Age Related Fibrosis Is Improved by Reducing Collagen Cross-Linking With Lysyl Oxidase Inhibition

2013 ◽  
Vol 29 (10) ◽  
pp. S247
Author(s):  
N. Rosin ◽  
M. Sopel ◽  
A. Falkenham ◽  
T. Myers ◽  
T.D. Lee ◽  
...  
Keyword(s):  
Lysyl Oxidase ◽  
Cross Linking ◽  
Age Related ◽  
Oxidase Inhibition ◽  
Collagen Cross Linking

scholarly journals Impact of Treatment on Myocardial Lysyl Oxidase Expression and Collagen Cross-Linking in Patients With Heart Failure

Hypertension ◽  
2009 ◽  
Vol 53 (2) ◽  
pp. 236-242 ◽  
Author(s):  
Begoña López ◽  
Ramón Querejeta ◽  
Arantxa González ◽  
Javier Beaumont ◽  
Mariano Larman ◽  
...  
Keyword(s):  
Heart Failure ◽  
Lysyl Oxidase ◽  
Cross Linking ◽  
Patients With Heart Failure ◽  
Collagen Cross Linking

Collagen cross-linking: Lysyl oxidase dependent synthesis of pyridinoline in vitro: Confirmation that pyridinoline is derived from collagen

1982 ◽  
Vol 108 (4) ◽  
pp. 1546-1550 ◽  
Author(s):  
Robert C. Siegel ◽  
Joseph C.C. Fu ◽  
Norihiko Uto ◽  
Kentaro Horiuchi ◽  
Daisaburo Fujimoto
Keyword(s):  
Lysyl Oxidase ◽  
Cross Linking ◽  
Collagen Cross Linking

scholarly journals The collagen cross‐linking enzyme lysyl oxidase is associated with the healing of human atherosclerotic lesions

2014 ◽  
Vol 276 (5) ◽  
pp. 525-536 ◽  
Author(s):  
O. A. Ovchinnikova ◽  
L. Folkersen ◽  
J. Persson ◽  
J. H. N. Lindeman ◽  
T. Ueland ◽  
...  
Keyword(s):  
Lysyl Oxidase ◽  
Cross Linking ◽  
Atherosclerotic Lesions ◽  
Collagen Cross Linking

scholarly journals Long-Term Exercise Training Attenuates Age-Related Diastolic Dysfunction: Association of Myocardial Collagen Cross-Linking

2009 ◽  
Vol 24 (1) ◽  
pp. 32 ◽  
Author(s):  
Su-Yeon Choi ◽  
Hyuk-Jae Chang ◽  
Sang-Il Choi ◽  
Kwang-Il Kim ◽  
Yong-Seok Cho ◽  
...  
Keyword(s):  
Exercise Training ◽  
Diastolic Dysfunction ◽  
Cross Linking ◽  
Age Related ◽  
Myocardial Collagen ◽  
Collagen Cross Linking

Effects of elevated circulating IGF-1 on the extracellular matrix in "high-growth" C57BL/6J mice

1996 ◽  
Vol 271 (3) ◽  
pp. R696-R703 ◽  
Author(s):  
K. Reiser ◽  
P. Summers ◽  
J. F. Medrano ◽  
R. Rucker ◽  
J. Last ◽  
...  
Keyword(s):  
Gene Expression ◽  
Granulation Tissue ◽  
Posttranslational Modifications ◽  
Lysyl Oxidase ◽  
High Growth ◽  
Cross Linking ◽  
Type I ◽  
Igf Binding Proteins ◽  
Lysyl Hydroxylase ◽  
Collagen Cross Linking

Collagen biosynthesis was analyzed in C57BL/6J mice homozygous for the high-growth locus. Plasma levels of insulin-like growth factor-1 (IGF-1) were significantly elevated in high-growth mice at all ages studied (3 wk-6 mo); IGF-binding proteins were also elevated. Skin biopsies were obtained from mice aged 3, 6, and 9 wk under halothane anesthesia. Mice were killed at 6 mo of age. Collagen, expressed per weight of tissue, was significantly increased in all tissues from high-growth mice, as was collagen cross-linking, expressed as moles of cross-link per mole of collagen. Expression of types I and III collagen, lysyl oxidase, and lysyl hydroxylase was increased in all tissues analyzed. There was a preferential increase in type III expression relative to type I expression. Rate and extent of accumulation of collagen in granulation tissue were measured in polyvinyl alcohol sponges implanted subcutaneously; collagen accumulation was significantly greater in the high-growth mice. These results suggest that 1) elevated circulating IGF-1 may increase collagen deposition both in normal tissue as well as in granulation tissue by increasing collagen gene expression, 2) IGF-1 may increase collagen cross-linking by stimulating expression of lysyl oxidase, and 3) the preferential increase in dihydroxylated cross-links observed in high-growth mice may be due to the stimulation of lysyl hydroxylase expression by IGF-1. In summary, elevated levels of IGF-1 appear to affect collagen both quantitatively and qualitatively, primarily through their effects on gene expression of collagen and of those enzymes responsible for posttranslational modifications of collagen.

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.

Sign in / Sign up

Export Citation Format

Share Document