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KLK1  -  kallikrein 1

Bos taurus

 
 
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Disease relevance of KLK1

 

High impact information on KLK1

  • The localization of glandular pancreatic kallikrein to the beta cells of the islets was the same as that of insulin in normal human pancreas and in two islet-cell tumors [6].
  • When beta cells were lacking in islet-cell tumors or in the pancreas of a patient with juvenile-onset diabetes, kallikrein antigen was not detectable [6].
  • The beta-cell localization of human pancreatic kallikrein, an endopeptidase that, in concert with carboxypeptidase B, converts bovine proinsulin to a polypeptide with the electrophoretic mobility of insulin, suggests that pancreatic kallikrein may be involved in the physiologic activation of proinsulin [6].
  • The data indicate that factor XII can initiate blood coagulation, fibrinolysis or kinin generation in the presence of kaolin and does so by converting prekallikrein to kallikrein [7].
  • Plasma renin activity, prostaglandin A and E levels, and urinary kallikrein, norepinephrine, and epinephrine excretions were within normal limits and did not change notably throughout the trial [8].
 

Biological context of KLK1

  • Whereas its affinity for bovine trypsin, chymotrypsin, and trypsinogen is almost identical to that of BPTI, the affinity for porcine pancreatic kallikrein is decreased, as expected on the basis of the amino acid substitutions [9].
  • Mapping the active sites of bovine thrombin, factor IXa, factor Xa, factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino acid and peptide thioesters: development of new sensitive substrates [10].
  • The peptide generated by sweat kallikrein was identified as lys-bradykinin using reverse phase high-performance liquid chromatography and by its amino acid sequence [11].
  • New aromatic diamidines with central alpha-oxyalkane or alpha, omega-dioxyalkane chains. Structure-activity relationships for the inhibition of trypsin, pancreatic kallikrein, and thrombin and for the inhibition of the overall coagulation process [12].
  • Pre-steady-state data, analyzed in the framework of the three-step model, show that for b. beta-trypsin, b. thrombin, h.u. kallikrein, and h. urokinase the acylation step (k2) is rate limiting above pH 6 and the deacylation step (k3) below pH 4 in the hydrolysis of ZLysONp and of ZAlaONp in the presence of acetamidine or ethylamine [13].
 

Anatomical context of KLK1

 

Associations of KLK1 with chemical compounds

  • When bovine HMW-kininogen was incubated with bovine plasma kallikrein, kinin-free HMW-kininogen, bradykinin, and a glycopeptide fragment (peptide 1-2; 12,584 daltons) were rapidly released [18].
  • Moreover, kallikrein was specific for aggregating PMN, because no aggregation was observed with Factor XII active fragments (23 nM), Factor XIa (0.6 U/ml or 15nM), thrombin (1.6 microM), plasmin (2 microM), porcine pancreatic elastase (2 microM), bovine pancreatic chymotrypsin (2 microM), or bradykinin (1 microM) [1].
  • Kallikrein-induced PMN aggregation was not mediated through C5-derived peptides, because identical responses were observed whether or not kallikrein had been preincubated with an antibody to C5 [1].
  • Kallikrein was a potent aggregant agent for PMN because similar responses were observed with kallikrein (0.5 U/ml or 0.23 microM) and an optimal dose (0.2 microM) of N-formyl-methionyl-leucyl-phenylalanine [1].
  • Since kallikrein is an arginine-directed serine protease, we hypothesized that an altered form of aprotinin, Arg15-aprotinin, might be a better inhibitor [19].
 

Physical interactions of KLK1

 

Enzymatic interactions of KLK1

 

Regulatory relationships of KLK1

  • Sweat kallikrein had a M(r) of 40,000 and was inhibited by aprotinin but not by soybean trypsin inhibitor [11].
  • Studies on prekallikrein of bovine plasma. II. Activation of prekallikrein with proteinases and properties of kallikrein activated by bovine Hageman factor [2].
 

Other interactions of KLK1

 

Analytical, diagnostic and therapeutic context of KLK1

References

  1. Purified human plasma kallikrein aggregates human blood neutrophils. Schapira, M., Despland, E., Scott, C.F., Boxer, L.A., Colman, R.W. J. Clin. Invest. (1982) [Pubmed]
  2. Studies on prekallikrein of bovine plasma. II. Activation of prekallikrein with proteinases and properties of kallikrein activated by bovine Hageman factor. Takahashi, H., Nagasawa, S., Suzuki, T. J. Biochem. (1980) [Pubmed]
  3. Estimation of urinary kininogenase activity using bovine serum low molecular weight kininogen. Abe, K., Kato, H., Sakurai, Y., Itoh, T., Saito, K., Haruyama, T., Otsuka, Y., Yoshinaga, K. Adv. Exp. Med. Biol. (1979) [Pubmed]
  4. A simple and sensitive method for determination of human urinary kallikrein activity (kininogenase activity), using human low molecular weight kininogen. Kondo, M., Shimamoto, K., Ura, N., Nishimiya, T., Mita, T., Nakagawa, M., Maeda, T., Yamaguchi, Y., Iimura, O. Endocrinol. Jpn. (1984) [Pubmed]
  5. Plasma kallikrein elevation in cattle induced with hepatic abscess. Motoi, Y., Takeuchi, S., Nakajima, Y. Nippon Juigaku Zasshi (1987) [Pubmed]
  6. Identification of human glandular kallikrein in the beta cell of the pancreas. ole-MoiYoi, O.K., Pinkus, G.S., Spragg, J., Austen, K.F. N. Engl. J. Med. (1979) [Pubmed]
  7. Surface activation of blood coagulation, fibrinolysis and kinin formation. Heimark, R.L., Kurachi, K., Fujikawa, K., Davie, E.W. Nature (1980) [Pubmed]
  8. Effect of ingestion of meat on plasma cholesterol of vegetarians. Sacks, F.M., Donner, A., Castelli, W.P., Gronemeyer, J., Pletka, P., Margolius, H.S., Landsberg, L., Kass, E.H. JAMA (1981) [Pubmed]
  9. Primary structure and antiproteolytic activity of a Kunitz-type inhibitor from bovine spleen. Fioretti, E., Iacopino, G., Angeletti, M., Barra, D., Bossa, F., Ascoli, F. J. Biol. Chem. (1985) [Pubmed]
  10. Mapping the active sites of bovine thrombin, factor IXa, factor Xa, factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino acid and peptide thioesters: development of new sensitive substrates. McRae, B.J., Kurachi, K., Heimark, R.L., Fujikawa, K., Davie, E.W., Powers, J.C. Biochemistry (1981) [Pubmed]
  11. Human eccrine sweat contains tissue kallikrein and kininase II. Hibino, T., Takemura, T., Sato, K. J. Invest. Dermatol. (1994) [Pubmed]
  12. New aromatic diamidines with central alpha-oxyalkane or alpha, omega-dioxyalkane chains. Structure-activity relationships for the inhibition of trypsin, pancreatic kallikrein, and thrombin and for the inhibition of the overall coagulation process. Geratz, J.D., Cheng, M.C., Tidwell, R.R. J. Med. Chem. (1975) [Pubmed]
  13. Catalytic properties of serine proteases. 2. Comparison between human urinary kallikrein and human urokinase, bovine beta-trypsin, bovine thrombin, and bovine alpha-chymotrypsin. Ascenzi, P., Menegatti, E., Guarneri, M., Bortolotti, F., Antonini, E. Biochemistry (1982) [Pubmed]
  14. The levels of factor XIIa generated in human plasma on an electronegative surface are insensitive to wide variation in the concentration of FXII, prekallikrein, high molecular weight kininogen or FXI. Mitropoulos, K.A. Thromb. Haemost. (1999) [Pubmed]
  15. Bradykinin stimulates aldosterone release from cultured bovine adrenocortical cells through bradykinin B2 receptors. Rosolowsky, L.J., Campbell, W.B. Endocrinology (1992) [Pubmed]
  16. Assembly and activation of HK-PK complex on endothelial cells results in bradykinin liberation and NO formation. Zhao, Y., Qiu, Q., Mahdi, F., Shariat-Madar, Z., Røjkjaer, R., Schmaier, A.H. Am. J. Physiol. Heart Circ. Physiol. (2001) [Pubmed]
  17. Dynamics of exogenous kallikrein-stimulated bovine sperm motility in the presence of seminal plasma kallikrein. Somlev, B., Subev, M. Theriogenology (1997) [Pubmed]
  18. Flaujeac factor deficiency. Reconstitution with highly purified bovine high molecular weight-kininogen and delineation of a new permeability-enhancing peptide released by plasma kallikrein from bovine high molecular weight-kininogen. Matheson, R.T., Miller, D.R., Lacombe, M.J., Han, Y.N., Iwanaga, S., Kato, H., wuepper, K.D. J. Clin. Invest. (1976) [Pubmed]
  19. Kinetics of inhibition of human plasma kallikrein by a site-specific modified inhibitor Arg15-aprotinin: evaluation using a microplate system and comparison with other proteases. Scott, C.F., Wenzel, H.R., Tschesche, H.R., Colman, R.W. Blood (1987) [Pubmed]
  20. Endothelial cells and components of the kallikrein-kinin system. Ryan, U.S., Ryan, J.W., Habliston, D.L., Pena, G.A. Adv. Exp. Med. Biol. (1979) [Pubmed]
  21. Bradykinin and kininogens in bovine milk. Wilson, W.E., Lazarus, L.H., Tomer, K.B. J. Biol. Chem. (1989) [Pubmed]
  22. Studies on the primary structure of bovine high-molecular-weight kininogen. Amino acid sequence of a fragment ("histidine-rich peptide") released by plasma kallikrein. Han, Y.N., Komiya, M., Iwanaga, S., Suzuki, T. J. Biochem. (1975) [Pubmed]
  23. Catalytic properties of human urinary kallikrein. Antonini, E., Ascenzi, P., Menegatti, E., Bortolotti, F., Guarneri, M. Biochemistry (1982) [Pubmed]
  24. Activation of bovine factor XII (Hageman factor) by plasma kallikrein. Fujikawa, K., Heimark, R.L., Kurachi, K., Davie, E.W. Biochemistry (1980) [Pubmed]
  25. An in vitro bovine pericardial hemocompatibility testing system. Amrani, D.L., Lee, C., Earles, K., DiOrio, J., Murphy, M., Yang, J., Rubalcaba, S., LiVecchi, A. J. Heart Valve Dis. (1998) [Pubmed]
  26. Fumaric acid, anti-thrombin substance from Rhizopus javanicus. Okamura, T., Horie, N., Miyazaki, Y., Ohsugi, M. J. Nutr. Sci. Vitaminol. (1997) [Pubmed]
  27. Refined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibitor complex. Chen, Z., Bode, W. J. Mol. Biol. (1983) [Pubmed]
  28. Hydroxyprolyl3-bradykinin in high molecular mass kininogen. Presence in human and monkey kininogens, but not in kininogens from bovine, rat, rabbit, guinea pig and mouse plasmas. Enjyoji, K., Kato, H. FEBS Lett. (1988) [Pubmed]
  29. Tissue kallikrein activity in seminal plasma of bovine ejaculates with different quality. Somlev, B., Helili, K., Karcheva, V. Theriogenology (1996) [Pubmed]
 
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