scholarly journals Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase.

1991 ◽  
Vol 266 (2) ◽  
pp. 1299-1303 ◽  
Author(s):  
B Steinmann ◽  
P Bruckner ◽  
A Superti-Furga
Keyword(s):  
Cyclosporin A ◽  
Triple Helix ◽  
Indirect Evidence ◽  
Collagen Triple Helix ◽  
Helix Formation ◽  
Triple Helix Formation ◽  
Physiologic Role

Elucidating pH-Dependent Collagen Triple Helix Formation through Interstrand Hydroxyproline-Glutamic Acid Interactions

ChemBioChem ◽  
2014 ◽  
Vol 16 (3) ◽  
pp. 407-410 ◽  
Author(s):  
Liwei Chen ◽  
Shuting Cai ◽  
Jaehong Lim ◽  
Su Seong Lee ◽  
Song-Gil Lee
Keyword(s):  
Glutamic Acid ◽  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Formation ◽  
Triple Helix Formation ◽  
Ph Dependent

scholarly journals Collagen Triple Helix Formation Can Be Nucleated at Either End

2003 ◽  
Vol 278 (10) ◽  
pp. 7747-7750 ◽  
Author(s):  
Sabine Frank ◽  
Sergei Boudko ◽  
Kazunori Mizuno ◽  
Therese Schulthess ◽  
Jürgen Engel ◽  
...  
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Formation ◽  
Triple Helix Formation

Investigation of pH-Dependent Collagen Triple-Helix Formation

2008 ◽  
Vol 47 (44) ◽  
pp. 8429-8432 ◽  
Author(s):  
Song-Gil Lee ◽  
Jee Yeon Lee ◽  
Jean Chmielewski
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Formation ◽  
Triple Helix Formation ◽  
Ph Dependent

Investigation of pH-Dependent Collagen Triple-Helix Formation

2008 ◽  
Vol 120 (44) ◽  
pp. 8557-8560 ◽  
Author(s):  
Song-Gil Lee ◽  
Jee Yeon Lee ◽  
Jean Chmielewski
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Formation ◽  
Triple Helix Formation ◽  
Ph Dependent

scholarly journals Further studies on the effect of the collagen triple-helix formation on the hydroxylation of lysine and the glycosylations of hydroxylysine in chick-embryo tendon and cartilage cells

1977 ◽  
Vol 166 (3) ◽  
pp. 357-362 ◽  
Author(s):  
Aarne Oikarinen ◽  
Henrik Anttinen ◽  
Kari I. Kivirikko
Keyword(s):  
Chick Embryo ◽  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Formation ◽  
Tendon Cells ◽  
Triple Helix Formation ◽  
Lysine Residues ◽  
Cartilage Cells ◽  
Helical Molecules ◽  
And Cartilage

The hydroxylation of lysine and glycosylations of hydroxylysine were studied in isolated chick-embryo tendon and cartilage cells under conditions in which collagen triple-helix formation was either inhibited or accelerated. The former situation was obtained by incubating the tendon cells with 0.6mm-dithiothreitol, thus decreasing their proline hydroxylase activity by about 99%. After labelling with [14C]proline, the formation of hydroxy[14C]proline was found to have declined by about 95%. Since the hydroxylation of a relatively large number of proline residues is required for triple-helix formation at 37°C, the pro-α-chains synthesized under these conditions apparently cannot form triple-helical molecules. Labelling experiments with [14C]lysine indicated that the degree of hydroxylation of the lysine residues in the collagen synthesized was slightly increased and the degree of the glycosylations of the hydroxylysine residues more than doubled, the largest increase being in the content of glucosylgalactosylhydroxylysine. Recovery of chick-embryo cartilage cells from temporary anoxia was used to obtain accelerated triple-helix formation. A marked decrease was found in the extent of hydroxylation of the lysine residues in the collagen synthesized under these conditions, and an even larger decrease occurred in the glycosylations of the hydroxylysine residues. The results support the previous suggestion that the triple-helix formation of the pro-α-chains prevents further hydroxylation of lysine residues and glycosylations of hydroxylysine residues during collagen biosynthesis.

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