Corticotropin releasing factor 2 receptor agonists

A variant, X21 technology, applied in the field of corticotropin-releasing factor 2 receptor agonists, which can solve problems such as skeletal muscle atrophy

Inactive Publication Date: 2006-11-29
THE PROCTER & GAMBLE COMPANY
View PDF33 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Unfortunately, corticosteroid treatment also causes skeletal muscle atrophy, which neg

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Corticotropin releasing factor 2 receptor agonists

Examples

Experimental program
Comparison scheme
Effect test

preparation example Construction

[0132] In the preparation of peptides, recombinant DNA technology or cell lines expressing these peptides can also be used. These recombination methods are well known in the art. Methods of generating rDNA molecules are well known in the art, see Sambrook et al., Molecular Cloning-A Laboratory Manual, Cold Spring Harbor Laboratory Press (1989). In order to express the recombinant peptide of the present invention, an expression vector is prepared, which includes a nucleic acid encoding a related polypeptide under the control of one or more regulatory elements. The nucleic acid sequence encoding the peptide of the invention can be deduced from the peptide sequence described or claimed herein.

[0133] By methods well known in the art, the isolated nucleic acid molecules encoding related peptides can be ligated into a suitable expression vector. The host expression vector system that can be used for the purpose of the present invention includes, but is not limited to: microorganisms,...

Embodiment 1

[0195] Savagine and other non-selective CRFR agonists are generally not effective in treating CRF 2 R-modulated conditions, because these agonists also activate CRF 1 R, which leads to undesirable side effects.

[0196] Table 2 lists the human urocortin I (hUcnI), human urocortin II (hUroII), human urocortin III (hUroIII), and human adrenocorticotropic hormone called SEQ ID NOs: 2, 4, 6, 8, 10, and 11, respectively. Comparison of CRF binding of natural sequence fragments of release factor (hCRF), ovine corticotropin (oCRF) and savagine (Svg).

[0197] SEQ ID

Embodiment 2

[0199] Table 3 lists the comparative CRF combinations of different embodiments of the present invention.

[0200] SEQ ID NO

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

Isolated corticotropin releasing factor derivatives, and nucleic acids encoding the same, are effective for treating corticotropin releasing factor 2 receptor modulated disorders such as muscular dystrophy.

Description

[0001] This application is a divisional application of the patent application with the international application number PCT / US03 / 01461 and the national application number 03802370.9. Invention field [0002] The present invention relates to novel peptides and nucleic acids encoding the peptides in the treatment of CRF 2 Application in R-regulated disorders. Background of the invention [0003] CRFR and ligand [0004] So far, at least two corticotropin releasing factor (CRF) receptors (CRF) have been identified 1 R and CRF 2 R), they belong to the G-protein coupled receptor (GPCR) class. CRF 1 R or CRF 2 Agonist activation of R results in G of adenylate cyclase αs activation. Adenylate cyclase catalyzes the formation of cAMP, which in turn has multiple effects, including activation of protein kinase A, intracellular calcium release, and activation of mitogen-activated protein kinase (MAP kinase). In other studies, after the activation of the CRF receptor agonist, the increase in t...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
IPC IPC(8): C07K14/575A61K38/22A61P21/00C12N15/16C07K
Inventor R·J·艾斯福特W·A·马泽
Owner THE PROCTER & GAMBLE COMPANY
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products