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US 2006/0069024 A1Published application
Plant PR-5 proteins as mammalian therapeutic agents
AssigneePurdue Research Foundation
InventorsRay Bressan, Meena Narasimhan
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AssigneePurdue Research Foundation
InventorsRay Bressan, Meena Narasimhan
Estimating the term…
Proteins of the PR-5 family having a lectin-like β barrel domain control apoptosis in yeast through receptor binding. Receptors that specifically bind to PR-5 proteins having a lectin-like β barrel domain have been found to be homologous to mammalian adiponectin receptors, and such PR-5 proteins can act as functional homologues of adiponectin and control adiponectin response in mammals. PR-5 proteins having a lectin-like β barrel domain, for example osmotin, can be used in the treatment of conditions in mammals which are the result of activation or inhibition of adiponectin receptor-mediated metaboloic pathways. PR-5 proteins having a lectin-like β barrel domain, nucleic acids encoding such proteins, and receptors that specifically bind such proteins, can also be used in screening and rational design of new therapeutic agents for use in mammals.
A pharmaceutical composition comprising a PR-5 protein having a lectin-like β barrel domain.
A method for treating a mammal suffering from a disorder that is the result of activation or inhibition of a metabolic pathway mediated by adiponectin or an adiponectin-like protein, comprising administration of a PR-5 protein having a lectin-like β barrel domain.
Use of a PR-5 protein in the rational design of a therapeutic agent that is an agonist or an antagonist of all or part of the adiponectin targets in a mammalian cell.
Use of a nucleic acid sequence that encodes a PR-5 protein having a lectin-like β barrel domain in the rational design of a therapeutic agent that is an agonist or antagonist of all or part of the adiponectin targets in a mammalian cell.
Use of a receptor protein having specific binding affinity for a PR-5 protein having a lectin-like β barrel domain, as a primary screen to identify a therapeutic agent that is an agonist or an antagonist of all or part of the adiponectin targets in a mammalian cell.
Dependencies are inferred from the claim text.