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SERPIND1  -  serpin peptidase inhibitor, clade D...

Homo sapiens

Synonyms: D22S673, HC-II, HC2, HCF2, HCII, ...
 
 
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Disease relevance of SERPIND1

  • Proteolysis products of HCII could play a role in the initial influx of PMN into a thrombus, and in the transition from acute to chronic inflammation, or to granulation and healing [1].
  • Hexahistidine-tagged HCII proteins lacking residues 1-66 (H6delta66HCII) containing either the wild-type Val 439 or one of six substitutions were-expressed in E. coli [2].
  • HCII activity increases during pregnancy, and HCII levels are significantly decreased in women with severe pre-eclampsia [3].
  • To understand the molecular mechanism for HCII deficiency in a patient with reduced circulating HCII antigen, we studied a Japanese patient with type I HCII deficiency who suffered from angina pectoris and coronary artery disease [4].
  • The concentrations of heparin cofactor II are higher in the plasmas of individuals with congenital antithrombin III deficiency and pregnant women than controls [5].
 

Psychiatry related information on SERPIND1

  • 1. Six Id- cell lines that secrete IgM kappa but lack Pr2 specificity were generated from an Id+ cell line, LS2 [6].
 

High impact information on SERPIND1

 

Chemical compound and disease context of SERPIND1

 

Biological context of SERPIND1

 

Anatomical context of SERPIND1

 

Associations of SERPIND1 with chemical compounds

 

Physical interactions of SERPIND1

  • Both thrombin-antithrombin III and thrombin-heparin cofactor II complexed with vitronectin were detected in all the plasmas [5].
  • The crystal structure of a heparin cofactor II (HCII)-thrombin Michaelis complex has revealed extensive contacts encompassing the N-terminal domain of HCII and exosite I of the proteinase [18].
  • In the APL group, the HC II level had a significant negative correlation with the thrombin-AT III complex (TAT), fibrinogen/fibrin degradation products, and D-dimer levels as well as the prothrombin time, while AT III showed no correlations with any of the haemostatic parameters [19].
 

Enzymatic interactions of SERPIND1

 

Regulatory relationships of SERPIND1

 

Other interactions of SERPIND1

  • We examined the contribution of Val439 to the reaction of HCII with thrombin and NE [2].
  • Using 0.03U/ml thrombin and 1nM HCII the stimulatory effect of GAGs was completely inhibited when Hep (less than or equal to 0.3 micrograms/ml) was preincubated with VN (60 micrograms/ml) and decreased to less than 50% when HS (50 micrograms/ml) was preincubated with VN (60 micrograms/ml) [23].
  • Furthermore, it can be deduced that the amino acid residues, proposed to mediate heparin binding in the serpins antithrombin III and heparin cofactor II, are conserved in PAI-1 [24].
  • Protein C inhibitor (PCI), antithrombin, and heparin cofactor II are members of the serine proteinase inhibitor (serpin) superfamily that inhibit proteinases at rates which increase in the presence of the glycosaminoglycan heparin [25].
  • In experiments with purified proteases, HCII did not significantly inhibit coagulation factors VIIa, IXa, Xa, XIa, XIIa, kallikrein, activated protein C, plasmin, urokinase, tissue plasminogen activator, leukocyte elastase, the gamma-subunit of nerve growth factor, and the epidermal growth factor-binding protein [26].
 

Analytical, diagnostic and therapeutic context of SERPIND1

References

  1. Characteristics of the chemotactic activity of heparin cofactor II proteolysis products. Hoffman, M., Pratt, C.W., Corbin, L.W., Church, F.C. J. Leukoc. Biol. (1990) [Pubmed]
  2. Altering heparin cofactor II at VAL439 (P6) either impairs inhibition of thrombin or confers elastase resistance. Cunningham, M.A., Bhakta, V., Sheffield, W.P. Thromb. Haemost. (2002) [Pubmed]
  3. Placental dermatan sulfate: isolation, anticoagulant activity, and association with heparin cofactor II. Giri, T.K., Tollefsen, D.M. Blood (2006) [Pubmed]
  4. Molecular and cellular basis for type I heparin cofactor II deficiency (heparin cofactor II Awaji). Kondo, S., Tokunaga, F., Kario, K., Matsuo, T., Koide, T. Blood (1996) [Pubmed]
  5. Inhibition of thrombin by antithrombin III and heparin cofactor II in vivo. Liu, L., Dewar, L., Song, Y., Kulczycky, M., Blajchman, M.A., Fenton, J.W., Andrew, M., Delorme, M., Ginsberg, J., Preissner, K.T. Thromb. Haemost. (1995) [Pubmed]
  6. Structural basis of a conserved idiotope expressed by an autoreactive human B cell lymphoma. Evidence that a VH CDR3 mutation alters idiotypy and specificity. Reidl, L.S., Friedman, D.F., Goldman, J., Hardy, R.R., Jefferies, L.C., Silberstein, L.E. J. Immunol. (1991) [Pubmed]
  7. Shape-shifting serpins--advantages of a mobile mechanism. Huntington, J.A. Trends Biochem. Sci. (2006) [Pubmed]
  8. An anticoagulant dermatan sulfate proteoglycan circulates in the pregnant woman and her fetus. Andrew, M., Mitchell, L., Berry, L., Paes, B., Delorme, M., Ofosu, F., Burrows, R., Khambalia, B. J. Clin. Invest. (1992) [Pubmed]
  9. Modulation of heparin cofactor II activity by histidine-rich glycoprotein and platelet factor 4. Tollefsen, D.M., Pestka, C.A. J. Clin. Invest. (1985) [Pubmed]
  10. Structure-activity relationships of heparin. Independence of heparin charge density and antithrombin-binding domains in thrombin inhibition by antithrombin and heparin cofactor II. Hurst, R.E., Poon, M.C., Griffith, M.J. J. Clin. Invest. (1983) [Pubmed]
  11. Homozygous deficiency of heparin cofactor II: relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis. Corral, J., Aznar, J., Gonzalez-Conejero, R., Villa, P., Miñano, A., Vayá, A., Carrell, R.W., Huntington, J.A., Vicente, V. Circulation (2004) [Pubmed]
  12. Decreased sensitivity to heparin in vitro in steroid-responsive nephrotic syndrome. Vermylen, C.G., Levin, M., Lanham, J.G., Hardisty, R.M., Barratt, T.M. Kidney Int. (1987) [Pubmed]
  13. Hereditary heparin cofactor II deficiency and the risk of development of thrombosis. Bertina, R.M., van der Linden, I.K., Engesser, L., Muller, H.P., Brommer, E.J. Thromb. Haemost. (1987) [Pubmed]
  14. Plasma heparin cofactor II in alcoholic liver disease. Andersson, T.R., Bell, H. J. Hepatol. (1988) [Pubmed]
  15. Ability of the digene hybrid capture II test to identify Chlamydia trachomatis and Neisseria gonorrhoeae in cervical specimens. Schachter, J., Hook, E.W., McCormack, W.M., Quinn, T.C., Chernesky, M., Chong, S., Girdner, J.I., Dixon, P.B., DeMeo, L., Williams, E., Cullen, A., Lorincz, A. J. Clin. Microbiol. (1999) [Pubmed]
  16. Heparin cofactor II-proteinase reaction products exhibit neutrophil chemoattractant activity. Hoffman, M., Pratt, C.W., Brown, R.L., Church, F.C. Blood (1989) [Pubmed]
  17. Leukocyte chemoattractant peptides from the serpin heparin cofactor II. Church, F.C., Pratt, C.W., Hoffman, M. J. Biol. Chem. (1991) [Pubmed]
  18. Reformable intramolecular cross-linking of the N-terminal domain of heparin cofactor II: effects on enzyme inhibition. Brinkmeyer, S., Eckert, R., Ragg, H. Eur. J. Biochem. (2004) [Pubmed]
  19. Preferential consumption of heparin cofactor II in disseminated intravascular coagulation associated with acute promyelocytic leukemia. Kario, K., Matsuo, T., Kodama, K., Katayama, S., Kobayashi, H. Thromb. Res. (1992) [Pubmed]
  20. Modulation of heparin cofactor II function by S protein (vitronectin) and formation of a ternary S protein-thrombin-heparin cofactor II complex. Preissner, K.T., Sié, P. Thromb. Haemost. (1988) [Pubmed]
  21. Isolation and characterization of a partial cDNA clone for heparin cofactor II1. Inhorn, R.C., Tollefsen, D.M. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  22. Altered dermatan sulfate structure and reduced heparin cofactor II-stimulating activity of biglycan and decorin from human atherosclerotic plaque. Shirk, R.A., Parthasarathy, N., San Antonio, J.D., Church, F.C., Wagner, W.D. J. Biol. Chem. (2000) [Pubmed]
  23. Modulation of heparin cofactor II activity by glycosaminoglycans and adhesive glycoproteins. Petzelbauer, E., Seiffert, D., Beckmann, R., Pusch, B., Geiger, M., Binder, B.R. Thromb. Res. (1992) [Pubmed]
  24. Functional interaction of plasminogen activator inhibitor type 1 (PAI-1) and heparin. Ehrlich, H.J., Keijer, J., Preissner, K.T., Gebbink, R.K., Pannekoek, H. Biochemistry (1991) [Pubmed]
  25. Modulation of protein C inhibitor activity. Neese, L.L., Pratt, C.W., Church, F.C. Blood Coagul. Fibrinolysis (1994) [Pubmed]
  26. The protease specificity of heparin cofactor II. Inhibition of thrombin generated during coagulation. Parker, K.A., Tollefsen, D.M. J. Biol. Chem. (1985) [Pubmed]
  27. Heparin cofactor IIOslo. Mutation of Arg-189 to His decreases the affinity for dermatan sulfate. Blinder, M.A., Andersson, T.R., Abildgaard, U., Tollefsen, D.M. J. Biol. Chem. (1989) [Pubmed]
  28. Identification of two sites of sulfation of human heparin cofactor II. Hortin, G., Tollefsen, D.M., Strauss, A.W. J. Biol. Chem. (1986) [Pubmed]
  29. Complete nucleotide sequence of the gene for human heparin cofactor II and mapping to chromosomal band 22q11. Herzog, R., Lutz, S., Blin, N., Marasa, J.C., Blinder, M.A., Tollefsen, D.M. Biochemistry (1991) [Pubmed]
 
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