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Gene Review

Klk1c9  -  kallikrein 1-related peptidase C9

Rattus norvegicus

Synonyms: KLK-S3, Klk-9, Klk9, Klks3, S3 kallikrein, ...
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Disease relevance of Klks3

  • Rats were infused with tissue kallikrein protein 5 days before (pretreated group) or after (treated group) ischemia [1].
  • These results indicate that tissue kallikrein, through the kinin B2 receptor, reverses salt-induced inflammation, renal fibrosis, and glomerular hypertrophy via suppression of oxidative stress [2].

Psychiatry related information on Klks3

  • In PER, neither the recovery PmvO2 values nor the mean response time (MRT; a weighted average of the time to 63% of the overall response) were altered by CHF (CON: 66.8 +/- 8.0, MOD: 72.4 +/- 11.8, SEV: 69.1 +/- 9.5 s) [3].

High impact information on Klks3

  • The prostate gland contained only rK9 where it was the major kallikrein-like component [4].
  • The substrate specificities of rK2 and rK9 were correlated with key amino acids defining their substrate binding site.(ABSTRACT TRUNCATED AT 400 WORDS)[4]
  • The restricted specificity of rK2 and rK9 is consistent with the presence of an extended substrate binding site, and hence with a processing enzyme function [4].
  • Their P1 specificities enabled both proteinases to release angiotensin II from angiotensinogen and from angiotensinogen I, but rK9 was at least 100 times less active than rK2 on both substrates [4].
  • The submandibular enzymatic vasoconstrictor is a kallikrein-like enzyme, having some properties of both tonin and thrombin [5].

Biological context of Klks3

  • Recently we have shown that rK9 and rK2 have distinct substrate specificities and sensitivities to inhibitors, despite their similar sequences [6].
  • The final rK9 model is structurally similar to rK2, but variable regions surrounding the active site differ quite markedly from the reference proteins [6].
  • Two proteins (pI 5.30 and 6.75-6.90) corresponded to protein bands in gels of rat submandibular-gland extracts, and were identified by partial amino acid sequence analysis as rK8 and rK9 respectively [7].
  • Competition experiments with Abz-TSVIRRPQ-EDDnp, which is resistant to most kallikreins, and Abz-TSVIRRVQ-EDDnp, a general kallikrein substrate, demonstrated that the former competitively inhibited hydrolysis by rK9 and hK1, with Ki values similar to the Km values for the substrate [8].
  • Its biological function may therefore differ from that of tissue kallikrein, especially as it does not induce a transient decrease in blood pressure when injected in vivo [9].

Anatomical context of Klks3


Associations of Klks3 with chemical compounds

  • The proposed conformation of the specificity pocket in rK9 differs from that of other serine proteinases, but it can still accommodate both aromatic and basic amino acid side chains at the substrate P1 position, thus explaining the dual chymotrypsin and trypsin-like activity of rK9 [6].
  • As a probe we used a phosphorus-32-labeled oligonucleotide specific for SEV mRNA [10].
  • The molecular masses of the prostate rK9 isoenzymes (24,600-29,300 Da) were close to that of submandibular-gland rK9 (24,600 Da), although differences were observed after reduction with mercaptoethanol [7].
  • 4. Treatment with aprotinin to inhibit tissue kallikrein reduced the scratching behaviour induced by sodium deoxycholic acid, whereas treatment with soybean trypsin inhibitor to inhibit plasma kallikrein did not [15].
  • In the intermediate segments, strong rK9-specific staining was observed adhering to the luminal wall as well as abundantly within the ductal lumen [11].

Other interactions of Klks3

  • We studied whether messenger RNA (mRNA) for SEV is present in the kidney and isolated glomeruli, using the polymerase chain reaction assay with primers specific to the entire rat kallikrein family that would amplify a 430-bp fragment from their mRNA [10].
  • Pro-rat atrial natriuretic peptide-mimicking peptides as substrates for rat kallikreins rK2 (tonin) and rK9 [16].
  • Peptide substrates with intramolecularly quenched fluorescence that reproduce the rat kininogen sequences at both ends of the bradykinin moiety were synthesized and used to investigate the kinin-releasing properties of five rat tissue kallikreins (rK1, rK2, rK7, rK9, rK10) [8].
  • The dual trypsin- and chymotrypsin-like enzymatic specificity of rK9 was assessed by determining specificity constants (k(cat)/K(m)) for the hydrolysis of fluorogenic substrates, the peptide sequences of which were derived from proparathyroid hormone (pro-PTH) and from semenogelin-I [13].
  • In addition to uPA, tissue PA (tPA) and tissue kallikrein were the proteases studied [17].

Analytical, diagnostic and therapeutic context of Klks3

  • In addition, sequence analysis revealed complete sequence similarity between rK9 and the immunoreactive prostate proteins with pI 7.15, 7.25, 7.50 and 8.27 [7].
  • In the present study, the immunohistochemical localization of rK9 was determined in rat prostate by the indirect immunofluorescence technique with polyclonal antisera against rat SMG rK9 in the first layer [11].
  • Specificity of the immunofluorescent staining reaction was verified by staining with the primary antiserum after addition of purified SMG or prostate rK9, or other members of the kallikrein family including prostate rK8. rK9-specific immunofluorescence was detected in the prostate ductal structures [11].
  • Mature rK9 was efficiently released from the fusion protein by trypsin and was purified to homogeneity by one-step affinity chromatography using soya bean trypsin inhibitor (SBTI) as affinity ligand [13].
  • PmvO2 dynamics were determined in SOL and PER muscles of control (CON: n= 6; left ventricular end-diastolic pressure, LVEDP: approximately 3 mmHg), moderate CHF (MOD: n= 7; LVEDP: approximately 11 mmHg) and severe CHF (SEV: n= 4; LVEDP: approximately 25 mmHg) following cessation of electrical stimulation (180 s; 1 Hz) [3].


  1. Early activation of bradykinin B2 receptor aggravates reactive oxygen species generation and renal damage in ischemia/reperfusion injury. Chiang, W.C., Chien, C.T., Lin, W.W., Lin, S.L., Chen, Y.M., Lai, C.F., Wu, K.D., Chao, J., Tsai, T.J. Free Radic. Biol. Med. (2006) [Pubmed]
  2. Reversal of renal fibrosis, inflammation, and glomerular hypertrophy by kallikrein gene delivery. Bledsoe, G., Shen, B., Yao, Y., Zhang, J.J., Chao, L., Chao, J. Hum. Gene Ther. (2006) [Pubmed]
  3. Effects of chronic heart failure in rats on the recovery of microvascular PO2 after contractions in muscles of opposing fibre type. McDonough, P., Behnke, B.J., Musch, T.I., Poole, D.C. Exp. Physiol. (2004) [Pubmed]
  4. Protein products of the rat kallikrein gene family. Substrate specificities of kallikrein rK2 (tonin) and kallikrein rK9. Moreau, T., Brillard-Bourdet, M., Bouhnik, J., Gauthier, F. J. Biol. Chem. (1992) [Pubmed]
  5. A novel serine protease with vasoconstrictor activity coded by the kallikrein gene S3. Yamaguchi, T., Carretero, O.A., Scicli, A.G. J. Biol. Chem. (1991) [Pubmed]
  6. Homology modelling of rat kallikrein rK9, a member of the tissue kallikrein family: implications for substrate specificity and inhibitor binding. Moreau, T., Gauthier, F. Protein Eng. (1996) [Pubmed]
  7. Purification of enzymes of the kallikrein gene family (rK8 and rK9) from the rat prostate. Schøyen, H., Wassdal, I., Toft, K., Almendingen, M., Berg, T. Biochem. J. (1994) [Pubmed]
  8. Kininogen-derived fluorogenic substrates for investigating the vasoactive properties of rat tissue kallikreins--identification of a T-kinin-releasing rat kallikrein. El Moujahed, A., Brillard-Bourdet, M., Juliano, M.A., Moreau, T., Chagas, J.R., Gutman, N., Prado, E.S., Gauthier, F. Eur. J. Biochem. (1997) [Pubmed]
  9. Microheterogeneity of rat submaxillary gland kallikrein k10, a member of the kallikrein family. Gutman, N., Elmoujahed, A., Brillard, M., Du Sorbier, B.M., Gauthier, F. Eur. J. Biochem. (1991) [Pubmed]
  10. Submandibular enzymatic vasoconstrictor messenger RNA in rat kidney. Saed, G.M., Beierwaltes, W.H., Carretero, O.A., Scicli, A.G. Hypertension (1992) [Pubmed]
  11. Immunohistochemical localization of rK9, an enzyme of the kallikrein gene family, in the rat ventral prostate. Berg, T., Schøyen, H. J. Histochem. Cytochem. (1995) [Pubmed]
  12. Differences in the glycosylation of rat submandibular kallikreins. Zhang, X.S., Proctor, G.B., Garrett, J.R., Shori, D.K., Carpenter, G.H. Glycoconj. J. (1996) [Pubmed]
  13. Purification and characterization of active recombinant rat kallikrein rK9. Zani, M., Brillard-Bourdet, M., Lazure, C., Juliano, L., Courty, Y., Gauthier, F., Moreau, T. Biochim. Biophys. Acta (2001) [Pubmed]
  14. Induction of salivary kallikreins by the diet containing a sweet-suppressive peptide, gurmarin, in the rat. Yamada, A., Nakamura, Y., Sugita, D., Shirosaki, S., Ohkuri, T., Katsukawa, H., Nonaka, K., Imoto, T., Ninomiya, Y. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  15. Reduction of sodium deoxycholic acid-induced scratching behaviour by bradykinin B2 receptor antagonists. Hayashi, I., Majima, M. Br. J. Pharmacol. (1999) [Pubmed]
  16. Pro-rat atrial natriuretic peptide-mimicking peptides as substrates for rat kallikreins rK2 (tonin) and rK9. Moreau, T., Brillard-Bourdet, M., Chagas, J., Gauthier, F. Biochim. Biophys. Acta (1995) [Pubmed]
  17. Activation of serpins and their cognate proteases in muscle after crush injury. Festoff, B.W., Reddy, R.B., VanBecelaere, M., Smirnova, I., Chao, J. J. Cell. Physiol. (1994) [Pubmed]
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