Search

Your search keyword '"collagen chaperones"' showing total 2 results
Start Over Descriptor "collagen chaperones"
2 results on '"collagen chaperones"'

1. Mutacje genów niekolagenowych we wrodzonej łamliwości kości - znaczenie produktów tych genów w biosyntezie kolagenu i patogenezie choroby.

Author

Galicka, Anna

Subjects
*OSTEOGENESIS imperfecta, *COLLAGEN genetics, *HYDROXYLATION, *MOLECULAR chaperones, *GENETIC transcription, *BONE growth
Abstract

Recent investigations revealed that the "brittle bone" phenotype in osteogenesis imperfecta (OI) is caused not only by dominant mutations in collagen type I genes, but also by recessively inherited mutations in genes responsible for the post-translational processing of type I procollagen as well as for bone formation. The phenotype of patients with mutations in noncollagen genes overlaps with very severe type III and lethal type II OI caused by mutations in collagen genes. Mutations in genes that encode proteins involved in collagen prolyl 3-hydroxylation (P3H1/CRTAP/CyPB) eliminated Pro986 hydroxylation and caused an increase in modification of collagen helix by prolyl 4-hydroxylase and lysyl hydroxylase. However, the importance of these disturbances in the disease pathomechanism is not known. Loss of complex proteins' function as collagen chaperones may dominate the disease mechanism. The latest findings added to the spectrum of OI-causing and collagen-influencing factors other chaperones (HSP47 and FKBP65) and protein BMP-1, which emphasizes the complexity of collagen folding and secretion as well as their importance in bone formation. Furthermore, mutations in genes encoding transcription factor SP7/Osterix and pigment epithelium-derived factor (PEDF) constitute a novel mechanism for OI, which is independent of changes in biosynthesis and processing of collagen. [ABSTRACT FROM AUTHOR]

Published
2012

2. [Mutations of noncollagen genes in osteogenesis imperfecta--implications of the gene products in collagen biosynthesis and pathogenesis of disease]

Author

Anna Galicka

Subjects
Microbiology (medical), pigment epithelium-derived factor, Lysyl hydroxylase, Procollagen-Proline Dioxygenase, lcsh:Medicine, Genes, Recessive, Biology, medicine.disease_cause, Bone morphogenetic protein 1, Collagen Type I, collagen 3-hydroxylation, Bone Morphogenetic Protein 1, Cyclophilins, Open Reading Frames, BMP-1, medicine, Humans, Nerve Growth Factors, Sp7 Transcription Factor, Eye Proteins, Gene, Serpins, Mutation, Extracellular Matrix Proteins, collagen chaperones, wrodzona łamliwość kości, lcsh:R, Proteins, Osteogenesis Imperfecta, mutations, medicine.disease, Molecular biology, Phenotype, Infectious Diseases, Osteogenesis imperfecta, transcription factor SP7, biology.protein, Procollagen-proline dioxygenase, Protein Processing, Post-Translational, Molecular Chaperones, Transcription Factors
Abstract

Recent investigations revealed that the “brittle bone” phenotype in osteogenesis imperfecta (OI) is caused not only by dominant mutations in collagen type I genes, but also by recessively inherited mutations in genes responsible for the post-translational processing of type I procollagen as well as for bone formation. The phenotype of patients with mutations in noncollagen genes overlaps with very severe type III and lethal type II OI caused by mutations in collagen genes. Mutations in genes that encode proteins involved in collagen prolyl 3-hydroxylation (P3H1/CRTAP/CyPB) eliminated Pro986 hydroxylation and caused an increase in modification of collagen helix by prolyl 4-hydroxylase and lysyl hydroxylase. However, the importance of these disturbances in the disease pathomechanism is not known. Loss of complex proteins’ function as collagen chaperones may dominate the disease mechanism. The latest findings added to the spectrum of OI-causing and collagen-influencing factors other chaperones (HSP47 and FKBP65) and protein BMP-1, which emphasizes the complexity of collagen folding and secretion as well as their importance in bone formation. Furthermore, mutations in genes encoding transcription factor SP7/Osterix and pigment epithelium-derived factor (PEDF) constitute a novel mechanism for OI, which is independent of changes in biosynthesis and processing of collagen.

Published
2012

Catalog

Books, media, physical & digital resources
See catalog results