Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Modulation of Cartilage Homeostasis By Active Domains of Cell Binding Extracellular Matrix Molecules

a cell binding extracellular matrix and active domain technology, applied in the direction of animals/human proteins, cyclic peptide ingredients, animals/human peptides, etc., can solve the problem of unfavorable side effects and the lik

Inactive Publication Date: 2007-09-27
HEINEGARD DICK +1
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Destruction of tissues is a feature of diseases affecting many organ types and represents an increasing problem to the population with particular emphasis on the aging.
However, many patients do not effectively respond to the above-mentioned treatments or the treatments lead to a number of undesired side-effects (see e.g. Smolen & Steiner, Nature Reviews, Vol. 2, (2003), 473-488)

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
  • Modulation of Cartilage Homeostasis By Active Domains of Cell Binding Extracellular Matrix Molecules
  • Modulation of Cartilage Homeostasis By Active Domains of Cell Binding Extracellular Matrix Molecules
  • Modulation of Cartilage Homeostasis By Active Domains of Cell Binding Extracellular Matrix Molecules

Examples

Experimental program
Comparison scheme
Effect test

examples

[0130] The following examples are intended to illustrate the invention without limiting it thereto.

[0131] To obtain evidence that chondroadherin-derived peptides modulate changes of the phenotype of cells involved in a disease associated with tissue changes, we have performed experiments with such cells (chondrocytes, synoviocytes), and in cartilage explants and an arthritis animal model.

[0132] Materials and Methods

Expression and Purification of Recombinant Protein

[0133] Human chondroadherin cDNA was ligated into the pQE8 vector (QIAGEN Inc. Valencia, Calif.) and expressed in M15 E. coli. Overnight cultures (8 ml) of stationary phase bacteria were used to inoculate 400 ml LB-medium (Luria-Bertani) and the cells were allowed to grow for 2.5 hour at 37° C. (OD600 of 0.7-0.9). Protein expression was induced by the addition of 2 mM IPTG (isopropyl-β-D-thiogalactopyranoside), (Sigma Chemicals CO., St Louis, Mo.) and the culture was grown for another 4.5 hour. Bacteria were then coll...

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

PropertyMeasurementUnit
pHaaaaaaaaaa
acceleration voltageaaaaaaaaaa
volumesaaaaaaaaaa
Login to View More

Abstract

A linear or cyclic peptide and the use of said peptide in medicine and especially in the manufacture of a medicament for the treatment and / or prophylaxis of a disease associated with inflammatory mediated cartilage destruction. The minimal core sequence of the linear or cyclic peptide is WLEAK. Alternatives are WLEAR and WLDAK.

Description

FIELD OF THE INVENTION [0001] The invention relates to a method for treatment and / or prophylaxis of a disease associated with tissue changes such as, e.g. an inflammatory joint disease such as, e.g., rheumatoid arthritis, psoriatic arthritis, juvenile chronic arthritis, systemic lupus erythematosus (SLE), infectious arthritis and juvenile idiopathic arthritis, other diseases involving joint structures such as, e.g., osteoarthritis, meniscal damage, gout, diseases affecting structural elements of the musculoskeletal system such as, e.g., tendon damage, ligament damage, and bone disease such as, e.g., osteoporosis, diseases affecting major arteries including atherosclerosis, vasculitis and trauma leading to injury, lung diseases including asthma and Chronic Obstructive Pulmonary Disease (COPD). The invention also relates to novel compounds for use in such a method and compositions, and in a preferred aspect the invention relates to novel peptide compounds with the core peptide sequenc...

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
Patent Type & Authority Applications(United States)
IPC IPC(8): A61K38/12A61K38/08A61K38/17C07K14/47C07K7/08C07K7/64C07K7/06A61P19/02A61K38/10A61K38/00C07K14/78
CPCC07K14/78A61K38/00A61P11/00A61P11/06A61P17/02A61P17/06A61P19/00A61P19/02A61P19/06A61P19/10A61P21/00A61P25/04A61P29/00A61P31/04A61P43/00A61P9/00A61P9/10
Inventor HEINEGARD, DICKCAMPER, LISBET AGNETA
Owner HEINEGARD DICK
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com