University of Virginia Patent Foundation

American Cyanamid Company

Lumos Pharma, Inc.

Other

Ammonett Pharma, LLC

Ferring Laboratories, Inc.

Michael Oliver Thorner

Bruce D Gaylinn

John R Zysk

Kevin R Lynch

Jeffrey K Harrison

William R Baumbach

Cecil Mark Eppler

Steve Harvey

Bruce David Gaylinn

Reiko Horikawa

Charles E Lyons, Jr

Andrew Alan Toogood

Daniel M Linkie

Described herein is a new oral method for using MK-0677 for detecting growth hormone (GH) deficiency (GHD). Also described is a method of treating growth hormone (GH) deficiency (GHD) in children with a functional hypothalamic-pituitary GH axis.

Detecting and treating growth hormone deficiency

The present invention relates to methods for treating sarcopenia with a growth hormone secretagogue.

Methods for treating sarcopenia with a growth hormone secretagogue

The present invention relates to chicken growth hormone releasing hormone (GHRH), its corresponding receptor, and nucleic acid sequences encoding these proteins. More particularly the present invention is directed to the use of the chicken GHRH hormone and its corresponding GHRH receptor to enhance the production of larger, leaner chickens and other avian species used for meat production.

Chicken growth hormone releasing hormone receptor

Growth hormone releasing hormone (GHRH) receptor binding has been characterized using a unique binding assay utilizing iodinated GHRH probes. Photoaffinity GHRH probes have been constructed which allow for photolabeling and characterization of the receptor. In addition, high affinity biotinylated GHRH analogs have been constructed. Solubilization of GHRH-R/GHRH complexes and extraction of specifically bound GHRH using a mild detergent solution, followed by affinity chromotography, leads to a substantially purified GHRH-R isolate. Electrophoretic treatment of the GHRH-R isolate produces GHRH-R of sufficient purity to conduct sequencing of the receptor.

Isolation and characterization of the growth hormone releasing hormone

Growth hormone releasing hormone (GHRH) receptor binding has been characterized using a unique binding assay utilizing iodinated GHRH probes. Photoaffinity GHRH probes have been constructed which allow for photolabeling and characterization of the receptor. In addition, high affinity biotinylated GHRH analogs have been constructed. Solubilization of GHRH-R/GHRH complexes and extraction of specifically bound GHRH using a mild detergent solution, followed by affinity chromatography, leads to a substantially purified GHRH-R isolate. Electrophoretic treatment of the GHRH-R isolate produces GHRH-R of sufficient purity to conduct sequencing of the receptor. Cloning of a gene encoding for polypeptides (protein or fragments thereof) having GHRH-R activity is accomplished using a bacterial host, and the cloned gene is expressed in a mammalian cell line. In addition, molecular cloning of the ovine GHRH-R is provided.

Molecular cloning of the ovine pituitary growth hormone releasing

Growth hormone releasing hormone (GHRH) receptor binding has been characterized using a unique binding assay utilizing iodinated GHRH probes. Photoaffinity GHRH probes have been constructed which allow for photolabeling and characterization of the receptor. In addition, high affinity biotinylated GHRH analogs have been constructed. Solubilization of GHRH-R/GHRH complexes and extraction of specifically bound GHRH using a mild detergent solution, followed by affinity chromatography, leads to a substantially purified GHRH-R isolate. Electrophoretic treatment of the GHRH-R isolate produces GHRH-R of sufficient purity to conduct sequencing of the receptor. Cloning of a gene encoding for polypeptides (protein or fragments thereof) having GHRH-R activity is accomplished using a bacterial host, and the cloned gene is expressed in a mammalian cell line.

Cloning of a gene encoding for the growth hormone releasing hormone

Growth hormone releasing hormone (GHRH) receptor binding has been characterized using a unique binding assay utilizing iodinated GHRH probes. Photoaffinity GHRH probes have been constructed which allow for photolabeling and characterization of the receptor. In addition, high affinity biotinylated GHRH analogs have been constructed. Solubilization of GHRH-R/GHRH complexes and extraction of specifically bound GHRH using a mild detergent solution, followed by affinity chromotography, leads to a substantially purified GHRH-R isolate. Electrophoretic treatment of the GHRH-R isolate produces GHRH-R of sufficient purity to conduct sequencing of the receptor. Cloning of a gene encoding for polypeptides (protein or fragments thereof) having GHRH-R activity is accomplished using a bacterial host, and the cloned gene is expressed in a mammalian cell line.

Nucleic acid encoding the growth hormone releasing hormone receptor

Nucleic acid molecule encoding the porcine growth hormone receptor

A method for increasing growth hormone secretion or inducing the biologic effects of growth hormone by continuous administration of growth hormone releasing factor or analog thereof is disclosed.

Method for increasing growth hormone secretion

A method and apparatus for therapeutically effective treatment of a living animal comprising administering a dynamic dosage of growth hormone releasing factor or analog thereof, or administering growth hormone or analogs thereof in a chronic course of treatment in a subdesensitizing regimen. Also a method of diagnosing living animals with an anterior pituitary unresponsive to growth hormone releasing factor or analogs thereof. A method of determining the optimum GRF and GH dynamic dosage for a given living animal, particularly a human.

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Charlottesville, VA, United States of America

Michael Oliver Thorner