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

Marker for diabetic complications

A technology for complications and diabetes, which is applied in the field of markers for diabetic complications, and can solve problems such as changes in uninvestigated quantities

Pending Publication Date: 2020-09-04
TOKAI UNIV +1
View PDF5 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0007] On the other hand, Glucoselysine (Glucoselysine) has a known structure, but the change of the amount under the condition has not been investigated

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
  • Marker for diabetic complications
  • Marker for diabetic complications
  • Marker for diabetic complications

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0078] (Detection of Glucose Lysine in Organisms (Rats) by LC-MS / MS)

[0079] Substances with increased accumulation in the lens of diabetic-induced rats were isolated and analyzed by LC-MS / MS (the results are shown in figure 1 )and 1 As a result of the identification of the structure by H-NMR, the structure of glucose lysine having the following structure and physical properties was found.

[0080]

[0081] 2-Amino-6-((2,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)amino)hexanoic acid

[0082] Chemical formula: C 12 H 24 N 2 O 7

[0083] Exact Mass: 308.16

[0084] Molecular weight: 308.33

[0085] m / z: 308.16 (100.0%), 309.16 (14.3%), 310.16 (1.5%)

[0086] Elemental analysis: C, 46.75; H, 7.85; N, 9.09; O, 36.32

[0087] Analysis of glucose lysine in organisms by LC-MS / MS.

[0088] That is, 1 mL of 6N iron-free hydrochloric acid was added to 200 μg of each of the lens fragmentation solutions of healthy rats and diabetic model rats (N=5), and the mixt...

Embodiment 2

[0094] (Detection of Glucose Lysine in Organisms (Rats) by Antibody)

[0095] Using an antibody recognizing glucose lysine and a CML antibody (anti-CML antibody clone 6D12, COSMO BIO), the content of glucose lysine and CML in the lenses of healthy rats and diabetic model rats (N=5) were measured .

[0096] show the result in image 3 . For CML, no significant differences were observed in the amounts in the lens of healthy and diabetic model rats. On the other hand, with regard to glucose lysine, a significant difference was observed for the amount in the lens of healthy rats and diabetic model rats.

[0097] It is clear that glucose lysine is significantly increased in the development of diabetes and its complications in the assay using a biological sample.

Embodiment 3

[0099] (Detection of Glucose Lysine in Organisms (Mouse) by LC-MS / MS)

[0100] For healthy mice (N=12) and diabetic model mice (N=20), based on the method of Example 1, glucose lysine in the lens was detected.

[0101] show the result in Figure 4 . As far as the elution position is concerned, glucose lysine and internal standard are all around 14min ( Figure 4 of A). It was shown that glucose lysine in the lens of diabetic model mice was significantly increased compared to healthy mice ( Figure 4 of B).

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 addresses the problem of providing a marker with which diabetic complications can be examined. Provided is a marker for examining diabetic complications which comprises a compound represented by formula (1), or a salt thereof.

Description

technical field [0001] The present invention relates to a marker for diabetic complications, a method for examining diabetic complications using the marker as an index, and the like. Background technique [0002] It is known that the bioaccumulation amount of AGEs (Advanced Glycation End-products), which are various advanced glycation end products produced by the reaction of proteins and reducing sugars, increases especially in lifestyle diseases (Non-Patent Document 1). [0003] Among them, N ε (carboxymethyl)lysine (carboxymethyllysine; CML) has been reported as a major antigenic AGEs structure derived from glucose, and since it is easy to measure, it has attracted attention as a target for drug development since the 1990s (Non-Patent Document 2). ). [0004] In this way, the structures of various AGEs including CML have been determined by using AGEs-specific monoclonal antibodies (Non-Patent Document 3) or liquid chromatography triple quadrupole mass spectrometry (LC-MS...

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): G01N33/66
CPCG01N33/66G01N33/6848G01N33/6893G01N2800/042G01N2800/56G01N2400/02G01N33/6812
Inventor 永井竜児谷口直之
Owner TOKAI UNIV
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