 scopus 로고    scopus 로고
    • Differential processing of stromal-derived factor-1α and stromal-derived factor-1β explains functional diversity
    • DOI 10.1182/blood-2003-08-2857
    • De La Luz Sierra, M., F. Yang, M. Narazaki, O. Salvucci, D. Davis, R. Yarchoan, H. H. Zhang, H. Fales, and G. Tosato. 2004. Differential processing of stromalderived factor-1α and stromal-derived factor-1β explains functional diversity. Blood 103: 2452-2459. (Pubitemid 38392993)
    • (2004) Blood , vol.103 , Issue.7 , pp. 2452-2459
    • De La Luz Sierra, M.1    Yang, F.2    Narazaki, M.3    Salvucci, O.4    Davis, D.5    Yarchoan, R.6    Zhang, H.H.7    Fales, H.8    Tosato, G.9
  • 11
    • 0022653736 scopus 로고
    • Decreased synthesis of serum carboxypeptidase N (SCPN) in familial SCPN deficiency
    • Mathews, K. P., J. G. Curd, and T. E. Hugli. 1986. Decreased synthesis of serum carboxypeptidase N (SCPN) in familial SCPN deficiency. J. Clin. Immunol. 6: 87-91.
    • (1986) J. Clin. Immunol. , vol.6 , pp. 87-91
    • Mathews, K.P.1    Curd, J.G.2    Hugli, T.E.3
  • 12
    • 0037275693 scopus 로고    scopus 로고
    • DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency
    • DOI 10.1007/s100380300003
    • Cao, H., and R. A. Hegele. 2003. DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency. J. Hum. Genet. 48: 20-22. (Pubitemid 36205642)
    • (2003) Journal of Human Genetics , vol.48 , Issue.1 , pp. 20-22
    • Cao, H.1    Hegele, R.A.2
  • 14
    • 1142285360 scopus 로고    scopus 로고
    • Expression of the third complement component (C3) and carboxypeptidase N small subunit (CPN1) during mouse embryonic development
    • Matthews, K. W., S. M. Drouin, C. Liu, J. F. Martin, R. A. Skidgel, and R. A. Wetsel. 2004. Expression of the third complement component (C3) and carboxypeptidase N small subunit (CPN1) during mouse embryonic development. Dev. Comp. Immunol. 28: 647-655.
    • (2004) Dev. Comp. Immunol. , vol.28 , pp. 647-655
    • Matthews, K.W.1    Drouin, S.M.2    Liu, C.3    Martin, J.F.4    Skidgel, R.A.5    Wetsel, R.A.6
  • 15
    • 0035873437 scopus 로고    scopus 로고
    • Characterization of mouse carboxypeptidase N small active subunit gene structure
    • Matthews, K. W., and R. A. Wetsel. 2001. Characterization of mouse carboxypeptidase N small active subunit gene structure. J. Immunol. 166: 6196-6202. (Pubitemid 32440750)
    • (2001) Journal of Immunology , vol.166 , Issue.10 , pp. 6196-6202
    • Matthews, K.W.1    Wetsel, R.A.2
  • 16
    • 0036191244 scopus 로고    scopus 로고
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
    • Campbell, W. D., E. Lazoura, N. Okada, and H. Okada. 2002. Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. Microbiol. Immunol. 46: 131-134.
    • (2002) Microbiol. Immunol. , vol.46 , pp. 131-134
    • Campbell, W.D.1    Lazoura, E.2    Okada, N.3    Okada, H.4
  • 17
    • 0029060126 scopus 로고
    • Human carboxypeptidase N: Lysine carboxypeptidase
    • Skidgel, R. A. 1995. Human carboxypeptidase N: lysine carboxypeptidase. Methods Enzymol. 248: 653-663.
    • (1995) Methods Enzymol. , vol.248 , pp. 653-663
    • Skidgel, R.A.1
  • 18
    • 0034670027 scopus 로고    scopus 로고
    • Cutting edge: Targeted disruption of the C3a receptor gene demonstrates a novel protective anti-inflammatory role for C3a in endotoxinshock
    • Kildsgaard, J., T. J. Hollmann, K. W. Matthews, K. Bian, F. Murad, and R. A. Wetsel. 2000. Cutting edge: targeted disruption of the C3a receptor gene demonstrates a novel protective anti-inflammatory role for C3a in endotoxinshock. J. Immunol. 165: 5406-5409.
    • (2000) J. Immunol. , vol.165 , pp. 5406-5409
    • Kildsgaard, J.1    Hollmann, T.J.2    Matthews, K.W.3    Bian, K.4    Murad, F.5    Wetsel, R.A.6
  • 19
    • 39149091052 scopus 로고    scopus 로고
    • Disruption of the C5a receptor gene increases resistance to acute Gram-negative bacteremia and endotoxic shock: Opposing roles of C3a and C5a
    • Hollmann, T. J., S. L. Mueller-Ortiz, M. C. Braun, and R. A. Wetsel. 2008. Disruption of the C5a receptor gene increases resistance to acute Gram-negative bacteremia and endotoxic shock: opposing roles of C3a and C5a. Mol. Immunol. 45: 1907-1915.
    • (2008) Mol. Immunol. , vol.45 , pp. 1907-1915
    • Hollmann, T.J.1    Mueller-Ortiz, S.L.2    Braun, M.C.3    Wetsel, R.A.4
  • 20
    • 34250179805 scopus 로고    scopus 로고
    • Complement C3a regulates Muc5ac expression by airway clara cells independently of Th2 responses
    • DOI 10.1164/rccm.200701-049OC
    • Dillard, P., R. A. Wetsel, and S. M. Drouin. 2007. Complement C3a regulates Muc5ac expression by airway Clara cells independently of Th2 responses. Am. J. Respir. Crit. Care Med. 175: 1250-1258. (Pubitemid 46905750)
    • (2007) American Journal of Respiratory and Critical Care Medicine , vol.175 , Issue.12 , pp. 1250-1258
    • Dillard, P.1    Wetsel, R.A.2    Drouin, S.M.3
  • 21
    • 0019159842 scopus 로고
    • An improved spectrophotometric assay for human plasma carboxypeptidase N
    • DOI 10.1016/0003-2697(80)90598-9
    • Plummer, T. H., Jr., and M. T. Kimmel. 1980. An improved spectrophotometric assay for human plasma carboxypeptidase N1. Anal. Biochem. 108: 348-353. (Pubitemid 11182101)
    • (1980) Analytical Biochemistry , vol.108 , Issue.2 , pp. 348-353
    • Plummer Jr., T.H.1    Kimmel, M.T.2
  • 22
    • 0016719394 scopus 로고
    • Plasma carboxypeptidase N, subunits and characteristics
    • Oshima, G., J. Kato, and E. G. Erdos. 1975. Plasma carboxypeptidase N, subunits and characteristics. Arch. Biochem. Biophys. 170: 132-138.
    • (1975) Arch. Biochem. Biophys. , vol.170 , pp. 132-138
    • Oshima, G.1    Kato, J.2    Erdos, E.G.3
  • 25
    • 33750014305 scopus 로고    scopus 로고
    • Which complement assays and typings are necessary for the diagnosis of complement deficiency in patients with lupus erythematosus? a study of 25 patients
    • DOI 10.1016/j.clim.2006.08.007, PII S1521661606008400
    • Boeckler, P., A. Meyer, B. Uring-Lambert, J. Goetz, B. Cribier, G. Hauptmann, and D. Lipsker. 2006. Which complement assays and typings are necessary for the diagnosis of complement deficiency in patients with lupus erythematosus?: a study of 25 patients. Clin. Immunol. 121: 198-202. (Pubitemid 44572978)
    • (2006) Clinical Immunology , vol.121 , Issue.2 , pp. 198-202
    • Boeckler, P.1    Meyer, A.2    Uring-Lambert, B.3    Goetz, J.4    Cribier, B.5    Hauptmann, G.6    Lipsker, D.7
  • 29
    • 34250737938 scopus 로고    scopus 로고
    • Gc-globulin concentrations and C5 haplotype-tagging polymorphisms contribute to variations in serum activity of complement factor C5
    • DOI 10.1016/j.clinbiochem.2007.02.001, PII S0009912007000963
    • Gressner, O., U. Meier, S. Hillebrandt, H. E. Wasmuth, J. Kohl, T. Sauerbruch, and F. Lammert. 2007. Gc-globulin concentrations and C5 haplotype-tagging polymorphisms contribute to variations in serum activity of complement factor C5. Clin. Biochem. 40: 771-775. (Pubitemid 46961957)
    • (2007) Clinical Biochemistry , vol.40 , Issue.11 , pp. 771-775
    • Gressner, O.1    Meier, U.2    Hillebrandt, S.3    E Wasmuth, H.4    Kohl, J.5    Sauerbruch, T.6    Lammert, F.7
  • 31
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • DOI 10.1074/jbc.271.28.16603
    • Bajzar, L., J. Morser, and M. Nesheim. 1996. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J. Biol. Chem. 271: 16603-16608. (Pubitemid 26239017)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.28 , pp. 16603-16608
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 32
    • 0025748556 scopus 로고
    • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
    • Eaton, D. L., B. E. Malloy, S. P. Tsai, W. Henzel, and D. Drayna. 1991. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J. Biol. Chem. 266: 21833-21838.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21833-21838
    • Eaton, D.L.1    Malloy, B.E.2    Tsai, S.P.3    Henzel, W.4    Drayna, D.5
  • 33
    • 0029023651 scopus 로고
    • Activation and characterization of procarboxypeptidase B from human plasma
    • Tan, A. K., and D. L. Eaton. 1995. Activation and characterization of procarboxypeptidase B from human plasma. Biochemistry 34: 5811-5816.
    • (1995) Biochemistry , vol.34 , pp. 5811-5816
    • Tan, A.K.1    Eaton, D.L.2
  • 34
    • 0036221061 scopus 로고    scopus 로고
    • Elastase from activated human neutrophils activates procarboxypeptidase R
    • Kawamura, T., N. Okada, and H. Okada. 2002. Elastase from activated human neutrophils activates procarboxypeptidase R. Microbiol. Immunol. 46: 225-230. (Pubitemid 34289020)
    • (2002) Microbiology and Immunology , vol.46 , Issue.3 , pp. 225-230
    • Kawamura, T.1    Okada, N.2    Okada, H.3
  • 35
    • 4644336103 scopus 로고    scopus 로고
    • Absence of procarboxypeptidase R induces complement-mediated lethal inflammation in lipopolysaccharide-primed mice
    • Asai, S., T. Sato, T. Tada, T. Miyamoto, N. Kimbara, N. Motoyama, H. Okada, and N. Okada. 2004. Absence of procarboxypeptidase R induces complement-mediated lethal inflammation in lipopolysaccharide-primed mice. J. Immunol. 173: 4669-4674. (Pubitemid 39280701)
    • (2004) Journal of Immunology , vol.173 , Issue.7 , pp. 4669-4674
    • Asai, S.1    Sato, T.2    Tada, T.3    Miyamoto, T.4    Kimbara, N.5    Motoyama, N.6    Okada, H.7    Okada, N.8
  • 37
    • 0036843274 scopus 로고    scopus 로고
    • In vivo regulation of plasminogen function by plasma carboxypeptidase B
    • Swaisgood, C. M., D. Schmitt, D. Eaton, and E. F. Plow. 2002. In vivo regulation of plasminogen function by plasma carboxypeptidase B. J. Clin. Invest. 110: 1275-1282.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1275-1282
    • Swaisgood, C.M.1    Schmitt, D.2    Eaton, D.3    Plow, E.F.4
  • 39
    • 0020595387 scopus 로고
    • Potentiation of the anaphylatoxins in vivo using an inhibitor of serum carboxypeptidase N (SCPN). I. Lethality and pathologic effects on pulmonary tissue
    • Huey, R., C. M. Bloor, M. S. Kawahara, and T. E. Hugli. 1983. Potentiation of the anaphylatoxins in vivo using an inhibitor of serum carboxypeptidase N (SCPN), I: Lethality and pathologic effects on pulmonary tissue. Am. J. Pathol. 112: 48-60. (Pubitemid 13069240)
    • (1983) American Journal of Pathology , vol.112 , Issue.1 , pp. 48-60
    • Huey, R.1    Bloor, C.M.2    Kawahara, M.S.3    Hugli, T.E.4
  • 40
    • 0021997799 scopus 로고
    • Mediators of lung injury in mice following systemic activation of complement
    • Tvedten, H. W., G. O. Till, and P. A. Ward. 1985. Mediators of lung injury in mice following systemic activation of complement. Am. J. Pathol. 119: 92-100. (Pubitemid 15088728)
    • (1985) American Journal of Pathology , vol.119 , Issue.1 , pp. 92-100
    • Tvedten, H.W.1    Till, G.O.2    Ward, P.A.3
  • 43
    • 3242776043 scopus 로고    scopus 로고
    • Comparative anti-inflammatory activities of antagonists to C3a and C5a receptors in a rat model of intestinal ischaemia/reperfusion injury
    • Proctor, L. M., T. V. Arumugam, I. Shiels, R. C. Reid, D. P. Fairlie, and S. M. Taylor. 2004. Comparative anti-inflammatory activities of antagonists to C3a and C5a receptors in a rat model of intestinal ischaemia/reperfusion injury. Br. J. Pharmacol. 142: 756-764.
    • (2004) Br. J. Pharmacol. , vol.142 , pp. 756-764
    • Proctor, L.M.1    Arumugam, T.V.2    Shiels, I.3    Reid, R.C.4    Fairlie, D.P.5    Taylor, S.M.6
  • 45
    • 0015101581 scopus 로고
    • Effects of some drugs on capillary permeability in the anaphylaxis of the mouse
    • Takagi, K., and T. Fukao. 1971. Effects of some drugs on capillary permeability in the anaphylaxis of the mouse. Jpn. J. Pharmacol. 21: 455-465.
    • (1971) Jpn. J. Pharmacol. , vol.21 , pp. 455-465
    • Takagi, K.1    Fukao, T.2
  • 46
    • 0014738265 scopus 로고
    • Turnover of pulmonary alveolar wall cells in guinea-pig and mouse after anaphylactic shock
    • Henderson, J. D., and H. Smith. 1970. Turnover of pulmonary alveolar wall cells in guinea-pig and mouse after anaphylactic shock. Br. J. Pharmacol. 38: 442P-443P.
    • (1970) Br. J. Pharmacol. , vol.38
    • Henderson, J.D.1    Smith, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.