Methods of reducing storage products using tripeptidyl...

Drug – bio-affecting and body treating compositions – Enzyme or coenzyme containing

Reexamination Certificate

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Details

C514S002600, C514S012200, C530S350000

Reexamination Certificate

active

07811559

ABSTRACT:
The present invention relates to a method for treating a patient having disorder characterized by a deficient amount of functional CLN2 protein in the affected cells, which comprises administering to the patient an amount of CLN2 protein effective to reduce or eliminate the symptoms caused by the deficiency in CLN2 protein.

REFERENCES:
patent: 6302685 (2001-10-01), Lobel et al.
patent: 6638712 (2003-10-01), Lobel et al.
Sondhi et al. (2001). Feasibility of gene therapy for late neuronal ceroid lipofuscinosis. Arch. Neurol. 58:1793-1798.
Ezaki, et al., A Lysosomal Proteinase, the Late Infantile Neuronal Ceroid Lipofuscinosis Gene (CLN2) Product, Is Essentiasl for Degradation of a Hydrophobic Protein, the Subunit c of ATP Synthase, Journal of Neurochemistry 1999, 72:2573-2582.
Brady & Barton, Enzyme Replacement Therapy for Gaucher disease: Critical Investigations beyond Demonstration of Clinical Efficacy, Biochemical Medicine and Metabolic Biology, 1994, 52:1-9.
Rider & Rider, Thirty Years of Batten Disease Research: Present Status and Future Goals, Molecular Genetics and Metabolism, 1999, 66:231-233.
Lin, et al., The Human CLN2 Protein/Tripeptidyl-Peptidate I is a Serine Protease thatAutoactivates at Acidic pH, Journal of Biological Chemistry, 2001, 276:2249-2255.
Lin & Lobel, Production and characterization of recombinant human CLN2 protein for enzyme-replacement therapy in late infantile neuronal ceroid lipofuscinosis, Biochem Journal, 2001, 357:49-55.
Zhong, et al., Two common mutations in the CLN2 gene underlie late infantile neuronal ceroid lipofuscinosis, Clinical Genetics, 1998, 54:234-238.
Hartikainen, et al.. Late Infantile Neuronal Ceroid Lipofuscinosis is Due to Splicing Mutations in the CLN2 Gene, Molecular Genetics and Metabolism, 1999, 67:162-168.
Schiffmann, et al., Infusion of α-galactosidase A reduces tissue globotriaosylceramide storage in patients with Fabry disease, PNAS, 2000, 97:365-370.
Chang et al.,Molecular Therapy, 16: 1-8 (2008).

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