Isozyme-specific antagonists of protein kinase C

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Reexamination Certificate

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C514S021700, C514S021800

Reexamination Certificate

active

07994133

ABSTRACT:
A method of changing or otherwise converting the biological activity of a PKC peptide agonist to a peptide antagonist is described. The method involves substituting one or more amino acid residues so as to effect a change in charge in the peptide and/or to otherwise make the sequence similar to a sequence derived from the PKC binding site on the RACK protein for the respective PKC enzyme. Methods of inhibiting the activity of a PKC enzyme, and various peptide antagonists of εPKC are also disclosed.

REFERENCES:
patent: 4120815 (1978-10-01), Raman
patent: 4457371 (1984-07-01), McCoy et al.
patent: 4673511 (1987-06-01), Richardson et al.
patent: 4699951 (1987-10-01), Allensen et al.
patent: 4734205 (1988-03-01), Jacques et al.
patent: 5128046 (1992-07-01), Marble et al.
patent: 5783405 (1998-07-01), Mochly-Rosen et al.
patent: 6042732 (2000-03-01), Jankowski et al.
patent: 6165977 (2000-12-01), Mochly-Rosen
patent: 6376467 (2002-04-01), Messing et al.
patent: 6686334 (2004-02-01), Messing et al.
patent: 7081444 (2006-07-01), Mochly-Rosen
patent: 7459424 (2008-12-01), Mochly-Rosen et al.
patent: 7544654 (2009-06-01), Mochly-Rosen
patent: WO 97/14038 (1997-04-01), None
patent: WO 98/17299 (1998-04-01), None
patent: WO 98/21271 (1998-05-01), None
patent: WO 02/078600 (2002-10-01), None
Aksoy, E. et al., “Protein kinase C epsilon: a new target to control inflammation and immune-mediated disorders”,International Journal of Biochemistry and Cell Biology, 36:183-188 (2004).
Bogatkevich, G,S., et al., “Thrombin differentiates normal lung fibroblasts to a myofibroblast phenotype via the proteolytically activated receptor-1 and a protein kinase C-dependent pathway”,The Journal of Biological Chemistry, 276(48):45184-45192 (2001).
Bradley, C.M. and Barrick, D., “Limits of cooperativity in a structurally modular protein: response of the Notch ankyrin domain to analogous alanine substitutions in each repeat”,Journal of Molecular Biology, 324(2):373-386 (2002).
Chen et al. “Opposing cardioprotective actions and parallel hypertrophic effects of deltaa-PKC and epsilon-PKC,” PNAS, 2001, 96, 11114-9.
Comalada, M. et al., “PKC epsilon is involved in JNK activation that mediates LPS-induced TNF-alpha, which induces apoptosis in macrophages”,Am. J. Physiol. Cell Physiol., 285:C1235-C1245 (2003).
Database UniProt Online!, “Transcription factor 12 (fragment”, retrieved from EBI accession No. UNIPROT: Q9NQY2, abstract (2000).
Disatnik, M.H. et al., “Sequential activation of individual PKC isozymes in integrin-mediated muscle cell spreading: a role for MARCKS in an integrin signaling pathway”Journal of Cell Science, 115(10):2151-2163 (2002).
Dorn II, G.W. et al., “Sustained in vivo cardiac protection by a rationally designed peptide that causes epsilon protein kinase C translocation”,Proc. Natl. Acad. Sci. USA, 96(22):12798-12803 (1999).
Fang, Q. et al., “Thrombin induces collagen gel contraction partially through PAR1 activation and PKC-epsilon”,Eur. Respir. J., 24:918-924 (2004).
Flanagan, J.M. et al., “Truncated staphylococcal nuclease is compact but disordered”,Proc. Natl. Acad. Sci. USA, 89(2):748-752 (1992).
Ginalski, K. et al., “Practical lessons from protein structure prediction”,Nucleic Acid Research, 33(6):1874-1891 (2005).
Johnson, J.A., et al., “A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function”,The Journal of Biological Chemistry, 271(40):24962-24966 (1996).
Pitt, M. et al., “Single amino acid substitution mutants ofKlebsiella pneumoniaesigma(54) defective in transcription”,Nucleic Acid Research, 28(22):4419-4427 (2000).
Ron, D. and Mochly-Rosen, D., “An autoregulatory region in protein kinase C: the pseudoanchoring site”,Proc. Natl. Acad. Sci. USA, 92(2):492-496 (1995).
Ron, D., et al., “C2 region-derived peptides inhibit translocation and function of beta protein kinase C in vivo”,The Journal of Biological Chemistry, 270(41):24180-24187 (1995).
Ron et al,. “Agonists and Antagonists of Protein Kinase C Function, Derived from its Binding Proteins”Journal of Biological Chemistry, 269(34):21395-21398 (1994).
Rudinger, “Characteristic of the amino acids as components of a peptide hormone sequence”, (Peptide Hormones (Ed. J.A. Parson) University Park Press. Baltimore pp. 1-7 (1976).
Sawai, M.V. et al., “Impact of single-residue mutations on the structure and function of ovispirin
ovispirin antimicrobial peptides”,Prot. Engin., 15(3):225-232 (2002).
Schechtman, D. et al., “A critical intramolecular interaction for protein kinase Cepsilon translocation”,The Journal of Biological Chemistry, 279(16):15831-15840 (2004).
Schnog, J.B. et al., “Sickle cell disease; a general overview”,J. Med.62:364-374 (2004).
Souroujon M C et al., “Peptide Modulators of Protein-Protein Interactions in Intracellularsignaling”Nature Biotechnology, Nature Publishing, 16(10):919 (1998).
Wadia & Dowdy “Protein transduction technology,” Curr Opin Biotech, 2002, 13,52-56.
Liron, et al., “Rational design of a selective antagonist of epsilon protein kinase C derived from the selective allosteric agonist, pseudo-RACK peptide”, J. Mol. Cell. Cardiol., vol. 42, No. 4, p. 835-841 (2007).

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