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Chemical Compound Review

AC1Q5JPJ     (2R)-N-[(1S)-1-[[(2S)-5...

Synonyms: AR-1I7035, S-2302, S-2648, AC1L3X44, 64816-19-9, ...
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Disease relevance of S-2302


High impact information on S-2302


Biological context of S-2302

  • Prekallikrein decreased significantly (p less than 0.01) from 1.49 +/- 0.15 S-2302 U/ml (mean +/- SEM) in early labor to 1.26 +/- 0.13 S-2302 U/ml in the immediate postpartum period [8].
  • The medicinal leech salivary gland secretion deprived of hirudin antithrombin activity inhibits amidolytic (substrate S-2302) and kininogenase (substrate kininogen) activities of plasma kallikrein, the main component of the intrinsic mechanism of blood coagulation [9].

Anatomical context of S-2302

  • The surface contacted plasmas cleaved the kallikrein-specific reagent S-2302 both after single surface contact, and after reincubation of surfaces in fresh plasma [10].

Associations of S-2302 with other chemical compounds


Gene context of S-2302


Analytical, diagnostic and therapeutic context of S-2302

  • In fractions from gel filtration of CPLa kallikrein was assayed as S-2302 amidase, high molecular weight kininogen (HK) was measured in rocket immunoassays, and HK and FXII were studied in PAGE immunoblot experiments [20].
  • Functional assays carried out with different peptide substrates (S-2222 for FXIIa, and S-2222, S-2302 and Bz-Pro-Phe-Arg-pNA for kallikrein) showed increases in OC plasma to about 150% for both proteases, in accordance with results obtained in radial immunodiffusion (RID) [21].


  1. Plasma prekallikrein: quantitative determination by direct activation with Hageman factor fragment (beta-XIIa). Alving, B.M., Tankersley, D.L., Mason, B.L. J. Lab. Clin. Med. (1983) [Pubmed]
  2. Dextran sulphate activation of the contact system in plasma and ascites. Johansen, H.T., Buøo, L., Karlsrud, T.S., Aasen, A.O. Thromb. Res. (1994) [Pubmed]
  3. Isolation and functional properties of the heavy and light chains of human plasma kallikrein. van der Graaf, F., Tans, G., Bouma, B.N., Griffin, J.H. J. Biol. Chem. (1982) [Pubmed]
  4. Autoactivation of human Hageman factor. Demonstration utilizing a synthetic substrate. Silverberg, M., Dunn, J.T., Garen, L., Kaplan, A.P. J. Biol. Chem. (1980) [Pubmed]
  5. Characterization of cerastobin, a thrombin-like enzyme from the venom of Cerastes vipera (Sahara sand viper). Farid, T.M., Tu, A.T., el-Asmar, M.F. Biochemistry (1989) [Pubmed]
  6. Determination of frequency of T cells expressing the T cell-specific serine proteinase 1 (TSP-1) reveals two types of L3T4+ T lymphocytes. Fruth, U., Nerz, G., Prester, M., Simon, H.G., Kramer, M.D., Simon, M.M. Eur. J. Immunol. (1988) [Pubmed]
  7. Different assessment of plasmin with different substrates. In vitro alteration of plasmin, influence of epsilon-aminocaproic acid and tranexamic acid upon its activity. Lämmle, B., Duckert, F. Thromb. Haemost. (1980) [Pubmed]
  8. Human plasma prekallikrein and high molecular weight kininogen decrease during parturition. Alving, B.M., Niebyl, J.R., Proud, D., Mason, B.L., Pisano, J.J. Thromb. Res. (1984) [Pubmed]
  9. Inhibition of plasma kallikrein. Kininase and kinin-like activities of preparations from the medicinal leeches. Baskova, I.P., Khalil, S., Nartikova, V.F., Paskhina, T.S. Thromb. Res. (1992) [Pubmed]
  10. Blood plasma contact activation on silicon, titanium and aluminium. Arvidsson, S., Askendal, A., Tengvall, P. Biomaterials (2007) [Pubmed]
  11. Isolation of a hemorrhagic toxin from Mojave rattlesnake (Crotalus scutulatus scutulatus) venom. Martinez, M., Rael, E.D., Maddux, N.L. Toxicon (1990) [Pubmed]
  12. Prekallikrein activation in human, bovine, and rabbit plasmas: presence of an inhibitor in bovine plasma. Weerasinghe, K.M. Inflammation (1992) [Pubmed]
  13. Contact activation factors in plasma from pregnant women--increased level of an association between factor XII and kallikrein. Briseid, K., Hoem, N.O., Johannesen, S., Fossum, S. Thromb. Res. (1991) [Pubmed]
  14. Jerdonase, a novel serine protease with kinin-releasing and fibrinogenolytic activity from Trimeresurus jerdonii venom. Jia, Y.H., Jin, Y., Lü, Q.M., Li, D.S., Wang, W.Y., Xiong, Y.L. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (2003) [Pubmed]
  15. Dynamics of kallikrein activity in different biological fluids of pregnant animals. Helili, K., Somlev, B., Karcheva, V. Agents Actions Suppl. (1992) [Pubmed]
  16. Acetylcysteine in rats: inhibition of activation of prekallikrein and factor XII--protection against dextran-induced blood pressure fall. Hoem, N.O., Briseid, G. Pharmacol. Toxicol. (1987) [Pubmed]
  17. Contact factor proteases and the complexes formed with alpha 2-macroglobulin can interfere in protein C assays by cleaving amidolytic substrates. Mackie, I.J., Gallimore, M., Machin, S.J. Blood Coagul. Fibrinolysis (1992) [Pubmed]
  18. Changes in plasma active and inactive renin and prekallikrein during hemodialysis. Tsai, T.J., Wu, C.Y., Chen, Y.M., Hsieh, B.S., Chen, W.Y., Yen, T.S. J. Formos. Med. Assoc. (1991) [Pubmed]
  19. Effect of sodium depletion on active renin, inactive renin and prekallikrein in plasma and urinary kallikrein excretion in glomerulonephritic patients. Tsai, T.J., Chen, W.Y., Yen, T.S. J. Formos. Med. Assoc. (1990) [Pubmed]
  20. Functional correlation between kallikrein and factor XII activated in human plasma. Briseid, K., Hoem, N.O., Johannesen, S., Marthinsen, K. Thromb. Res. (1990) [Pubmed]
  21. Contact factors in plasma from women on oral contraception--significance of factor XI for the measured activity of factor XII. Fossum, S., Hoem, N.O., Johannesen, S., Korpberget, M., Nylund, E., Sandem, S., Briseid, K. Thromb. Res. (1994) [Pubmed]
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