Therapeutic medication for cartilage disorder

A cartilage and disease technology, applied in the field of pharmaceutical compositions for the prevention and/or treatment of cartilage diseases, can solve problems such as inability to cope with large defects, inability to naturally regenerate, and failure to establish a root therapy for traumatic articular cartilage defects.

Pending Publication Date: 2021-09-21
OSAKA UNIV +1
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0002] Cartilaginous tissue, such as articular cartilage, is not easily repaired and rarely regenerates naturally once damaged
For example, the treatment of traumatic articular cartilage defects is mainly symptomatic therapy (such as oral analgesics and intra-articular injection of hyaluronic acid), and so far no radical treatment for traumatic articular cartilage defects has been established.
In addition, surgical treatment methods (such as autologous osteochondral column transplantation) exist for traumatic articular cartilage defects, but there are problems such as inability to cope with large defects because the patient's normal tissue needs to be harvested

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
  • Therapeutic medication for cartilage disorder
  • Therapeutic medication for cartilage disorder
  • Therapeutic medication for cartilage disorder

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0072] Evaluation of the Efficacy of HMGB1 Fragment Peptides on Articular Cartilage Defects

[0073] (1) Materials and methods

[0074] i) Preparation of medicine

[0075] A peptide consisting of amino acid residues 1-44 (SEQ ID NO: 1) of human HMGB1 protein was chemically synthesized by solid phase method. Hereinafter, the HMGB1 fragment peptide is referred to as HMGB1 peptide (1-44), and in the figures corresponding to the examples, the peptide is simply indicated as "1-44".

[0076] ii) Generation of cartilage defect model mice

[0077] C57BL / 6J mice (6-7 weeks old, male, wild type) were purchased from CLEA Japan, Inc., and then adapted to the animal facility until reaching 8 weeks of age (about 25 g at 8 weeks of age). While mice were under 1.5-2.0% (v / v) isoflurane inhalation anesthesia, the lateral lower limbs were shaved to create cartilage defects, and a longitudinal skin incision of approximately 1 cm was applied with scissors in the middle of the knee joint . Th...

Embodiment 2

[0093] Histological staining of articular cartilage

[0094] method

[0095] Cartilage defect model mice were produced in the same manner as in Example 1 and continued to be bred. Tissue at the cartilage defect-generating site including the knee joint was removed from the mice at 12 weeks after the operation to produce paraffin sections, and the sections were subjected to immunostaining and safranin O staining with an anti-type II collagen antibody. In addition, cartilage tissues of knee joints were removed from normal mice of the same strain to produce paraffin sections, and type II collagen immunostaining and safranin O staining were performed on the sections in the same manner.

[0096] result

[0097] In the cartilage defect model mice, the tissue at the site of the cartilage defect in the knee joint at 12 weeks after operation (i.e., the tissue that was allowed to recover naturally after the cartilage defect was generated) was hardly shown in either safranin O staining ...

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 inventors of the present invention searched for a substance that is effective in treating a cartilage disorder, and as a result, found that, in an animal model of joint cartilage deficiency, an HMGB1 fragment peptide having a specific amino acid sequence exhibits the effect of reproducing a healthy cartilage tissue including a hyaline cartilage. Based on this finding, the present invention provides a pharmaceutical composition that contains the specific HMGB1 fragment peptide and that is for preventing and / or treating a cartilage disorder.

Description

technical field [0001] The present application relates to a pharmaceutical composition for preventing and / or treating cartilage disorders containing a fragment peptide of a high mobility group box 1 (HMGB1) protein. This application claims priority from Japanese Patent Application No. 2018-200866 filed on October 25, 2018, the entire contents of which are incorporated herein by reference. Background technique [0002] Cartilaginous tissue, such as articular cartilage, is not easily repaired, and once damaged it rarely regenerates naturally. For example, the treatment of traumatic articular cartilage defects is mainly symptomatic therapy (such as oral administration of analgesics and intra-articular injection of hyaluronic acid), and no radical treatment for traumatic articular cartilage defects has been established so far. In addition, there are surgical treatment methods for traumatic articular cartilage defects such as autologous osteochondral column transplantation, but ...

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(China)
IPC IPC(8): A61P19/00A61P19/02A61K38/16
CPCA61P19/02A61P19/00A61K38/1709C07K14/47A61K38/16
Inventor 玉井克人新保敬史佐佐木英嗣对马誉大山崎尊彦
Owner OSAKA UNIV
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