Citations to this article

A substitution at a non-glycine position in the triple-helical domain of pro alpha 2(I) collagen chains present in an individual with a variant of the Marfan syndrome.
C L Phillips, … , S R Pinnell, R J Wenstrup
C L Phillips, … , S R Pinnell, R J Wenstrup
Published November 1, 1990
Citation Information: J Clin Invest. 1990;86(5):1723-1728. https://doi.org/10.1172/JCI114897.
View: Text | PDF
Research Article Article has an altmetric score of 3

A substitution at a non-glycine position in the triple-helical domain of pro alpha 2(I) collagen chains present in an individual with a variant of the Marfan syndrome.

Abstract

A substitution for a highly conserved non-glycine residue in the triple-helical domain of the pro alpha 2(I) collagen molecule was found in an individual with a variant of the Marfan syndrome. A single base change resulted in substitution of arginine618 by glutamine at the Y position of a Gly-X-Y repeat, and is responsible for the decreased migration in SDS-polyacrylamide gels of some pro alpha 2(I) chains of type I collagen synthesized by dermal fibroblasts from this individual. Family studies suggest that this substitution was inherited from the individual's father who also produces abnormally migrating pro alpha 2(I) collagen chains and shares some of the abnormal skeletal features. This single base change creates a new Bsu36 I (Sau I, Mst II) restriction site detectable in genomic DNA by Southern blot analysis when probed with a COL1A2 fragment. The analysis of 52 control individuals (103 chromosomes) was negative for the new Bsu36 I site, suggesting that the substitution is not a common polymorphism.

Authors

C L Phillips, A W Shrago-Howe, S R Pinnell, R J Wenstrup

×

Total citations by year

Year: 2020 2018 2016 2015 2012 2011 2008 2007 2004 2000 1998 1997 1994 1993 1992 1991 Total
Citations: 1 1 2 1 2 1 1 4 1 3 1 2 3 3 1 2 29
Citation information

Citations to this article (29)

Title and authors Publication Year
Comprehensive Genetic Analysis of 128 Candidate Genes in a Cohort With Idiopathic, Severe, or Familial Osteoporosis
MG Rocha-Braz, MM França, AM Fernandes, AM Lerario, EA Zanardo, LS de Santana, LD Kulikowski, RM Martin, BB Mendonca, B Ferraz-de-Souza 		Journal of the Endocrine Society 2020
Genetics of the extracellular matrix in aortic aneurysmal diseases
CJ Lin, CY Lin, NO Stitziel 		Matrix biology : journal of the International Society for Matrix Biology 2018
Targeted next-generation sequencing makes new molecular diagnoses and expands genotype–phenotype relationship in Ehlers–Danlos syndrome
RA Weerakkody, J Vandrovcova, C Kanonidou, M Mueller, P Gampawar, Y Ibrahim, P Norsworthy, J Biggs, A Abdullah, D Ross, HA Black, D Ferguson, NJ Cheshire, H Kazkaz, R Grahame, N Ghali, A Vandersteen, FM Pope, TJ Aitman 		Genetics in Medicine 2016
Identification of a p.Arg708Gln variant in COL1A2 in atypical femoral fractures
T Funck-Brentano, A Ostertag, F Debiais, P Fardellone, C Collet, E Mornet, M Cohen-Solal 		Joint Bone Spine 2016
Molecular diagnosis of hypophosphatasia and differential diagnosis by targeted Next Generation Sequencing
A Taillandier, C Domingues, CD Cazanove, V Porquet-Bordes, S Monnot, T Kiffer-Moreira, A Rothenbuhler, P Guggenbuhl, C Cormier, G Baujat, F Debiais, Y Capri, M Cohen-Solal, P Parent, J Chiesa, A Dieux, F Petit, J Roume, M Isnard, V Cormier-Daire, A Linglart, JL Millán, JP Salles, C Muti, B Simon-Bouy, E Mornet 		Molecular Genetics and Metabolism 2015
The effect of point mutations on structure and mechanical properties of collagen-like fibril: A molecular dynamics study
AE Marlowe, A Singh, YG Yingling 		Materials Science and Engineering: C 2012
Identification of a functional proprotein convertase cleavage site in microfibril-associated glycoprotein 2
LJ Donovan, SE Cha, AR Yale, S Dreikorn, A Miyamoto 		Matrix Biology 2012
Genotype-Phenotype Correlations in Autosomal Dominant Osteogenesis Imperfecta
IM Amor, FH Glorieux, F Rauch 		Journal of osteoporosis 2011
Collagen
P Fratzl 		2008
Y-position cysteine substitution in type I collagen (alpha1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype
WA Cabral, E Makareeva, AD Letocha, N Scribanu, A Fertala, A Steplewski, DR Keene, AV Persikov, S Leikin, JC Marini 		Human Mutation 2007
Three arginine to cysteine substitutions in the pro-alpha (I)-collagen chain cause Ehlers-Danlos syndrome with a propensity to arterial rupture in early adulthood
F Malfait, S Symoens, JD Backer, T Hermanns-Lê, N Sakalihasan, CM Lapière, P Coucke, AD Paepe 		Human Mutation 2007
Overexpression of the C-type natriuretic peptide (CNP) is associated with overgrowth and bone anomalies in an individual with balanced t(2;7) translocation
R Bocciardi, R Giorda, J Buttgereit, S Gimelli, MT Divizia, S Beri, S Garofalo, S Tavella, M Lerone, O Zuffardi, M Bader, R Ravazzolo, G Gimelli 		Human Mutation 2007
A novel arginine-to-cysteine substitution in the triple helical region of the α1(I) collagen chain in a family with an osteogenesis imperfecta/Ehlers-Danlos phenotype
AM Lund, F Joensen, E Christensen, M Dunø, F Skovby, M Schwartz 		Clinical Genetics 2007
Potential modifier role of the R618Q variant of proα2(I)collagen in type I collagen fibrillogenesis: in vitro assembly analysis
AN Vomund, SR Braddock, GF Krause, CL Phillips 		Molecular Genetics and Metabolism 2004
Variation in the Vitreous Phenotype of Stickler Syndrome Can Be Caused by Different Amino Acid Substitutions in the X Position of the Type II Collagen Gly-X-Y Triple Helix
AJ Richards, DM Baguley, JR Yates, C Lane, M Nicol, PS Harper, JD Scott, MP Snead 		The American Journal of Human Genetics 2000
Variation in the Vitreous Phenotype of Stickler Syndrome Can Be Caused by Different Amino Acid Substitutions in the X Position of the Type II Collagen Gly‐X‐Y Triple Helix
AJ Richards, DM Baguley, JR Yates, C Lane, M Nicol, PS Harper, JD Scott, MP Snead 		The American Journal of Human Genetics 2000
Gelenkpathologie
W Mohr 		2000
An α2(I) glycine to aspartate substitution is responsible for the presence of a kink in type I collagen in a lethal case of osteogenesis imperfecta
A Forlino, DR Keene, K Schmidt, JC Marini 		Matrix Biology 1998
Osteoporosis
DL Glaser, FS Kaplan 		Spine 1997
The human type I collagen mutation database
R Dalgleish 		Nucleic Acids Research 1997
Mutations in the alpha 2(IV) basement membrane collagen gene of Caenorhabditis elegans produce phenotypes of differing severities
MH Sibley, PL Graham, N Mende, JM Kramer 		The EMBO Journal 1994
Identification of type I collagen gene polymorphisms: Tolerance of sequence variation at an α2(I) Helix Y position
R Sztrolovics, MV der Rest, PJ Roughley 		Matrix Biology 1994
Mutation analysis of coding sequences for type I procollagen in individuals with low bone density
LD Spotila, A Colige, L Sereda, CD Constantinou-Deltas, MP Whyte, LB Riggs, JL Shaker, TD Spector, E Hume, N Olsen, M Attie, A Tenenhouse, E Shane, W Briney, DJ Prockop 		Journal of Bone and Mineral Research 1994
The Molecular Basis of Marfan Syndrome
CL Maslen, RW Glanville 		DNA and Cell Biology 1993
Mutations in the COL1A2 gene of type I collagen that result in nonlethal forms of osteogenesis imperfecta
RJ Wenstrup, LW Lever, CL Phillips, LD Quarles 		American Journal of Medical Genetics 1993
Collagens and their Abnormalities in a Wide Spectrum of Diseases
KI Kivirikko 		Annals of Medicine 1993
Elucidation of the gene defect in Marfan syndrome Success by two complementary research strategies
L Peltonen, K Kainulainen 		FEBS Letters 1992
Osteogenesis imperfecta due to recurrent point mutations at CpG dinucleotides in the COL1A1 gene of type I collagen
CJ Pruchno, DH Cohn, GA Wallis, MC Willing, BJ Starman, X Zhang, PH Byers 		Human Genetics 1991
The effects of different cysteine for glycine substitutions within alpha 2(I) chains. Evidence of distinct structural domains within the type I collagen triple helix
RJ Wenstrup, AW Shrago-Howe, LW Lever, CL Phillips, PH Byers, DH Cohn 		The Journal of biological chemistry 1991

Advertisement