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Calmodulin-binding peptides isolated from α-casein peptone

Published online by Cambridge University Press:  01 June 2009

Kenji Kizavva ,
Keiko Naganuma  and
Umeji Murakami
Kenji Kizavva
Affiliation:
Biochemistry Laboratory, Kanebo Ltd, 5-3-28 Kotobuki-cho, Odawara 250, Japan
Keiko Naganuma
Affiliation:
Biochemistry Laboratory, Kanebo Ltd, 5-3-28 Kotobuki-cho, Odawara 250, Japan
Umeji Murakami
Affiliation:
Biochemistry Laboratory, Kanebo Ltd, 5-3-28 Kotobuki-cho, Odawara 250, Japan
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Summary

Peptides that inhibit calmodulin-dependent cyclic nucleotide phosphodiesterase were isolated from a pepsin digest of α-casein. Analysis of these peptides showed that they corresponded to the αs2-casein sequences 164–179 (Leu–Lys–Lys–Ile–Ser–Gln–Arg–Tyr–Gln–Lys–Phe–Ala–Leu–Pro–Gln–Tyr), 183–206 (Val–Tyr–Gln–His–Gln–Lys–Ala–Met–Lys–Pro–Trp–Ile–Gln–Pro–Lys–Thr–Lys–Val–Ile–Pro–Tyr–Val–Arg–Tyr) and 183–207 (C-terminus, Val–Tyr–Gln–His–Gln–Lys–Ala–Met–Lys–Pro–Trp–Ile–Gln–Pro–Lys–Thr–Lys–Val–Ile–Pro–Tyr–Val–Arg–Tyr–Leu). These peptides inhibited calmodulin-induced cyclic nucleotide phosphodiesterase activity over the range 1–50 μM without affecting the basal enzyme activity. These results demonstrated that the affinities of these peptides for calmodulin are comparable to the affinities of certain endogenous neurohormones and proteins that interact with calmodulin.

Type
Original Articles
Information
Journal of Dairy Research , Volume 62 , Issue 4 , November 1995 , pp. 587 - 592
Copyright
Copyright © Proprietors of Journal of Dairy Research 1995

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References

REFERENCES

Anderson, J. P. & Morrow, J. S. 1987 The interaction of calmodulin with human erythrocyte spectrin: inhibition of protein 4.1-stimulated actin binding. Journal of Biological Chemistry 262 6365–6372CrossRefGoogle ScholarPubMed
Brignon, G., Ribadeau Dumas, B., Mercier, J. -C, Pélissier, J. -P. & Das, B. C. 1977 Complete amino acid sequence of bovine αs2-casein. FEBS Letters 76 274–279Google Scholar
Chastre, E., Emami, S., Rosselin, G. & Gespach, C. 1987 Ontogenic development of vasoactive intestinal peptide receptors in rat intestinal cells and liver. Endocrinology 121 2211–2221CrossRefGoogle ScholarPubMed
Fiat, A. -M., Migliore-Samour, D., JollèS, P., Drouet, L., Sollier, C. B. D. & Caen, J. 1993 Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities. Journal of Dairy Science 76 301–310CrossRefGoogle ScholarPubMed
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. 1951 Protein measurement with the Folin phenol reagent.Journal of Biological Chemistry 193 265–275CrossRefGoogle ScholarPubMed
McIlroy, B. K., Walters, J. D., Blackshear, P. J. & Johnson, J. D. 1991 Phosphorylation-dependent binding of a synthetic MARCKS peptide to calmodulin. Journal of Biological Chemistry 266 4959–4964Google Scholar
Malencik, D. A. & Anderson, S. R. 1983 Binding of hormones and neuropeptides by calmodulin. Biochemistry 22 1995–2001Google Scholar
Marston, S. B., Fraser, I. D. C., Huber, P. A. J., Pritchard, K., Gusev, N. B. & Torok, K. 1994 Location of two contact sites between human smooth muscle caldesmon and Ca2+-calmodulin. Journal of Biologica Chemistry 269 8134–8139CrossRefGoogle Scholar
Mezgueldi, M., Derancourt, J., Calas, B., Kassab, R. & Fattoum, A. 1994 Precise identification of the regulatory F-actin- and calmodulin-binding sequences in the 10-kDa carboxyl-terminal domain of caldesmon. Journal of Biological Chemistry 269 12824–12832CrossRefGoogle ScholarPubMed
O'Neil, K. T. & DeGrado, W. F. 1990 How calmodulin binds its targets: sequence independent recognition of amphiphilic a-helices. Trends in Biochemical Sciences 15 59–64CrossRefGoogle Scholar
Payne, M. E., Fong, Y. -L., Ono, T., Colbran, R. J., Kemp, B. E., Soderling, T. R. & Means, A. R. 1988 Calcium/calmodulin-dependent protein kinase II: characterization of distinct calmodulin binding and inhibitory domains. Journal of Biological Chemistry 263 7190–7195CrossRefGoogle ScholarPubMed
Sellinger-Barnette, M. & Weiss, B. 1982 Interaction of β-endorphin and other opioid peptides with calmodulin. Molecular Pharmacology 21 86–91Google ScholarPubMed
Weinman, S. J., Weinman, J. S. & Rainteau, D. P. 1994 Calmodulin in rat enterocyte: an immunogold electron-microscope study. Cell and Tissue Research 276 353–357CrossRefGoogle ScholarPubMed
Weiss, B., Lehne, R. & Strada, S. 1972 Rapid microassay of adenosine 3′, 5′-monophosphate phosphodiesterase activity. Analytical Biochemistry 45 222–235CrossRefGoogle ScholarPubMed