In Silico Analysis of Collagens Missense SNPs and Human Abnormalities.
Collagens
Extra cellular matrix
In silico
Missense SNPs
Journal
Biochemical genetics
ISSN: 1573-4927
Titre abrégé: Biochem Genet
Pays: United States
ID NLM: 0126611
Informations de publication
Date de publication:
Oct 2022
Oct 2022
Historique:
received:
15
07
2021
accepted:
06
12
2021
pubmed:
24
1
2022
medline:
16
9
2022
entrez:
23
1
2022
Statut:
ppublish
Résumé
Collagens are the most abundant proteins in the extra cellular matrix/ECM of human tissues that are encoded by different genes. There are single nucleotide polymorphisms/SNPs which are considered as the most useful biomarkers for some disease diagnosis or prognosis. The aim of this study is screening and identifying the functional missense SNPs of human ECM-collagens and investigating their correlation with human abnormalities. All of the missense SNPs were retrieved from the NCBI SNP database and screened for a global frequency of more than 0.1. Seventy missense SNPs that met the screening criteria were characterized for functional and stability impact using six and three protein analysis tools, respectively. Next, HOPE and geneMANIA analysis tools were used to show the effect of SNPs on three-dimensional structure (3D) and physical interaction of proteins. Results showed that 13 missense SNPs (rs2070739, rs28381984, rs13424243, rs1800517, rs73868680, rs12488457, rs1353613, rs59021909, rs9830253, rs2228547, rs3753841, rs2855430, and rs970547), which are in nine different collagen genes, affect the structure and function of different collagen proteins. Among these polymorphisms, COL4A3-rs13424243 and COL6A6-rs59021909 were predicted as the most effective ones. On the other hand, designed mutated and native 3D of rs13424243 variant illustrated that it can disturb the protein motifs. Also, geneMANIA predicted that COL4A3 and COL6A6 are interacting with some proteins including: DDR1, COL6A1, COL11A2 and so on. Based on our findings, ECM-collagens functional SNPs are important and may be considered as a risk factor or molecular marker for human disorders in the future studies.
Identifiants
pubmed: 35066702
doi: 10.1007/s10528-021-10172-6
pii: 10.1007/s10528-021-10172-6
doi:
Substances chimiques
Collagen
9007-34-5
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1630-1656Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Adzhubei I, Jordan DM, Sunyaev SR (2013) Predicting functional effect of human missense mutations using PolyPhen-2. Curr Protoc Hum Genet 76(1):7–20
Bächinger HP, Mizuno K, Vranka JA, Boudko SP (2010) Collagen formation and structure. Comprehensive natural products II: chemistry and biology. Elsevier Ltd, Amsterdam
Baumert P, G-REX Consortium, Stewart CE, Lake MJ, Drust B, Erskine RM (2018) Variations of collagen-encoding genes are associated with exercise-induced muscle damage. Physiol Genomics 50(9):691–693
pubmed: 29799806
pmcid: 6172608
doi: 10.1152/physiolgenomics.00145.2017
Biswas S, Munier FL, Yardley J, Hart-Holden N, Perveen R, Cousin P, Sutphin JE, Noble B, Batterbury M, Kielty C, Hackett A (2001) Missense mutations in COL8A2, the gene encoding the α2 chain of type VIII collagen, cause two forms of corneal endothelial dystrophy. Hum Mol Genet 10(21):2415–2423
pubmed: 11689488
doi: 10.1093/hmg/10.21.2415
Boffa JJ, Tharaux PL, Placier S, Ardaillou R, Dussaule JC, Chatziantoniou C (1999) Angiotensin II activates collagen type I gene in the renal vasculature of transgenic mice during inhibition of nitric oxide synthesis: evidence for an endothelin-mediated mechanism. Circulation 100(18):1901–1908
pubmed: 10545435
doi: 10.1161/01.CIR.100.18.1901
Capriotti E, Fariselli P, Casadio R (2005) I-Mutant2. 0: predicting stability changes upon mutation from the protein sequence or structure. Nucleic Acids Res 33(suppl-2):W306–W310
pubmed: 15980478
pmcid: 1160136
doi: 10.1093/nar/gki375
Capriotti E, Calabrese R, Casadio R (2006) Predicting the insurgence of human genetic diseases associated to single point protein mutations with support vector machines and evolutionary information. Bioinformatics 22(22):2729–2734
pubmed: 16895930
doi: 10.1093/bioinformatics/btl423
Capriotti E, Calabrese R, Fariselli P, Martelli PL, Altman RB, Casadio R (2013) WS-SNPs&GO: a web server for predicting the deleterious effect of human protein variants using functional annotation. BMC Genomics 14(3):1–7
Cescon M, Gattazzo F, Chen P, Bonaldo P (2015) Collagen VI at a glance. J Cell Sci 128(19):3525–3531
pubmed: 26377767
Chen CW, Lin J, Chu YW (2013) iStable: off-the-shelf predictor integration for predicting protein stability changes. BMC Bioinform 14(Suppl 2):S5
Cheng J, Randall A, Baldi P (2006) Prediction of protein stability changes for single-site mutations using support vector machines. Proteins 62(4):1125–1132
pubmed: 16372356
doi: 10.1002/prot.20810
Chiquet M, Birk DE, Bönnemann CG, Koch M (2014) Collagen XII: protecting bone and muscle integrity by organizing collagen fibrils. Int J Biochem Cell Biol 53:51–54
pubmed: 24801612
pmcid: 4119597
doi: 10.1016/j.biocel.2014.04.020
Choi Y, Chan AP (2015) PROVEAN web server: a tool to predict the functional effect of amino acid substitutions and indels. Bioinformatics 31(16):2745–2747
pubmed: 25851949
pmcid: 4528627
doi: 10.1093/bioinformatics/btv195
Chung HJ, Uitto J (2010) Type VII collagen: the anchoring fibril protein at fault in dystrophic epidermolysis bullosa. Dermatol Clin 28(1):93–105
pubmed: 19945621
pmcid: 2791403
doi: 10.1016/j.det.2009.10.011
David Ho KW, Wallace MR, Sibille KT, Bartley EJ, Cruz-Almeida Y, Glover TL, King CD, Goodin BR, Addison A, Edberg JC, Herbert MS (2017) Single nucleotide polymorphism in the COL11A2 gene associated with lowered heat pain sensitivity in knee osteoarthritis. Mol Pain. https://doi.org/10.1177/1744806917724259
doi: 10.1177/1744806917724259
pmcid: 5562334
Di Lullo GA, Sweeney SM, Korkko J, Ala-Kokko L, San Antonio JD (2002) Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J Biol Chem 277(6):4223–4231
pubmed: 11704682
doi: 10.1074/jbc.M110709200
Dorison A, Dussaule JC, Chatziantoniou C (2017) The role of discoidin domain receptor 1 in inflammation, fibrosis and renal disease. Nephron 137(3):212–220
pubmed: 28743124
doi: 10.1159/000479119
Duan Y, Liu G, Sun Y, Wu J, Xiong Z, Jin T, Chen M (2020) Collagen type VI α5 gene variations may predict the risk of lung cancer development in Chinese Han population. Sci Rep 10(1):1–9
doi: 10.1038/s41598-020-61614-x
Flamant M, Placier S, Rodenas A, Curat CA, Vogel WF, Chatziantoniou C, Dussaule JC (2006) Discoidin domain receptor 1 null mice are protected against hypertension-induced renal disease. J Am Soc Nephrol 17(12):3374–3381
pubmed: 17093065
doi: 10.1681/ASN.2006060677
Franz M, Rodriguez H, Lopes C, Zuberi K, Montojo J, Bader GD, Morris Q (2018) GeneMANIA update 2018. Nucleic Acids Res 46(W1):W60–W64
pubmed: 29912392
pmcid: 6030815
doi: 10.1093/nar/gky311
Fratzl P (2008) Collagen: structure and mechanics. Springer Science & Business Media, Boston
doi: 10.1007/978-0-387-73906-9
Gelse K, Pöschl E, Aigner T (2003) Collagens-structure, function, and biosynthesis. Adv Drug Deliv Rev 55(12):1531–1546
pubmed: 14623400
doi: 10.1016/j.addr.2003.08.002
Gerecke DR, Meng X, Liu B, Birk DE (2003) Complete primary structure and genomic organization of the mouse Col14a1 gene. Matrix Biol 22(3):209–216
pubmed: 12853031
doi: 10.1016/S0945-053X(03)00021-0
Gowen LC, Petersen DN, Mansolf AL, Qi H, Stock JL, Tkalcevic GT, Simmons HA, Crawford DT, Chidsey-Frink KL, Ke HZ, McNeish JD (2003) Targeted disruption of the osteoblast/osteocyte factor 45 gene (OF45) results in increased bone formation and bone mass. J Biol Chem 278(3):1998–2007
pubmed: 12421822
doi: 10.1074/jbc.M203250200
Gudmann NS, Karsdal MA (2016) Type X collagen. Biochemistry of collagens, laminins and elastin. Academic Press, Cambridge, pp 73–76
doi: 10.1016/B978-0-12-809847-9.00010-6
Heo WI, Park KY, Jin T, Lee MK, Kim M, Choi EH, Kim HS, Bae JM, Moon NJ, Seo SJ (2017) Identification of novel candidate variants including COL6A6 polymorphisms in early-onset atopic dermatitis using whole-exome sequencing. BMC Med Genet 18(1):1–9
doi: 10.1186/s12881-017-0368-9
Jamieson SE, de Roubaix LA, Cortina-Borja M, Tan HK, Mui EJ, Cordell HJ, Kirisits MJ, Miller EN, Peacock CS, Hargrave AC, Coyne JJ (2008) Genetic and epigenetic factors at COL2A1 and ABCA4 influence clinical outcome in congenital toxoplasmosis. PLoS ONE 3(6):e2285. https://doi.org/10.1371/journal.pone.0002285
doi: 10.1371/journal.pone.0002285
pubmed: 18523590
pmcid: 2390765
Juskaite V, Corcoran DS, Leitinger B (2017) Collagen induces activation of DDR1 through lateral dimer association and phosphorylation between dimers. Elife 6:e25716. https://doi.org/10.7554/eLife.25716
doi: 10.7554/eLife.25716
pubmed: 28590245
pmcid: 5489314
Kaur J, Reinhardt DP (2015) Extracellular matrix (ECM) molecules. Stem cell biology and tissue engineering in dental sciences. Academic Press, Cambridge, pp 25–45
doi: 10.1016/B978-0-12-397157-9.00003-5
Kaynak M, Nijman F, van Meurs J, Reijman M, Meuffels DE (2017) Genetic variants and anterior cruciate ligament rupture: a systematic review. Sports Med 47(8):1637–1650
pubmed: 28102489
pmcid: 5507974
doi: 10.1007/s40279-017-0678-2
Keene DR, Engvall E, Glanville RW (1988) Ultrastructure of type VI collagen in human skin and cartilage suggests an anchoring function for this filamentous network. J Cell Biol 107(5):1995–2006
pubmed: 3182942
doi: 10.1083/jcb.107.5.1995
Khoshnoodi J, Pedchenko V, Hudson BG (2008) Mammalian collagen IV. Microsc Res Tech 71(5):357–370
pubmed: 18219669
pmcid: 4788096
doi: 10.1002/jemt.20564
Kittelberger R, Davis PF, Flynn DW, Greenhill NS (1990) Distribution of type VIII collagen in tissues: an immunohistochemical study. Connect Tissue Res 24(3–4):303–318
pubmed: 2376131
doi: 10.3109/03008209009152157
Kruegel J, Rubel D, Gross O (2013) Alport syndrome—insights from basic and clinical research. Nat Rev Nephrol 9(3):170–178
pubmed: 23165304
doi: 10.1038/nrneph.2012.259
Kuang X, Sun L, Wu Y, Huang W (2020) A novel missense mutation of COL4A5 gene alter collagen IV α5 chain to cause X-linked Alport syndrome in a Chinese family. Transl Pediatr 9(5):587–595
pubmed: 33209720
pmcid: 7658769
doi: 10.21037/tp-20-47
Kumar P, Henikoff S, Ng PC (2009) Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm. Nat Protoc 4(7):1073–1081
pubmed: 19561590
doi: 10.1038/nprot.2009.86
Kusindarta DL, Wihadmadyatami H (2018) The role of extracellular matrix in tissue regeneration. Tissue Regen 75728:6
Latvanlehto A, Fox MA, Sormunen R, Tu H, Oikarainen T, Koski A, Naumenko N, Shakirzyanova A, Kallio M, Ilves M, Giniatullin R (2010) Muscle-derived collagen XIII regulates maturation of the skeletal neuromuscular junction. J Neurosci 30(37):12230–12241
pubmed: 20844119
pmcid: 2955218
doi: 10.1523/JNEUROSCI.5518-09.2010
Laurie GW, Leblond CP, Inoue S, Martin GR, Chung A (1984) Fine structure of the glomerular basement membrane and immunolocalization of five basement membrane components to the lamina densa (basal lamina) and its extensions in both glomeruli and tubules of the rat kidney. Am J Anat 169(4):463–481
pubmed: 6375342
doi: 10.1002/aja.1001690408
Lee JM, Yang PW, Chiang TH, Huang YC, Hsieh CY (2014) The genetic polymorphisms of ATG5 and COL4A3 are associated with the prognosis of patients with esophageal squamous cell carcinoma. Am Assoc Can Res. https://doi.org/10.1158/1538-7445.AM2014-2859
doi: 10.1158/1538-7445.AM2014-2859
Leeming DJ, Karsdal MA (2016) Type V collagen. Biochemistry of collagens, laminins and elastin. Academic Press, Cambridge, pp 43–48
doi: 10.1016/B978-0-12-809847-9.00005-2
Li L, Sun Z, Chen J, Zhang Y, Shi H, Zhu L (2020) Genetic polymorphisms in collagen-related genes are associated with pelvic organ prolapse. Menopause 27(2):223–229
pubmed: 31663982
pmcid: 7012360
doi: 10.1097/GME.0000000000001448
Liang C, Wang P, Liu X, Yang C, Ma Y, Yong L, Zhu B, Liu X, Liu Z (2018) Whole-genome sequencing reveals novel genes in ossification of the posterior longitudinal ligament of the thoracic spine in the Chinese population. J Orthop Surg Res 13(1):1–8
doi: 10.1186/s13018-018-1022-8
Longo I, Porcedda P, Mari F, Giachino D, Meloni I, Deplano C, Brusco A, Bosio M, Massella L, Lavoratti G, Roccatello D (2002) COL4A3/COL4A4 mutations: from familial hematuria to autosomal-dominant or recessive Alport syndrome. Kidney Int 61(6):1947–1956
pubmed: 12028435
doi: 10.1046/j.1523-1755.2002.00379.x
Maeda S, Ishidou Y, Koga H, Taketomi E, Ikari K, Komiya S, Takeda J, Sakou T, Inoue I (2001) Functional impact of human collagen α2 (XI) gene polymorphism in pathogenesis of ossification of the posterior longitudinal ligament of the spine. J Bone Miner Res 16(5):948–957
pubmed: 11341341
doi: 10.1359/jbmr.2001.16.5.948
Manon-Jensen T, Karsdal MA (2016) Type XII collagen. Biochemistry of collagens, laminins and elastin. Academic Press, Cambridge, pp 81–85
doi: 10.1016/B978-0-12-809847-9.00012-X
Matsunaga S, Sakou T (2012) Ossification of the posterior longitudinal ligament of the cervical spine: etiology and natural history. Spine 37(5):E309–E314
pubmed: 22146284
doi: 10.1097/BRS.0b013e318241ad33
Mio F, Chiba K, Hirose Y, Kawaguchi Y, Mikami Y, Oya T, Mori M, Kamata M, Matsumoto M, Ozaki K, Tanaka T (2007) A functional polymorphism in COL11A1, which encodes the α1 chain of type XI collagen, is associated with susceptibility to lumbar disc herniation. Am J Hum Genet 81(6):1271–1277
pubmed: 17999364
pmcid: 2276353
doi: 10.1086/522377
Moll S, Desmoulière A, Moeller MJ, Pache JC, Badi L, Arcadu F, Richter H, Satz A, Uhles S, Cavalli A, Drawnel F (2019) DDR1 role in fibrosis and its pharmacological targeting. Biochim Biophys Acta 1866(11):118474. https://doi.org/10.1016/j.bbamcr.2019.04.004
doi: 10.1016/j.bbamcr.2019.04.004
Muiznieks LD, Keeley FW (2013) Molecular assembly and mechanical properties of the extracellular matrix: a fibrous protein perspective. Biochim Biophys Acta Mol Basis Dis 1832(7):866–875
doi: 10.1016/j.bbadis.2012.11.022
Murdoch AD, Hardingham TE, Eyre DR, Fernandes RJ (2016) The development of a mature collagen network in cartilage from human bone marrow stem cells in Transwell culture. Matrix Biol 50:16–26
pubmed: 26523516
doi: 10.1016/j.matbio.2015.10.003
Myllyharju J, Kivirikko KI (2004) Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet 20(1):33–43
pubmed: 14698617
doi: 10.1016/j.tig.2003.11.004
Nimni ME (1980) The molecular organization of collagen and its role in determining the biophysical properties of the connective tissues. Biorheology 17(1–2):51–82
pubmed: 6996757
doi: 10.3233/BIR-1980-171-210
Pan TC, Zhang RZ, Pericak-Vance MA, Tandan R, Fries T, Stajich JM, Viles K, Vance JM, Chu ML, Speer MC (1998) Missense mutation in a von willebrand factor type A domain of the α3 (VI) collagen gene (COL6A3) in a family with bethlem myopathy. Hum Mol Genet 7(5):807–812
pubmed: 9536084
doi: 10.1093/hmg/7.5.807
Park HJ, Choe BK, Kim SK, Park HK, Kim JW, Chung JH, Hong IK, Chung DH, Kwon KH (2011) Association between collagen type XI α1 gene polymorphisms and papillary thyroid cancer in a Korean population. Exp Ther Med 2(6):1111–1116
pubmed: 22977629
pmcid: 3440783
doi: 10.3892/etm.2011.318
Patino MG, Neiders ME, Andreana S, Noble B, Cohen RE (2002) Collagen: an overview. Implant Dent 11(3):280–285
pubmed: 12271567
doi: 10.1097/00008505-200207000-00014
Quigley HA (1996) Number of people with glaucoma worldwide. Br J Ophthalmol 80(5):389–393
pubmed: 8695555
pmcid: 505485
doi: 10.1136/bjo.80.5.389
Reva B, Antipin Y, Sander C (2011) Predicting the functional impact of protein mutations: application to cancer genomics. Nucleic Acids Res 39(17):e118–e118
pubmed: 21727090
pmcid: 3177186
doi: 10.1093/nar/gkr407
Ricard-Blum S (2011) The collagen family. Cold Spring Harb Perspect Biol 3(1):a004978
pubmed: 21421911
pmcid: 3003457
doi: 10.1101/cshperspect.a004978
Rieder MJ, Taylor SL, Clark AG, Nickerson DA (1999) Sequence variation in the human angiotensin converting enzyme. Nat Genet 22(1):59–62
pubmed: 10319862
doi: 10.1038/8760
Rozario T, DeSimone DW (2010) The extracellular matrix in development and morphogenesis: a dynamic view. Dev Biol 341(1):126–140
pubmed: 19854168
doi: 10.1016/j.ydbio.2009.10.026
Saravani R, Hasanian-Langroudi F, Validad MH, Yari D, Bahari G, Faramarzi M, Khateri M, Bahadoram S (2015) Evaluation of possible relationship between COL4A4 gene polymorphisms and risk of keratoconus. Cornea 34(3):318–322
pubmed: 25651396
doi: 10.1097/ICO.0000000000000356
Shen G (2005) The role of type X collagen in facilitating and regulating endochondral ossification of articular cartilage. Orthod Craniofac Res 8(1):11–17
pubmed: 15667640
doi: 10.1111/j.1601-6343.2004.00308.x
Sheu JJ, Lin YJ, Chang JS, Wan L, Chen SY, Huang YC, Chan C, Chiu IW, Tsai FJ (2010) Association of COL11A2 polymorphism with susceptibility to Kawasaki disease and development of coronary artery lesions. Int J Immunogenet 37(6):487–492
pubmed: 20618517
doi: 10.1111/j.1744-313X.2010.00952.x
Shrivastava A, Radziejewski C, Campbell E, Kovac L, McGlynn M, Ryan TE, Davis S, Goldfarb MP, Glass DJ, Lemke G, Yancopoulos GD (1997) An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors. Mol Cell 1(1):25–34
pubmed: 9659900
doi: 10.1016/S1097-2765(00)80004-0
Siebuhr AS, Karsdal MA (2016) Type XIII collagen. Biochemistry of collagens, laminins and elastin. Academic Press, Cambridge, pp 87–91
doi: 10.1016/B978-0-12-809847-9.00013-1
Song Y, Du Z, Ren M, Yang Q, Wang Q, Chen G, Zhao H, Li Z, Wang J, Zhang G (2017) Association of gene variants of transcription factors PPARγ, RUNX2, Osterix genes and COL2A1, IGFBP3 genes with the development of osteonecrosis of the femoral head in Chinese population. Bone 101:104–112
pubmed: 28476574
doi: 10.1016/j.bone.2017.05.002
Štabuc-Šilih M, Ravnik-Glavač M, Glavač D, Hawlina M, Stražišar M (2009) Polymorphisms in COL4A3 and COL4A4 genes associated with keratoconus. Mol vis 15:2848–2860
pubmed: 20029656
pmcid: 2796875
Sukhumsirichart W (2018) Polymorphisms. Genetic diversity and disease susceptibility. IntechOpen, London
Tai Z, Huang L, Lu F, Shi Y, Ma S, Cheng J, Lin H, Liu X, Li Y, Yang Z (2017) Association study of candidate genes for susceptibility to Kashin-Beck disease in a Tibetan population. BMC Med Genet 18(1):1–8
doi: 10.1186/s12881-017-0423-6
Tanaka T, Ikari K, Furushima K, Okada A, Tanaka H, Furukawa KI, Yoshida K, Ikeda T, Ikegawa S, Hunt SC, Takeda J (2003) Genomewide linkage and linkage disequilibrium analyses identify COL6A1, on chromosome 21, as the locus for ossification of the posterior longitudinal ligament of the spine. Am J Hum Genet 73(4):812–822
pubmed: 12958705
pmcid: 1180604
doi: 10.1086/378593
Van Der Rest M, Garrone R (1991) Collagen family of proteins. FASEB J 5(13):2814–2823
pubmed: 1916105
doi: 10.1096/fasebj.5.13.1916105
Venselaar H, Te Beek TA, Kuipers RK, Hekkelman ML, Vriend G (2010) Protein structure analysis of mutations causing inheritable diseases. An e-Science approach with life scientist friendly interfaces. BMC Bioinform 11(1):1–10
doi: 10.1186/1471-2105-11-548
Vogel W, Gish GD, Alves F, Pawson T (1997) The discoidin domain receptor tyrosine kinases are activated by collagen. Mol Cell 1(1):13–23
pubmed: 9659899
doi: 10.1016/S1097-2765(00)80003-9
Wan Y, Li S, Gao Y, Tang L, Cao W, Sun X (2019) COL11A1 polymorphisms are associated with primary angle-closure glaucoma severity. J Ophthalmol. https://doi.org/10.1155/2019/2604386
doi: 10.1155/2019/2604386
pubmed: 30809385
pmcid: 6369458
Wang DG, Fan JB, Siao CJ, Berno A, Young P, Sapolsky R, Ghandour G, Perkins N, Winchester E, Spencer J, Kruglyak L (1998) Large-scale identification, mapping, and genotyping of single-nucleotide polymorphisms in the human genome. Science 280(5366):1077–1082
pubmed: 9582121
doi: 10.1126/science.280.5366.1077
Wang X, Li W, Wei K, Xiao R, Wang J, Ma H, Qin L, Shao W, Li C (2018) Missense mutations in COL4A5 or COL4A6 genes may cause cerebrovascular fibromuscular dysplasia: case report and literature review. Medicine 97(30):e11538. https://doi.org/10.1097/MD.0000000000011538
doi: 10.1097/MD.0000000000011538
pubmed: 30045277
pmcid: 6078732
Wang DD, Gao FJ, Hu FY, Li JK, Zhang SH, Xu P, Chang Q, Jiang R, Wu JH (2020) Next-generation sequencing-aided precise diagnosis of Stickler syndrome type I. Acta Ophthalmol 98(4):e440–e446
pubmed: 31736238
doi: 10.1111/aos.14302
Whittaker CA, Hynes RO (2002) Distribution and evolution of von willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. Mol Biol Cell 13(10):3369–3387
pubmed: 12388743
pmcid: 129952
doi: 10.1091/mbc.e02-05-0259
Xue F, Rabie ABM, Luo G (2014) Analysis of the association of COL2A1 and IGF-1 with mandibular prognathism in a Chinese population. Orthod Craniofac Res 17(3):144–149
pubmed: 24386886
doi: 10.1111/ocr.12038
Yang C, Song Y, Chen Z, Yuan X, Chen X, Ding G, Guan Y, McGrath M, Song C, Tong T, Wang H (2019) A nonsense mutation in COL4A4 gene causing isolated hematuria in either heterozygous or homozygous state. Front Genet 10:628. https://doi.org/10.3389/fgene.2019.00628
doi: 10.3389/fgene.2019.00628
pubmed: 31312213
pmcid: 6614519
Yao Y, Pei F, Kang P (2011) Selenium, iodine, and the relation with Kashin-Beck disease. Nutrition 27(11–12):1095–1100
pubmed: 21967994
doi: 10.1016/j.nut.2011.03.002
Zenteno JC, Crespí J, Buentello-Volante B, Buil JA, Bassaganyas F, Vela-Segarra JI, Diaz-Cascajosa J, Marieges MT (2014) Next generation sequencing uncovers a missense mutation in COL4A1 as the cause of familial retinal arteriolar tortuosity. Graefes Arch Clin Exp Ophthalmol 252(11):1789–1794
pubmed: 25228067
doi: 10.1007/s00417-014-2800-6
Zhang Y, Chen Q (2000) Changes of matrilin forms during endochondral ossification: molecular basis of oligomeric assembly. J Biol Chem 275(42):32628–32634
pubmed: 10930403
doi: 10.1074/jbc.M002594200