High-affinity antagonists of ELR-CXC chemokines

a chemokine and high-affinity technology, applied in the field of cxc chemokine receptor antagonists, can solve the problem that no cxc chemokine antagonists are known in the prior art that are effectiv

Inactive Publication Date: 2007-01-25
UNIVERSITY OF SASKATCHEWAN
View PDF1 Cites 15 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0007] Compositions of the present invention include novel ELR-CXC chemokine agonist and antagonist proteins that are capable of binding to CXCR1 or CXCR2 receptors in mammalian cells. These include agonists and antagonists that are capable of high-affinity binding, wherein “high-affinity” refers to the agonist's or antagonist's affinity for the receptor being sufficient such that it can block the wild-type chemokine agonist under physiologically relevant concentrations. The novel antagonist proteins also include those that are substantially equivalent (th

Problems solved by technology

But, despite active research in the field, no CXC chemokine antagonists are known in the prior art that ar

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
  • High-affinity antagonists of ELR-CXC chemokines
  • High-affinity antagonists of ELR-CXC chemokines
  • High-affinity antagonists of ELR-CXC chemokines

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0069] (The following abbreviations are used throughout this disclosure: ARDS, acute respiratory distress syndrome; BALF, bronchoalveolar lavage fluid(s); BHR, Bolton-Hunter Reagent; CXCR1, CXCR2, CXCL8 receptors A, B, respectively; ELR, glutamic acid-lysine-arginine motif; CXCL1, growth-related oncogenealpha; CXCL4, platelet factor-4; CXCL5, epithelial-derived neutrophil activator-78; CXCL6, granulocyte chemotactic protein-2; CXCL8, interleukin-8; fMLP, formyl methionyl-leucylproline bacterial tripeptide; IPTG, isopropyl-thio-D-galactopyranoside; MIP-2, macrophage inflammatory protein-2; PMSF, phenylmethylsulfonyl fluoride; TMB, tetramethylbenzidine.)

[0070] As used herein, ‘an agonist’ refers to an agent that causes a cell to become activated.

[0071] As used herein, ‘an antagonist’ refers to an agent that prevents the cell from being activated in the presence or absence of the agonist.

[0072] As used herein, “purified” does not require absolute purity but is instead intended as a ...

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

The present invention provides novel polypeptide sequences, methods for production thereof and uses thereof for novel ELR—CXC chemokine receptor agonists and antagonists.

Description

CROSS REFERENCE TO RELATED APPLICATION [0001] This application is a continuation-in-part of U.S. patent application Ser. No. 10 / 087,273, filed Mar. 1, 2002 which claims the benefit of U.S. Provisional Patent Application No. 60 / 273,181, filed on Mar. 1, 2001.FIELD OF THE INVENTION [0002] The present invention relates to the field of CXC chemokine receptor antagonists. BACKGROUND OF THE INVENTION [0003] The CXC chemokines that possess the receptor-signaling glutamic acid-leucine-arginine (ELR) motif (e.g., CXCL1 / GRO□, CXCL8 / IL-8; Baggiolini, M. 1998. Nature. 392:565-568) are important to the influx of inflammatory cells that mediates much of the pathology in multiple settings, including ischemia-reperfusion injury (Sekido, N. et al. 1993. Nature. 365:654-657; Villard, J. et al. 1995. Am. J. Respir. Crit. Care Med. 152:1549-1554), endotoxemia-induced acute respiratory distress syndrome (ARDS; Mukaida, N. et al. 1998. Inflamm. Res. 47 suppl. 3):S151-157), arthritis, and immune complex-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): A61K38/19C07K14/52A61K38/00C12N15/09A61P9/10A61P11/00A61P13/12A61P15/14A61P43/00C07K1/22C07K14/47C07K14/54C07K19/00C12N1/15C12N1/19C12N1/21C12N5/10C12N7/00C12N15/12C12P21/02
CPCC07K14/5421A61P11/00A61P13/12A61P15/14A61P37/00A61P43/00A61P9/10
Inventor GORDON, JOHN R.LI, FANG
Owner UNIVERSITY OF SASKATCHEWAN
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

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap