dc.contributor.author | Prockop, D. J. | en |
dc.contributor.author | Constantinou-Deltas, Constantinos D. | en |
dc.contributor.author | Dombrowski, K. E. | en |
dc.contributor.author | Hojima, Y. | en |
dc.contributor.author | Kadler, K. E. | en |
dc.contributor.author | Kuivaniemi, H. | en |
dc.contributor.author | Tromp, G. | en |
dc.contributor.author | Vogel, B. E. | en |
dc.creator | Prockop, D. J. | en |
dc.creator | Constantinou-Deltas, Constantinos D. | en |
dc.creator | Dombrowski, K. E. | en |
dc.creator | Hojima, Y. | en |
dc.creator | Kadler, K. E. | en |
dc.creator | Kuivaniemi, H. | en |
dc.creator | Tromp, G. | en |
dc.creator | Vogel, B. E. | en |
dc.date.accessioned | 2019-11-04T12:52:33Z | |
dc.date.available | 2019-11-04T12:52:33Z | |
dc.date.issued | 1989 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/53330 | |
dc.description.abstract | Recent data from several laboratories have established that most variants of osteogenesis imperfecta (OI) are caused by mutations in the 2 structural genes for type I procollagen. There are 2 general reasons for the large number of mutations in type I procollagen in OI. One reason is that most of the structure of the procollagen monomer is essential for normal biological function of the protein. The second reason is that most of the mutations cause synthesis of structurally altered proα chains of type I procollagen. The deleterious effects of the structurally altered proα chains are then amplified by at least 3 mechanisms. One mechanism is a phenomenon referred to as 'procollagen suicide' whereby altered proα chains cause degradation of normal proα chains synthesized by the same cell. Another mechanism involves the fact that many of the structurally altered proα chains prevent normal processing of the N-propeptides of procollagen and persistence of the N-propeptide interferes with normal fibril assembly. A third mechanism is a recently discovered phenomenon in which a substitution of a bulkier amino acid for glycine can cause a kink in the triple helix of the molecule. The kinked collagen, in turn, causes formation of abnormally branced fibrils. Because the deleterious effects of abnormal proα chains are amplified by these 3 mechanisms, most of the mutations are dominant and many are dominant lethal. The conclusion that most variants of OI are caused by mutations in the structural genes for type I procollagen has broad implications for other diseases that affect connective tissue, diseases such as chondrodystrophies, osteoarthritis, and osteoporosis. | en |
dc.source | American Journal of Medical Genetics | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024446845&partnerID=40&md5=8d97b964d1544b8653265f5ccb0ca322 | |
dc.subject | human | en |
dc.subject | priority journal | en |
dc.subject | review | en |
dc.subject | Base Sequence | en |
dc.subject | Molecular Sequence Data | en |
dc.subject | Mutation | en |
dc.subject | heredity | en |
dc.subject | connective tissue disease | en |
dc.subject | Connective Tissue Diseases | en |
dc.subject | Amino Acid Sequence | en |
dc.subject | osteogenesis imperfecta | en |
dc.subject | procollagen | en |
dc.subject | mutant | en |
dc.subject | procollagen type 1 | en |
dc.subject | collagen disease | en |
dc.title | Type I procollagen: The gene-protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissue | en |
dc.type | info:eu-repo/semantics/article | |
dc.description.volume | 34 | |
dc.description.startingpage | 60 | |
dc.description.endingpage | 67 | |
dc.author.faculty | Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Βιολογικών Επιστημών / Department of Biological Sciences | |
dc.type.uhtype | Article | en |
dc.description.notes | <p>Cited By :57</p> | en |
dc.source.abbreviation | Am.J.Med.Genet. | en |
dc.contributor.orcid | Constantinou-Deltas, Constantinos D. [0000-0001-5549-9169] | |
dc.gnosis.orcid | 0000-0001-5549-9169 | |