scholarly journals p-Dimethylaminobenzaldehyde-reactive substances in tail tendon collagen of streptozotocin-diabetic rats: temporal relation to biomechanical properties and advanced glycation endproduct (AGE)-related fluorescence

2000 ◽  
Vol 1502 (3) ◽  
pp. 398-404 ◽  
Author(s):  
M Stefek ◽  
A Gajdosik ◽  
A Gajdosikova ◽  
L Krizanova
Keyword(s):  
Biomechanical Properties ◽  
Diabetic Rats ◽  
Temporal Relation ◽  
Advanced Glycation ◽  
Advanced Glycation Endproduct ◽  
Age Related ◽  
Streptozotocin Diabetic Rats ◽  
Tail Tendon ◽  
Tendon Collagen

Effect of green tea extract on advanced glycation and cross-linking of tail tendon collagen in streptozotocin induced diabetic rats

2008 ◽  
Vol 46 (1) ◽  
pp. 280-285 ◽  
Author(s):  
Pon Velayutham Anandh Babu ◽  
Kuruvimalai Ekambaram Sabitha ◽  
Chennam Srinivasulu Shyamaladevi
Keyword(s):  
Green Tea ◽  
Diabetic Rats ◽  
Green Tea Extract ◽  
Cross Linking ◽  
Advanced Glycation ◽  
Tail Tendon ◽  
Tea Extract ◽  
Tendon Collagen

A Novel Type of Advanced Glycation Endproduct Found in Diabetic Rats

2005 ◽  
pp. 434
Author(s):  
Toshihiko Osawa ◽  
Tomoko Oya ◽  
Harue Kumon ◽  
Yasujiro Morimitsu ◽  
Hiroyuki Kobayashi ◽  
...  
Keyword(s):  
Diabetic Rats ◽  
Advanced Glycation ◽  
Advanced Glycation Endproduct

scholarly journals Age-related changes in the physical properties, cross-linking, and glycation of collagen from mouse tail tendon

2020 ◽  
Vol 295 (31) ◽  
pp. 10562-10571 ◽  
Author(s):  
Melanie Stammers ◽  
Irina M. Ivanova ◽  
Izabella S. Niewczas ◽  
Anne Segonds-Pichon ◽  
Matthew Streeter ◽  
...  
Keyword(s):  
The Other ◽  
Cross Linking ◽  
Structural Protein ◽  
Cross Link ◽  
Age Related ◽  
Cross Links ◽  
Tail Tendon ◽  
Collagen Cross Linking ◽  
Age Related Changes ◽  
Tendon Collagen

Collagen is a structural protein whose internal cross-linking critically determines the properties and functions of connective tissue. Knowing how the cross-linking of collagen changes with age is key to understanding why the mechanical properties of tissues change over a lifetime. The current scientific consensus is that collagen cross-linking increases with age and that this increase leads to tendon stiffening. Here, we show that this view should be reconsidered. Using MS-based analyses, we demonstrated that during aging of healthy C57BL/6 mice, the overall levels of collagen cross-linking in tail tendon decreased with age. However, the levels of lysine glycation in collagen, which is not considered a cross-link, increased dramatically with age. We found that in 16-week-old diabetic db/db mice, glycation reaches levels similar to those observed in 98-week-old C57BL/6 mice, while the other cross-links typical of tendon collagen either decreased or remained the same as those observed in 20-week-old WT mice. These results, combined with findings from mechanical testing of tendons from these mice, indicate that overall collagen cross-linking in mouse tendon decreases with age. Our findings also reveal that lysine glycation appears to be an important factor that contributes to tendon stiffening with age and in diabetes.

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