Characterization and Substrate Specificities of Various Mouse Kallikreins

  • Obaid U. Beg
  • Mukarram Uddin


Kallikrein gene family in mouse consists of 25 gene members.Only few members of this family have been characterized.These include epidermal growth factor binding proteins A, -B, -C, γ-renin, α- and γ- nerve growth factors (α- and γ-NGF’s) and prorenin converting enzyme.These proteins show specificity towards various growth factors and enzymes.We have carried out the characterization of mK11, a product of clone mKlk-11. This protein was present at higher levels in the mice genetically selected for high blood pressure.However, the protein was not detected in the mice selected for low blood pressure. The substrate specificity of this protein was tested on tetradecapeptide (TDP, a renin substrate) and β-lactoglobulin (β-lg). The protein shows specificity toward Tyr-Ile (4–5) bond in TDP and Tyr-Ser (20–21) and Arg-Val (40–41) bonds in β-lg. Another member of the kallikrein family, γ-NGF was found to cleave the Phe-His (8–9) bond in TDP.The cleavage specificity of these proteins raises the possibility of the involvement of these proteins in the processing of angiotensin-II (AT-II). Furthermore, these proteins may play a role in the regulation of local blood pressure/flow. The characterization of these kallikrein family members and determination of their substrate specificities is presented.


Nerve Growth Factor Substrate Specificity Renin Angiotensin System Amino Acid Sequence Analysis Iodoacetic Acid 
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  1. 1.
    Evans,B.A., Drinkwater,C.C. and Richards, R.I. (1987) J.Biol.Chem. 262: 8027–8034.PubMedGoogle Scholar
  2. 2.
    Carretero, O.A., Carbini, L.A. and Scicili, A.G. (1993) J. Hypertension 11: 693–697.CrossRefGoogle Scholar
  3. 3.
    Drinkwater, C.C., Evans, B.A. and Richards, R.I. (1987) Biochemistry 26: 6750–6756.PubMedCrossRefGoogle Scholar
  4. 4.
    Kim, W.S., Nakayama, K., Nakagawa, T., Kawamura, Y., Haraguchi, K. and Murakami, K. (1991) J.Biol.Chem. 266: 19283–19287.PubMedGoogle Scholar
  5. 5.
    Evans, B.A. and Richards, R.I. (1985) EMBO.J. 4: 133–138.PubMedGoogle Scholar
  6. 6.
    Drinkwater, C.C., Evans, B.A. and Richards, R.I. (1988) J.Biol.Chem. 263: 8565–8568.PubMedGoogle Scholar
  7. 7.
    Clements, J.A. (1989) Endocrine Rev. 10: 393–419.CrossRefGoogle Scholar
  8. 8.
    Moreau,T., Brillard-Bourdet, M., Bouhnik, J. and Gauthier, F. (1992) J.Biol.Chem. 267: 10045–10051.PubMedGoogle Scholar
  9. 9.
    Darby, I.A. (1986) Location of renin and angiotensinogen gene expression using hybridization histochemistry, Ph.D. thesis, University of Melbourne, Australia.Google Scholar
  10. 10.
    Kageyama, R., Ohkubo, H. and Nakanishi, S. (1984) Biochemistry 23: 3603–3609.PubMedCrossRefGoogle Scholar
  11. 11.
    Drinkwater, C.C., Evans, B.A. and Richards, R.I. (1988) TIBS, 169–172.Google Scholar
  12. 12.
    Erdos, E.G. and Skidgel, R.A. (1990) Kidney International 38: S24 - S27.Google Scholar
  13. 13.
    Edwards, R.H., Shelby, M.J., Garcia, P.B. and Rutter, W.J. (1988) J.Biol.Chem. 263: 6810–6815.PubMedGoogle Scholar
  14. 14.
    Wang, M.H., Gonias, S.L., Skeel, A., Wolf, B.B., Yoshimura, T. and Leonard, E.J. (1994) J.Biol.Chem. 269: 13806–13810.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Obaid U. Beg
    • 1
  • Mukarram Uddin
    • 1
  1. 1.Department of Anatomy and Cell Biology and Molecular Biology Core Facility Division of Biomedical SciencesMeharry Medical CollegeNashvilleUSA

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