메뉴 건너뛰기




Volumn 105, Issue 1, 1996, Pages 191-197

The catabolism of intact, reactive centre-cleaved and proteinase- complexed C1 inhibitor in the guinea pig

Author keywords

complement; protein catabolism; serpins

Indexed keywords

BLOOD CLOTTING FACTOR 12; KALLIKREIN;

EID: 0030057113     PISSN: 00099104     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2249.1996.d01-714.x     Document Type: Article
Times cited : (12)

References (34)
  • 1
    • 0024146204 scopus 로고
    • C1 inhibitor and hereditary angioneurotic edema
    • Davis AE III. C1 inhibitor and hereditary angioneurotic edema. Ann Rev Immunol 1988; 6:595-628.
    • (1988) Ann Rev Immunol , vol.6 , pp. 595-628
    • Davis III, A.E.1
  • 2
    • 0017077229 scopus 로고
    • Hereditary angioedema: The clinical syndrome and its management
    • Frank MM, Gelfand JA, Atkinson JP. Hereditary angioedema: the clinical syndrome and its management. Ann Int Med 1976; 84:580-93.
    • (1976) Ann Int Med , vol.84 , pp. 580-593
    • Frank, M.M.1    Gelfand, J.A.2    Atkinson, J.P.3
  • 3
    • 0024423930 scopus 로고
    • 1-antitrypsin for structure and function of serpins
    • 1-antitrypsin for structure and function of serpins. Biochemistry 1989; 28:8951-66.
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 4
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M Jr, Kato I. Protein inhibitors of proteinases. Ann Rev Biochem 1980; 49:593-626.
    • (1980) Ann Rev Biochem , vol.49 , pp. 593-626
    • Laskowski Jr., M.1    Kato, I.2
  • 5
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis J, Salvesen GS. Human plasma proteinase inhibitors. Ann Rev Biochem 1983; 52:655-709.
    • (1983) Ann Rev Biochem , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 6
    • 0020067533 scopus 로고
    • The in vivo metabolism of antithrombin III and antithrombin III complexes
    • Shifman MA, Pizzo SV. The in vivo metabolism of antithrombin III and antithrombin III complexes. J Biol Chem 1982; 257:3243-8.
    • (1982) J Biol Chem , vol.257 , pp. 3243-3248
    • Shifman, M.A.1    Pizzo, S.V.2
  • 7
    • 0025191834 scopus 로고
    • Turnover of *I-Protein C inhibitor and *I-αi-antitrypsin and their complexes with activated protein C
    • Laurell M, Stenflo J, Carlson TH. Turnover of *I-Protein C inhibitor and *I-αi-antitrypsin and their complexes with activated protein C. Blood 1990; 76:2290-5.
    • (1990) Blood , vol.76 , pp. 2290-2295
    • Laurell, M.1    Stenflo, J.2    Carlson, T.H.3
  • 10
    • 0023950380 scopus 로고
    • In vivo catabolism of heparin cofactor II and its complex with thrombin: Evidence for a common receptor-mediated clearance pathway for three serine proteinase inhibitors
    • Pratt CW, Church FC, Pizzo SV. In vivo catabolism of heparin cofactor II and its complex with thrombin: evidence for a common receptor-mediated clearance pathway for three serine proteinase inhibitors. Arch Biochem Biophys 1988; 262:111-7.
    • (1988) Arch Biochem Biophys , vol.262 , pp. 111-117
    • Pratt, C.W.1    Church, F.C.2    Pizzo, S.V.3
  • 11
    • 0025873532 scopus 로고
    • Evidence for a tetrahedral intermediate complex during serpin-proteinase interactions
    • Matheson NR, van Halbeek H, Travis J. Evidence for a tetrahedral intermediate complex during serpin-proteinase interactions. J Biol Chem 1991; 266:13489-91.
    • (1991) J Biol Chem , vol.266 , pp. 13489-13491
    • Matheson, N.R.1    Van Halbeek, H.2    Travis, J.3
  • 13
    • 0024453908 scopus 로고
    • Serpin receptor 1: A hepatic receptor that mediates the clearance of antithrombin III-proteinase complexes
    • Pizzo SV. Serpin receptor 1: a hepatic receptor that mediates the clearance of antithrombin III-proteinase complexes. Am J Med 1989; 87 (Suppl. 3B):10s-14s.
    • (1989) Am J Med , vol.87 , Issue.SUPPL. 3B
    • Pizzo, S.V.1
  • 16
    • 0027470437 scopus 로고
    • Clearance of human native proteinase-complexed, and proteolytically inactivated Cl-inhibitor in rats
    • de Smet BJGL, de Boer JP, Agterberg J, Rigter G, Bleeker WK, Hack CE. Clearance of human native proteinase-complexed, and proteolytically inactivated Cl-inhibitor in rats. Blood 1993; 81:56-61.
    • (1993) Blood , vol.81 , pp. 56-61
    • De Smet, B.J.G.L.1    De Boer, J.P.2    Agterberg, J.3    Rigter, G.4    Bleeker, W.K.5    Hack, C.E.6
  • 18
    • 0024412729 scopus 로고
    • A new simplified procedure for Cl inhibitor purification. A novel use for jacalinagarose
    • Pilatte Y, Hammer CH, Frank MM, Fries LF. A new simplified procedure for Cl inhibitor purification. A novel use for jacalinagarose. J Immunol Methods 1989; 120:37-43.
    • (1989) J Immunol Methods , vol.120 , pp. 37-43
    • Pilatte, Y.1    Hammer, C.H.2    Frank, M.M.3    Fries, L.F.4
  • 19
    • 0021928848 scopus 로고
    • Primary structure of the reactive site of human Cl inhibitor
    • Salvesen GS, Catanese JJ, Kress LF, Travis J. Primary structure of the reactive site of human Cl inhibitor. J Biol Chem 1985; 260:2432-6.
    • (1985) J Biol Chem , vol.260 , pp. 2432-2436
    • Salvesen, G.S.1    Catanese, J.J.2    Kress, L.F.3    Travis, J.4
  • 20
    • 0020380627 scopus 로고
    • A new solid-state reagent to iodinate proteins. I. Conditions for the efficient labeling of antiserum
    • Markwell MAK. A new solid-state reagent to iodinate proteins. I. Conditions for the efficient labeling of antiserum. Analyt Biochem 1982; 125:427-31.
    • (1982) Analyt Biochem , vol.125 , pp. 427-431
    • Markwell, M.A.K.1
  • 21
    • 36149059384 scopus 로고
    • 131I labeled plasma proteins
    • 131I labeled plasma proteins. Phys Med Biol 1957; 2:36-53.
    • (1957) Phys Med Biol , vol.2 , pp. 36-53
    • Matthews, C.M.E.1
  • 22
    • 0020682111 scopus 로고
    • Behavior in vivo of normal and dysfunctional Cl inhibitor in normal subjects and patients with hereditary angioneurotic edema
    • Quastel M, Harrison R, Cicardi M, Alper CA, Rosen FS. Behavior in vivo of normal and dysfunctional Cl inhibitor in normal subjects and patients with hereditary angioneurotic edema. J Clin Invest 1983; 71:1041-6.
    • (1983) J Clin Invest , vol.71 , pp. 1041-1046
    • Quastel, M.1    Harrison, R.2    Cicardi, M.3    Alper, C.A.4    Rosen, F.S.5
  • 23
    • 46149128444 scopus 로고
    • Prolonged vascular retention of a hemoglobin solution modified by cross-linking with 2-nor-2 formylpyridoxal 5́-phosphate
    • Bleeker WK, van der Plas J, Agterberg J, Rigter G, Bakker JC. Prolonged vascular retention of a hemoglobin solution modified by cross-linking with 2-nor-2 formylpyridoxal 5́-phosphate. J Lab Clin Med 1986; 108:448-54.
    • (1986) J Lab Clin Med , vol.108 , pp. 448-454
    • Bleeker, W.K.1    Van Der Plas, J.2    Agterberg, J.3    Rigter, G.4    Bakker, J.C.5
  • 24
    • 0025871316 scopus 로고
    • Pharmacokinetics of activated protein C in guinea pigs
    • Berger Jr H, Kirstein CG, Orthner CL. Pharmacokinetics of activated protein C in guinea pigs. Blood 1991; 77:2174-84.
    • (1991) Blood , vol.77 , pp. 2174-2184
    • Berger Jr., H.1    Kirstein, C.G.2    Orthner, C.L.3
  • 25
    • 0347922052 scopus 로고
    • Life-span of plasma coagulation factors
    • Williams WJ, Beutler E, Erslav AJ, Lichtman MA, eds. New York: McGraw-Hill
    • Comp PC. Life-span of plasma coagulation factors. In: Williams WJ, Beutler E, Erslav AJ, Lichtman MA, eds. Hematology. New York: McGraw-Hill, 1990:1290-4.
    • (1990) Hematology , pp. 1290-1294
    • Comp, P.C.1
  • 26
    • 0020672314 scopus 로고
    • Ligand binding, conformational change and plasma elimination of human, mouse and rat alpha-macroglobulin proteinase inhibitors
    • Gonias SL, Balber AE, Hubbard WJ, Pizzo SV. Ligand binding, conformational change and plasma elimination of human, mouse and rat alpha-macroglobulin proteinase inhibitors. Biochem J 1983; 209:99-105.
    • (1983) Biochem J , vol.209 , pp. 99-105
    • Gonias, S.L.1    Balber, A.E.2    Hubbard, W.J.3    Pizzo, S.V.4
  • 30
    • 0026546881 scopus 로고
    • Structural basis of latency in plasminogen activator inhibitor-1
    • Mottonen J, Strand A, Symersky J et al. Structural basis of latency in plasminogen activator inhibitor-1. Nature 1992; 355:270-3.
    • (1992) Nature , vol.355 , pp. 270-273
    • Mottonen, J.1    Strand, A.2    Symersky, J.3
  • 32
    • 0028407364 scopus 로고
    • Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
    • Wei A, Rubin H, Cooperman BS, Christianson DW. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Struct Biol 1994; 1:251-8.
    • (1994) Struct Biol , vol.1 , pp. 251-258
    • Wei, A.1    Rubin, H.2    Cooperman, B.S.3    Christianson, D.W.4
  • 33
    • 0027491244 scopus 로고
    • Cl inhibitorserine proteinase complexes and the biosynthesis of Cl-inhibitor by HepG2 and U937 cells
    • Patston PA, Medcalf RL, Kourteva Y, Schapira M. Cl inhibitorserine proteinase complexes and the biosynthesis of Cl-inhibitor by HepG2 and U937 cells. Blood 1993; 82:3371-9.
    • (1993) Blood , vol.82 , pp. 3371-3379
    • Patston, P.A.1    Medcalf, R.L.2    Kourteva, Y.3    Schapira, M.4
  • 34
    • 0025143104 scopus 로고
    • Identification of determinants involved in binding of tissue-type plasminogen activator-plasminogen activator inhibitor type 1 complexes to HepG2 cells
    • Morton PA, Owensby DA, Wun TC, Billadello JJ, Schwartz AL. Identification of determinants involved in binding of tissue-type plasminogen activator-plasminogen activator inhibitor type 1 complexes to HepG2 cells. J Biol Chem 1990; 265:14093-9.
    • (1990) J Biol Chem , vol.265 , pp. 14093-14099
    • Morton, P.A.1    Owensby, D.A.2    Wun, T.C.3    Billadello, J.J.4    Schwartz, A.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.