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PROC  -  protein C (inactivator of coagulation...

Sus scrofa

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Disease relevance of PROC

  • This protein is involved in activated protein C resistance, the most common inherited thrombotic disorder known [1].
  • Nearly occlusive platelet thrombosis, which occurs within 30 min of crushing 1 cm segments of carotid arteries with a standard hemostat, is blocked by endogenous protein C activation initiated 2 min before the crush injury [2].
  • We have completed production in rabbits of potent antisera to the 90 classified rhinovirus serotypes by using methods previously described (M. K. Cooney and G. E. Kenny, Proc. Soc. Exp. Biol. Med. 133:645-650, 1970) [3].
  • To express the pig citrate synthase cDNA in Escherichia coli, we employed the inducible T7 RNA polymerase/promoter double plasmid expression vectors pGP1-2 and pT7-7 [Tabor, S., & Richardson, C. C. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 1074-1078] [4].
  • The deviation of OMSVP3 from OMTKY3 complexed with the Streptomyces griseus protease B is very small [Fujinaga, M., Read, R. J., Sielecki, A., Ardelt, W., Laskowski, M., Jr and James, M. N. G. (1982) Proc. Natl Acad. Sci. USA, 79, 4868-4872] [5].

High impact information on PROC

  • The open reading frame of 1011 bases corresponds to 337 amino acids, two more than have been previously reported [Marcus, F., Edelstein, I., Reardon, I. & Heinrikson, R. L. (1982) Proc. Natl. Acad. Sci. USA 79, 7161-7165] [6].
  • Protein C activation following coronary artery occlusion in the in situ porcine heart [7].
  • Mutations in the AMP binding site of porcine fructose-1,6-bisphosphatase were carried out by site-specific mutagenesis based on the crystal structure of the enzyme (Ke, H., Zhang, Y., and Lipscomb, W.L. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 5243-5247) [8].
  • Activation of platelets by thrombin results in a dramatic increase in tyrosine phosphorylation on multiple cellular proteins (Ferrell, J. E., and Martin, G. S. (1988) Mol. Cell. Biol. 8, 3603-3610; Golden, A., and Brugge, J. S. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 901-905; Nakamura, S., and Yamamura, H. (1989) J. Biol. Chem. 264, 7089-7091) [9].
  • Lanthanides compete with Rb+ and Na+ in membranes digested with trypsin so as to produce 19-kDa and smaller fragments of the alpha-chain (Karlish, S.J.D., Goldshleger, R., and Stein, W. D. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 4566-4570), also suggestive of a direct interaction of lanthanides with Na+ and K+ sites [10].

Chemical compound and disease context of PROC


Biological context of PROC

  • Actin-activated ATP hydrolysis by phosphorylated arterial myosin is Ca2+-dependent at Mg2+ concentrations which allow myosin to bind 2 mol of Ca2+ per mol (S. Chacko and A. Rosenfeld (1982) Proc. Natl. Acad. Sci. U. S. A. 79, 292-296) [12].
  • The recovery of PEC after transfection of RNA transcripts was dependent on the presence of bile acids, consistent with our recent identification of a bile acid-mediated signaling pathway required for PEC replication (Chang et al., Proc. Natl. Acad. Sci. USA 101:8733-8788, 2004) [13].
  • Compared with the control group, platelets were lower in the MAFI group (p<.005), PTT was prolonged in both the MAFI and AFI groups (p<.005), fibrinogen was lower in both the MAFI and AFI groups (p<.05), prothrombin index was lower (i.e., prothrombin time was prolonged) in the MAFI group (p<.05), and protein C was lower in the MAFI group (p<.005) [14].
  • The following parameters were measured: Platelets, partial thromboplastin time, prothrombin time, fibrinogen, factors V, VII, VIII, antithrombin III, and protein C. The values relative to baseline in the MAFI and AFI groups were compared with control by rank order test [14].
  • The recent X-ray crystallographic resolution of pig kidney FBPase (H. Ke, C. M. Thorpe, B. A. Seaton, F. Marcus, and W. N. Lipscomb, 1989, Proc. Natl. Acad. Sci. USA 86, 1475-1479) has allowed the discussion of the amino acid sequence of spinach chloroplast FBPase in structural terms [15].

Anatomical context of PROC

  • Endogenously activated protein C is evaluated for antithrombotic activity in porcine carotid arteries subjected to mechanical trauma [2].
  • The ubiquitin-proteasome pathway has been implicated in the penetration of ascidian vitelline envelope by the fertilizing spermatozoon (Sawada et al., Proc Natl Acad Sci U S A 2002; 99:1223-1228) [16].
  • This carboxyl-terminal domain constitutes an essential site for MAPs interaction and plays a role in modulating the interactions responsible for tubulin self-assembly into microtubules [Serrano et al. (1984) Proc. Natl Acad. Sci. USA 81, 5989; and Biochemistry 23, 4675] [17].
  • LLC-PK1/PKE20 cells (a continuous epithelial cell line) has two different Na/H exchange activities: Na/H-1 located in the basolateral membrane and Na/H-2 located in the apical membrane [Casavola et al. (1989) Biochem Biophys Res Commun 165:833-837; Haggerty et al. (1988) Proc Natl Acad Sci USA 86:6797-6801] [18].
  • (Proc. Natl. Acad. Sci. USA. 81:4833-4837, 1984) to isolate a mutant of LLC-PK1 cells that is deficient in Na-H antiporter activity [19].

Associations of PROC with chemical compounds

  • The results are therefore in agreement with a [3Fe-4S] cluster having 2.7-A Fe-Fe distances (Beinert, H., Emptage, M. H., Dreyer, J.-L., Scott, R. A., Hahn, J. E., Hodgson, K. O., and Thomson, A. J. (1983) Proc. Natl. Acad. Sci. U. S. A. 80, 393-396) [20].
  • The thermosensitive enzyme differs from the wild type protein in that a serine is substituted for a proline residue at position 87 (Gilles, A.-M., Saint Girons, I., Monnot, M., Fermandjian, S., Michelson, S., and Bârzu, O. (1986) Proc. Natl. Acad. Sci. U. S. A., 83, 5798-5802) [21].
  • A scheme utilizing repeated cycles of assembly and disassembly was used to prepare tubulin and microtubule-associated proteins (MAPs) (Shelanski, M. L., Gaskin, F., and Cantor, C. R. (1973) Proc. Natl. Acad. Sci. U. S. A. 70, 765-768) [22].
  • At concentrations of D-alpha-aminobutyrate below 0.5 mM, the rapid reaction and steady state results are consistent with the mechanism previously proposed for D-alanine (Massey, V., and Gibson, Q. H. (1964) Fed. Proc. 23, 18-29; Porter, D. J. T., Voet, J. G., and Bright, H. J. (1977) J. Biol. Chem. 252, 4464-4473) [23].
  • An acidic lipid fraction isolated from pig liver (Forsee, W. T. & Elbein, A.D. (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 2574-2578) stimulated the incorporation of mannose from GDP-[14C]mannose into lipid-linked oligosaccharides using a particulate enzyme fraction from maturing cotton bolls [24].

Other interactions of PROC

  • Multilayer structures in lipid monolayer films containing surfactant protein C: effects of cholesterol and POPE [25].
  • Platelet plasminogen activator inhibitor: purification and characterization of interaction with plasminogen activators and activated protein C [26].
  • The increase in Protein C, total Protein S, and 6-keto-PGF1a (favoring antithrombosis), and decrease in endothelin-1 and TxB2 levels (favoring vasodilatation), following NPC 15669 may explain the reduction in infarct size previously reported with this agent [27].
  • Mg given at reperfusion onset was associated with a diminished ET-1 (32.9%), decreased fibronectin level (21.7-25.2%), and increased protein C concentrations (31.9-52.3%) when compared with both the control and late Mg group [28].

Analytical, diagnostic and therapeutic context of PROC

  • Three of these four cysteines (peptides 3 and 7) correlated with those proposed to be cluster ligands recently determined by x-ray crystallography (Robbins, A. H. and Stout, C. D. (1989) Proteins, in press; Robbins, A. H., and Stout, C. D.,, (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 3639-3643) for pig heart aconitase [29].
  • Reverse-phase HPLC of the hydrophobic pulmonary surfactant proteins: detection of a surfactant protein C isoform containing Nepsilon-palmitoyl-lysine [30].
  • Mac-1 inhibition was associated with the elevated protein C during late reperfusion [31].


  1. Porcine factor V: cDNA cloning, gene mapping, three-dimensional protein modeling of membrane binding sites and comparative anatomy of domains. Grimm, D.R., Colter, M.B., Braunschweig, M., Alexander, L.J., Neame, P.J., Kim, H.K. Cell. Mol. Life Sci. (2001) [Pubmed]
  2. Antithrombotic action of endogenous porcine protein C activated with a latent porcine thrombin preparation. McBane, R.D., Wysokinski, W.E., Chesebro, J.H., Owen, W.G. Thromb. Haemost. (1995) [Pubmed]
  3. Antigenic groupings of 90 rhinovirus serotypes. Cooney, M.K., Fox, J.P., Kenny, G.E. Infect. Immun. (1982) [Pubmed]
  4. Isolation, nucleotide sequence, and expression of a cDNA encoding pig citrate synthase. Evans, C.T., Owens, D.D., Sumegi, B., Kispal, G., Srere, P.A. Biochemistry (1988) [Pubmed]
  5. The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3). Bode, W., Epp, O., Huber, R., Laskowski, M., Ardelt, W. Eur. J. Biochem. (1985) [Pubmed]
  6. Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase. Williams, M.K., Kantrowitz, E.R. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  7. Protein C activation following coronary artery occlusion in the in situ porcine heart. Snow, T.R., Deal, M.T., Dickey, D.T., Esmon, C.T. Circulation (1991) [Pubmed]
  8. Replacement of glutamic acid 29 with glutamine leads to a loss of cooperativity for AMP with porcine fructose-1,6-bisphosphatase. Chen, M., Chen, L., Fromm, H.J. J. Biol. Chem. (1994) [Pubmed]
  9. Protein-tyrosine kinase p72syk is activated by thrombin and is negatively regulated through Ca2+ mobilization in platelets. Taniguchi, T., Kitagawa, H., Yasue, S., Yanagi, S., Sakai, K., Asahi, M., Ohta, S., Takeuchi, F., Nakamura, S., Yamamura, H. J. Biol. Chem. (1993) [Pubmed]
  10. Characterization of lanthanides as competitors of Na+ and K+ in occlusion sites of renal (Na+,K+)-ATPase. David, P., Karlish, S.J. J. Biol. Chem. (1991) [Pubmed]
  11. Mild myocardial stunning affects platelet aggregation and certain hemostatic factors in swine. Serebruany, V.L., Yurovsky, V.V., Gurbel, P.A. Clin. Appl. Thromb. Hemost. (1999) [Pubmed]
  12. Effects of Ca2+ and Mg2+ on the actin-activated ATP hydrolysis by phosphorylated heavy meromyosin from arterial smooth muscle. Kaminski, E.A., Chacko, S. J. Biol. Chem. (1984) [Pubmed]
  13. Reverse genetics system for porcine enteric calicivirus, a prototype sapovirus in the Caliciviridae. Chang, K.O., Sosnovtsev, S.S., Belliot, G., Wang, Q., Saif, L.J., Green, K.Y. J. Virol. (2005) [Pubmed]
  14. Meconium and amniotic fluid embolism: effects on coagulation in pregnant mini-pigs. Petroianu, G.A., Altmannsberger, S.H., Maleck, W.H., Assmus, H.P., Friedberg, C., Bergler, W.F., Rüfer, R. Crit. Care Med. (1999) [Pubmed]
  15. Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase. Marcus, F., Harrsch, P.B. Arch. Biochem. Biophys. (1990) [Pubmed]
  16. Proteasomal interference prevents zona pellucida penetration and fertilization in mammals. Sutovsky, P., Manandhar, G., McCauley, T.C., Caamaño, J.N., Sutovsky, M., Thompson, W.E., Day, B.N. Biol. Reprod. (2004) [Pubmed]
  17. Characterization and structural aspects of the enhanced assembly of tubulin after removal of its carboxyl-terminal domain. Maccioni, R.B., Serrano, L., Avila, J., Cann, J.R. Eur. J. Biochem. (1986) [Pubmed]
  18. Polarized expression of Na+/H+ exchange activity in LLC-PK1/PKE20 cells: II. Hormonal regulation. Casavola, V., Reshkin, S.J., Murer, H., Helmle-Kolb, C. Pflugers Arch. (1992) [Pubmed]
  19. Isolation and characterization of a Na-H antiporter-deficient mutant of LLC-PK1 cells. Agarwal, N., Haggerty, J.G., Adelberg, E.A., Slayman, C.W. Am. J. Physiol. (1986) [Pubmed]
  20. Iron-sulfur cluster in aconitase. Crystallographic evidence for a three-iron center. Robbins, A.H., Stout, C.D. J. Biol. Chem. (1985) [Pubmed]
  21. Circular dichroism investigation of Escherichia coli adenylate kinase. Monnot, M., Gilles, A.M., Girons, I.S., Michelson, S., Bârzu, O., Fermandjian, S. J. Biol. Chem. (1987) [Pubmed]
  22. Zinc ion-induced assembly of tubulin. Gaskin, F., Kress, Y. J. Biol. Chem. (1977) [Pubmed]
  23. The kinetic mechanism of D-amino acid oxidase with D-alpha-aminobutyrate as substrate. Effect of enzyme concentration on the kinetics. Fitzpatrick, P.F., Massey, V. J. Biol. Chem. (1982) [Pubmed]
  24. Biosynthesis of lipid-linked oligosaccharides in cotton fibers. Stimulation by lipids from pig liver. Forsee, W.T., Elbein, A.D. J. Biol. Chem. (1977) [Pubmed]
  25. Multilayer structures in lipid monolayer films containing surfactant protein C: effects of cholesterol and POPE. Malcharek, S., Hinz, A., Hilterhaus, L., Galla, H.J. Biophys. J. (2005) [Pubmed]
  26. Platelet plasminogen activator inhibitor: purification and characterization of interaction with plasminogen activators and activated protein C. Fay, W.P., Owen, W.G. Biochemistry (1989) [Pubmed]
  27. Effects of a novel Mac-1 inhibitor, NPC 15669, on hemostatic parameters during preconditioned myocardial infarction. Serebruany, V.L., Yurovsky, V.V., Gurbel, P.A. Life Sci. (1999) [Pubmed]
  28. Hemostatic changes after early versus late intracoronary magnesium during acute myocardial infarction in swine. Serebruany, V.L., Herzog, W.R., Schlossberg, M.L., Edenbaum, L.R., Gurbel, P.A. J. Cardiovasc. Pharmacol. (1996) [Pubmed]
  29. Cysteine labeling studies of beef heart aconitase containing a 4Fe, a cubane 3Fe, or a linear 3Fe cluster. Plank, D.W., Kennedy, M.C., Beinert, H., Howard, J.B. J. Biol. Chem. (1989) [Pubmed]
  30. Reverse-phase HPLC of the hydrophobic pulmonary surfactant proteins: detection of a surfactant protein C isoform containing Nepsilon-palmitoyl-lysine. Gustafsson, M., Curstedt, T., Jörnvall, H., Johansson, J. Biochem. J. (1997) [Pubmed]
  31. Serial changes of natural antithrombotics during myocardial ischemia-reperfusion in swine. Effects of magnesium, diltiazem, and a novel Mac-1 inhibitor. Serebruany, V.L., Herzog, W.R., Gurbel, P.A. Blood Coagul. Fibrinolysis (1996) [Pubmed]
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