Disulfide-Bridged Heterotrimeric Collagen Peptides Containing the Collagenase Cleavage Site of Collagen Type I. Synthesis and Conformational Properties

1999 ◽  
Vol 121 (4) ◽  
pp. 653-661 ◽  
Author(s):  
Johannes Ottl ◽  
Luis Moroder
Keyword(s):  
Cleavage Site ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Collagen Peptides ◽  
Conformational Properties

scholarly journals A critical crosslink region in human-bone-derived collagen type I. Specific cleavage site at residue Leu95

1990 ◽  
Vol 192 (1) ◽  
pp. 153-159 ◽  
Author(s):  
Boris BATGE ◽  
Holger NOTBOHM ◽  
Joachim DIEBOLD ◽  
Hartwig LEHMANN ◽  
Michael BODO ◽  
...  
Keyword(s):  
Cleavage Site ◽  
Collagen Type ◽  
Collagen Type I ◽  
Human Bone ◽  
Type I

scholarly journals AP Collagen Peptides Prevent Cortisol-Induced Decrease of Collagen Type I in Human Dermal Fibroblasts

2021 ◽  
Vol 22 (9) ◽  
pp. 4788
Author(s):  
Minjung Chae ◽  
Il-Hong Bae ◽  
Sung Hwan Lim ◽  
Kyoungmi Jung ◽  
Jonghwa Roh ◽  
...  
Keyword(s):  
Stress Responses ◽  
Collagen Type ◽  
Transforming Growth Factor ◽  
Collagen Type I ◽  
Dermal Fibroblasts ◽  
Type I ◽  
Human Dermal Fibroblasts ◽  
Collagen Peptides ◽  
Wide Range ◽  
Dependent Inhibition

Cortisol is an endogenous glucocorticoid (GC) and primary stress hormone that regulates a wide range of stress responses in humans. The adverse effects of cortisol on the skin have been extensively documented but the underlying mechanism of cortisol-induced signaling is still unclear. In the present study, we investigate the effect of cortisol on collagen type I expression and the effect of AP collagen peptides, collagen tripeptide-rich hydrolysates containing 3% glycine-proline- hydroxyproline (Gly-Pro-Hyp, GPH) from the fish skin, on the cortisol-mediated inhibition of collagen type I and the cortisol-induced signaling that regulates collagen type I production in human dermal fibroblasts (HDFs). We determine that cortisol downregulates the expression of collagen type I. AP collagen peptides or GC receptor (GR) inhibitors recover the cortisol-mediated inhibition of collagen type I and GR activation. AP collagen peptides or GR inhibitors also prevent the cortisol-dependent inhibition of transforming growth factor (TGF)-β signaling. AP collagen peptides or GR inhibitors are effective in the prevention of collagen type I inhibition mediated by cortisol in senescent HDFs and reconstituted human skin models. Taken together, GR signaling might be responsible for the cortisol-mediated inhibition of TGF-β. AP collagen peptides act as GR-mediated signaling blockers, preventing the cortisol-dependent inhibition of collagen type I. Therefore, AP collagen peptides have the potential to improve skin health.

scholarly journals Relative rates of biosynthesis of collagen type I, type V and type VI in calf cornea

1991 ◽  
Vol 274 (2) ◽  
pp. 615-617 ◽  
Author(s):  
P Kern ◽  
M Menasche ◽  
L Robert
Keyword(s):  
Type I Collagen ◽  
Collagen Type ◽  
Corneal Stroma ◽  
Collagen Type I ◽  
Type I ◽  
Type Vi Collagen ◽  
Sds Page ◽  
Proline Incorporation ◽  
Type V

The biosynthesis of type I, type V and type VI collagens was studied by incubation of calf corneas in vitro with [3H]proline as a marker. Pepsin-solubilized collagen types were isolated by salt fractionation and quantified by SDS/PAGE. Expressed as proportions of the total hydroxyproline solubilized, corneal stroma comprised 75% type I, 8% type V and 17% type VI collagen. The rates of [3H]proline incorporation, linear up to 24 h for each collagen type, were highest for type VI collagen and lowest for type I collagen. From pulse-chase experiments, the calculated apparent half-lives for types I, V and VI collagens were 36 h, 10 h and 6 h respectively.

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