scholarly journals Cyclophilin B control of lysine post-translational modifications of skin type I collagen

PLoS Genetics ◽  
2019 ◽  
Vol 15 (6) ◽  
pp. e1008196 ◽  
Author(s):  
Masahiko Terajima ◽  
Yuki Taga ◽  
Wayne A. Cabral ◽  
Ying Liu ◽  
Masako Nagasawa ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Skin Type ◽  
Type I ◽  
Post Translational Modifications ◽  
Cyclophilin B

Sub‐ and Supramolecular X‐Ray Characterization of Engineered Tissues from Equine Tendon, Bovine Dermis, and Fish Skin Type‐I Collagen

2020 ◽  
Vol 20 (5) ◽  
pp. 2000017 ◽  
Author(s):  
Alberta Terzi ◽  
Nunzia Gallo ◽  
Simona Bettini ◽  
Teresa Sibillano ◽  
Davide Altamura ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Skin Type ◽  
Type I ◽  
Fish Skin ◽  
X Ray ◽  
Engineered Tissues

scholarly journals Abnormal type I collagen metabolism by cultured fibroblasts in lethal perinatal osteogenesis imperfecta

1984 ◽  
Vol 217 (1) ◽  
pp. 103-115 ◽  
Author(s):  
J F Bateman ◽  
T Mascara ◽  
D Chan ◽  
W G Cole
Keyword(s):  
Osteogenesis Imperfecta ◽  
Cell Lines ◽  
Type I Collagen ◽  
The Other ◽  
Collagen Metabolism ◽  
Structural Defects ◽  
Collagen Molecule ◽  
Type I ◽  
Cultured Fibroblasts ◽  
Post Translational Modifications

Cultured skin fibroblasts from seven consecutive cases of lethal perinatal osteogenesis imperfecta (OI) expressed defects of type I collagen metabolism. The secretion of [14C]proline-labelled collagen by the OI cells was specifically reduced (51-79% of control), and collagen degradation was increased to twice that of control cells in five cases and increased by approx. 30% in the other two cases. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that four of the OI cell lines produced two forms of type I collagen consisting of both normally and slowly migrating forms of the alpha 1(I)- and alpha 2(I)-chains. In the other three OI cell lines only the ‘slow’ alpha (I)′- and alpha 2(I)′-chains were detected. In both groups inhibition of the post-translational modifications of proline and lysine resulted in the production of a single species of type I collagen with normal electrophoretic migration. Proline hydroxylation was normal, but the hydroxylysine contents of alpha 1(I)′- and alpha 2(I)′-chains purified by h.p.l.c. were greater than in control alpha-chains. The glucosylgalactosylhydroxylysine content was increased approx. 3-fold while the galactosylhydroxylysine content was only slightly increased in the alpha 1(I)′-chains relative to control alpha 1(I)-chains. Peptide mapping of the CNBr-cleavage peptides provided evidence that the increased post-translational modifications were distributed throughout the alpha 1(I)′- and alpha 2(I)′-chains. It is postulated that the greater modification of these chains was due to structural defects of the alpha-chains leading to delayed helix formation. The abnormal charge heterogeneity observed in the alpha 1 CB8 peptide of one patient may reflect such a structural defect in the type I collagen molecule.

scholarly journals Racemization and isomerization of type I collagen C-telopeptides in human bone and soft tissues: assessment of tissue turnover

2000 ◽  
Vol 345 (3) ◽  
pp. 481-485 ◽  
Author(s):  
Evelyne GINEYTS ◽  
Paul A. C. CLOOS ◽  
Olivier BOREL ◽  
Laurent GRIMAUD ◽  
Pierre D. DELMAS ◽  
...  
Keyword(s):  
Bone Resorption ◽  
Type I Collagen ◽  
Soft Tissues ◽  
Systematic Evaluation ◽  
Specific Marker ◽  
Type I ◽  
Aspartic Acid Residue ◽  
Post Translational Modifications ◽  
High Degree

Urinary excretion of the type I collagen C-telopeptide (CTx) has been shown to be a sensitive index of the rate of bone resorption. The human type I collagen sequence A1209HDGGR1214 of CTx can undergo racemization of the aspartic acid residue Asp1211 and isomerization of the bond between this residue and Gly1212. These spontaneous non-enzymic chemical reactions takes place in vivo in bone, and the degree of racemization and isomerization of CTx molecules may be an index of the biological age and the remodelling of bone. The aim of the present study was to investigate the degree of racemization and isomerization of type I collagen in human connective soft tissues, in order to estimate the rate of collagen turnover in adult tissues and compare it with that of bone. We also performed a systematic evaluation of the pyridinium cross-link content in adult human tissues. Using antibodies raised against the different CTx forms, we found that bone and dermis are the tissues that show most racemization and isomerization. The type I collagen of arteries, lung, intestine, kidney, skeletal muscle and heart shows significantly less racemization and isomerization than that of bone, suggesting that these soft tissues have a faster turnover than bone. We also found that pyridinoline and, to a lesser degree, deoxypyridinoline are distributed throughout the different tissues investigated. Because bone type I collagen is characterized by a high degree of both racemization/isomerization and deoxypyridinoline cross-linking, the concomitant assessment of these two post-translational modifications is likely to result in a highly specific marker of bone resorption.

scholarly journals Abnormal Type I Collagen Post-translational Modification and Crosslinking in a Cyclophilin B KO Mouse Model of Recessive Osteogenesis Imperfecta

PLoS Genetics ◽  
2014 ◽  
Vol 10 (6) ◽  
pp. e1004465 ◽  
Author(s):  
Wayne A. Cabral ◽  
Irina Perdivara ◽  
MaryAnn Weis ◽  
Masahiko Terajima ◽  
Angela R. Blissett ◽  
...  
Keyword(s):  
Mouse Model ◽  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Type I ◽  
Post Translational Modification ◽  
Cyclophilin B

scholarly journals Characterization of an .ALPHA.3 chain from carp skin type I collagen.

1990 ◽  
Vol 56 (9) ◽  
pp. 1509-1514 ◽  
Author(s):  
Yoshirou Miyauchi ◽  
Shigeru Kimura
Keyword(s):  
Type I Collagen ◽  
Skin Type ◽  
Type I

scholarly journals Molecular Characterization of Collagen Hydroxylysine O-Glycosylation by Mass Spectrometry: Current Status

2013 ◽  
Vol 66 (7) ◽  
pp. 760 ◽  
Author(s):  
Irina Perdivara ◽  
Mitsuo Yamauchi ◽  
Kenneth B. Tomer
Keyword(s):  
Mass Spectrometry ◽  
Type I Collagen ◽  
Molecular Mapping ◽  
Biological Significance ◽  
The Body ◽  
Current Status ◽  
Future Research ◽  
Type I ◽  
Post Translational Modifications

The most abundant proteins in vertebrates – the collagen family proteins – play structural and biological roles in the body. The predominant member, type I collagen, provides tissues and organs with structure and connectivity. This protein has several unique post-translational modifications that take place intra- and extra-cellularly. With growing evidence of the relevance of such post-translational modifications in health and disease, the biological significance of O-linked collagen glycosylation has recently drawn increased attention. However, several aspects of this unique modification – the requirement for prior lysyl hydroxylation as a substrate, involvement of at least two distinct glycosyl transferases, its involvement in intermolecular crosslinking – have made its molecular mapping and quantitative characterization challenging. Such characterization is obviously crucial for understanding its biological significance. Recent progress in mass spectrometry has provided an unprecedented opportunity for this type of analysis. This review summarizes recent advances in the area of O-glycosylation of fibrillar collagens and their characterization using state-of-the-art liquid chromatography–mass spectrometry-based methodologies, and perspectives on future research. The analytical characterization of collagen crosslinking and advanced glycation end-products are not addressed here.

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