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Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta.
Hum Mutat. 2001 Oct; 18(4):319-26.HM

Abstract

Triple helix formation is a prerequisite for the passage of type I procollagen from the endoplasmic reticulum and secretion from the cell to form extracellular fibrils that will support mineral deposition in bone. Analysis of cDNA from 11 unrelated individuals with osteogenesis imperfecta (OI) revealed the presence of 11 novel, short in-frame deletions or duplications of three, nine, or 18 nucleotides in the helical coding regions of the COL1A1 and COL1A2 collagen genes. Triple helix formation was impaired, type I collagen alpha chains were post-translationally overmodified, and extracellular secretion was markedly reduced. With one exception, the obligate Gly-Xaa-Yaa repeat pattern of amino acids in the helical domains was not altered, but the Xaa- and Yaa position residues were out of register relative to the amino acid sequences of adjacent chains in the triple helix. Thus, the identity of these amino acids, in addition to third position glycines, is important for normal helix formation. These findings expand the known repertoire of uncommon in-frame deletions and duplications in OI, and provide insight into normal collagen biosynthesis and collagen triple helix formation.

Authors+Show Affiliations

Department of Pathology, University of Washington, Seattle, Washington, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

11668615

Citation

Pace, J M., et al. "Deletions and Duplications of Gly-Xaa-Yaa Triplet Repeats in the Triple Helical Domains of Type I Collagen Chains Disrupt Helix Formation and Result in Several Types of Osteogenesis Imperfecta." Human Mutation, vol. 18, no. 4, 2001, pp. 319-26.
Pace JM, Atkinson M, Willing MC, et al. Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta. Hum Mutat. 2001;18(4):319-26.
Pace, J. M., Atkinson, M., Willing, M. C., Wallis, G., & Byers, P. H. (2001). Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta. Human Mutation, 18(4), 319-26.
Pace JM, et al. Deletions and Duplications of Gly-Xaa-Yaa Triplet Repeats in the Triple Helical Domains of Type I Collagen Chains Disrupt Helix Formation and Result in Several Types of Osteogenesis Imperfecta. Hum Mutat. 2001;18(4):319-26. PubMed PMID: 11668615.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta. AU - Pace,J M, AU - Atkinson,M, AU - Willing,M C, AU - Wallis,G, AU - Byers,P H, PY - 2001/10/23/pubmed PY - 2002/1/23/medline PY - 2001/10/23/entrez SP - 319 EP - 26 JF - Human mutation JO - Hum Mutat VL - 18 IS - 4 N2 - Triple helix formation is a prerequisite for the passage of type I procollagen from the endoplasmic reticulum and secretion from the cell to form extracellular fibrils that will support mineral deposition in bone. Analysis of cDNA from 11 unrelated individuals with osteogenesis imperfecta (OI) revealed the presence of 11 novel, short in-frame deletions or duplications of three, nine, or 18 nucleotides in the helical coding regions of the COL1A1 and COL1A2 collagen genes. Triple helix formation was impaired, type I collagen alpha chains were post-translationally overmodified, and extracellular secretion was markedly reduced. With one exception, the obligate Gly-Xaa-Yaa repeat pattern of amino acids in the helical domains was not altered, but the Xaa- and Yaa position residues were out of register relative to the amino acid sequences of adjacent chains in the triple helix. Thus, the identity of these amino acids, in addition to third position glycines, is important for normal helix formation. These findings expand the known repertoire of uncommon in-frame deletions and duplications in OI, and provide insight into normal collagen biosynthesis and collagen triple helix formation. SN - 1098-1004 UR - https://www.unboundmedicine.com/medline/citation/11668615/Deletions_and_duplications_of_Gly_Xaa_Yaa_triplet_repeats_in_the_triple_helical_domains_of_type_I_collagen_chains_disrupt_helix_formation_and_result_in_several_types_of_osteogenesis_imperfecta_ L2 - https://doi.org/10.1002/humu.1193 DB - PRIME DP - Unbound Medicine ER -