Age-Related Changes in the Reducible Cross-Links of Human Dermis Collagen

Dermatology ◽  
1977 ◽  
Vol 155 (6) ◽  
pp. 335-339 ◽  
Author(s):  
D. Volpin ◽  
M.G. Giro ◽  
I. Castellani ◽  
A. Peserico
Keyword(s):  
Age Related ◽  
Human Dermis ◽  
Cross Links ◽  
Age Related Changes

scholarly journals Age-related changes in collagen synthesis and degradation in rat tissues. Importance of degradation of newly synthesized collagen in regulating collagen production

1991 ◽  
Vol 276 (2) ◽  
pp. 307-313 ◽  
Author(s):  
P K Mays ◽  
R J McAnulty ◽  
J S Campa ◽  
G J Laurent
Keyword(s):  
Skeletal Muscle ◽  
Collagen Synthesis ◽  
Rat Tissues ◽  
Age Related ◽  
Developmental Growth ◽  
Cross Links ◽  
Fractional Synthesis ◽  
Synthesis And Degradation ◽  
Age Related Changes

During developmental growth, collagens are believed to be continuously deposited into an extracellular matrix which is increasingly stabilized by the formation of covalent cross-links throughout life. However, the age-related changes in rates of synthetic and degradative processes are less well understood. In the present study we measured rates of collagen synthesis in vivo using a flooding dose of unlabelled proline given with [14C]proline and determining production of hydroxy[14C]proline. Degradation of newly synthesized collagen was estimated from the amount of free hydroxy [14C]proline in tissues 30 min after injection. Collagen fractional synthesis rates ranged from about 5%/day in skeletal muscle to 20%/day in hearts of rats aged 1 month. At 15 months of age, collagen fractional synthesis rates had decreased markedly in lung and skin, but in skeletal muscle and heart, rates were unchanged. At 24 months of age, synthesis rates had decreased by at least 10-fold in all tissues, compared with rates at 1 month. The proportion of newly synthesized collagen degraded ranged from 6.4 +/- 0.4% in skin to 61.6 +/- 5.0% in heart at 1 month of age. During aging the proportion degraded increased in all tissues to maximal values at 15 months, ranging from 56 +/- 7% in skin to 96 +/- 1% in heart. These data suggest that there are marked age-related changes in rates of collagen metabolism. They also indicate that synthesis is active even in old animals, where the bulk of collagens produced are destined to be degraded.

Age-related changes of blood vessels in the human dermis

2015 ◽  
Vol 5 (2) ◽  
pp. 65-71 ◽  
Author(s):  
A. G. Gunin ◽  
V. V. Petrov ◽  
O. V. Vasilieva ◽  
N. N. Golubtsova
Keyword(s):  
Blood Vessels ◽  
Age Related ◽  
Human Dermis ◽  
Age Related Changes

Age-related changes in mast cells and eosinophils of human dermis

2013 ◽  
Vol 44 (3) ◽  
pp. 139-143 ◽  
Author(s):  
V. V. Petrov ◽  
O. V. Vasilyeva ◽  
N. K. Kornilova ◽  
A. G. Gunin
Keyword(s):  
Mast Cells ◽  
Age Related ◽  
Human Dermis ◽  
Age Related Changes

scholarly journals Isotonic and Isometric Thermal Contraction of Human Dermis. II. Age-Related Changes*

1964 ◽  
Vol 43 (5) ◽  
pp. 341-348 ◽  
Author(s):  
Dee M. Rasmussen ◽  
Khalil G. Wakim ◽  
R.K. Winkelmann
Keyword(s):  
Thermal Contraction ◽  
Age Related ◽  
Human Dermis ◽  
Age Related Changes

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.

scholarly journals Age-Related Changes in Proliferation, the Numbers of Mast Cells, Eosinophils, and cd45-Positive Cells in Human Dermis

2010 ◽  
Vol 66A (4) ◽  
pp. 385-392 ◽  
Author(s):  
A. G. Gunin ◽  
N. K. Kornilova ◽  
O. V. Vasilieva ◽  
V. V. Petrov
Keyword(s):  
Mast Cells ◽  
Age Related ◽  
Human Dermis ◽  
Age Related Changes

Age-related changes in angiogenesis in human dermis

2014 ◽  
Vol 55 ◽  
pp. 143-151 ◽  
Author(s):  
Andrei G. Gunin ◽  
Vadim V. Petrov ◽  
Natalia N. Golubtzova ◽  
Olga V. Vasilieva ◽  
Natalia K. Kornilova
Keyword(s):  
Age Related ◽  
Human Dermis ◽  
Age Related Changes
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