Coupling factor 6 inhibitor and potentiator and use thereof

Details Coupling factor 6 inhibitor and potentiator and use thereof Coupling factor 6 inhibitor and potentiator and use thereof

2006-05-23

2006-05-23

Nolan, Patrick J. (Department: 1644)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving antigen-antibody binding, specific binding protein...

C436S501000

Reexamination Certificate

active

07049079

ABSTRACT:
Methods of measuring the presence/absence of a coupling factor 6, which is a subunit of H+-transporting ATP synthase→H+ATP synthase present in the mitochondrial inner membrane, in the blood and the concentration thereof are provided. Further, relations among the coupling factor 6 level in the blood and diseases and relations among the inhibition of the effect of the coupling factor and therapeutic effects on diseases are clarified and thus techniques for diagnosing and treating these diseases are provided.The present invention provides a vector containing a DNA encoding the coupling factor 6 or fragment thereof; a transformant transformed by this vector; and a method of producing the coupling factor 6 and its fragment. The present invention further provides an antibody reacting specifically with the coupling factor 6; a process of producing the antibody; and a method of assaying the coupling factor 6.

REFERENCES:
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Osani, T. et al. “Coupling factor is a novel endogenous inhibitory peptide . . . in endothelial Cells” CIRCULATION, vol. 98, No. 17, p. 1529, Oct. 27, 1998, XP009031815 Abstract.
Osanai et al., A novel inhibitory effect on prostacyclin synthesis of coupling factor 6 extracted from the heart of spontaneously hypertensive rats,J. Biol Chem, 1998, pp. 31778-31783.
Ando et al, Differential display and cloning of shear stress-responsive messenger RNAs in human endothelial cells, Biochem & Biophy Res Comm. 1996, pp. 347-351.
Evans et al, An import-competant precursor of small subunit of ribulose-1,5-bisphosphate carboxylase generated by factor Xa cleavage from a beta-glactosidase fusion expressed inEscherichia coli, Protein Expr Purif, 1992, pp. 178-184.

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