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Identification of a Novel Homozygous IHH Variant Causing Novel Acromesomelic Maroteaux-Type Skeletal Dysplasia in a Pakistani Family Cover

Identification of a Novel Homozygous IHH Variant Causing Novel Acromesomelic Maroteaux-Type Skeletal Dysplasia in a Pakistani Family

By: ,  ,  ,  ,  ,  ,   and    
Open Access
|May 2026

References

  1. Kurt F, Ceylaner S, Yakut HI (2013) Acromesomelic dysplasia with cardiac and neurologic abnormalities: An association by chance, new features of Maroteaux type or a new syndrome? Genet Counse 24: 75–80.
  2. Khan S, Basit S, Khan MA, Muhammad N, Ahmad W (2016) Genetics of human isolated acromesomelic dysplasia. Eur J Med Genet 59: 198–203. https://doi.org/10.1016/j.ejmg.2016.02.011
  3. Hassan M, & Lachman RS (2007) Taybi & Lachman’s radiology of syndromes, metabolic disorders and skeletal dysplasias (5th ed.). Mosby.
  4. Unger S, Ferreira CR, Mortier GR, Ali H, Bertola DR, Calder A, Cohn DH, Cormier-Daire V, Girisha KM, Hall C, Krakow D, Mäkitie O, Mundlos S, Nishimura G, Robertson SP, Savarirayan R, Sillence D, Simon M, Sutton VR, Superti-Furga A (2023) Nosology of genetic skeletal disorders: 2023 revision. Amer J Med Genet Part A 191: 1164–1209. https://doi.org/10.1002/ajmg.a.63132
  5. Kant SG, Polinkovsky A, Mundlos S, Zabel B, Thomeer RTWM & Zonderland HM (1998) Acromesomelic dysplasia Maroteaux type maps to human chromosome 9. A J Hum Genet 63: 155–162. https://doi.org/10.1086/301917
  6. Thomas JT, Kilpatrick MW, Lin, K, Erlacher L, Lembessis P, Costa T, Tsipouras P, Luyten, FP (1997) Disruption of human limb morphogenesis by a dominant negative mutation in CDMP1. Nature Genet 17: 58–64. https://doi.org/10.1038/ng0997-58
  7. Faiyaz-Ul-Haque M, Ahmad W, Zaidi SHE, Haque S, Teebi AS, Ahmad M, Cohn DH, Tsui LC (2002) Mutation in the cartilage-derived morphogenetic protein-1 (CDMP1) gene in kindred affected with fibular hypoplasia and complex brachydactyly (Du Pan syndrome) Clin Genet 61: 454–458. https://doi.org/10.1034/j.1399-0004.2002.610610.x
  8. Byrnes AM, Racacho L, Nikkel SM, Xiao F, MacDonald H, Underhill TM, Bulman DE (2010) Mutations in GDF5 presenting as semidominant brachydactyly A1. Hum Mut 31: 1155–1162. https://doi.org/10.1002/humu.21338
  9. Stange K, Desir J, Kakar N, Mueller TD, Budde BS, Gordon CT, Horn D, Seemann P, Borck GA (2015) A hypomorphic BMPR1B mutation causes Du Pan acromesomelic dysplasia. Orphanet J Rare Dis10: 84. https://doi.org/10.1186/s13023-015-0299-5
  10. Díaz-González F, Wadhwa S, Rodriguez-Zabala M, Kumar S, Aza-Carmona M, Sentchordi-Montane L, Alonso M, Ahmad I, Zahra S, Kumar D, Kushwah N, Shamim U, Sait H, Kapoor S, Roldan B, Nishimura G, Offiah AC, Faruq M, Heath KE (2022) Biallelic cGMP-dependent type II protein kinase gene (PRKG2) variants cause a novel acromesomelic dysplasia. J Med Genet 59: 28–38. https://doi.org/110.1136/jmedgenet-2020-107177
  11. Osebold WR, Remondini DJ, Lester EL, Spranger JW, Opitz JM (1985) An autosomal dominant syndrome of short stature with mesomelic shortness of limbs, abnormal carpal and tarsal bones, hypoplastic middle phalanges, and bipartite calcanei. Am J Med Genet 22: 791–809. https://doi.org/10.1002/ajmg.1320220414
  12. Faivre L, Le Merrer M, Megarbane A, Gilbert B, Mortier G, Cusin V, Munnich A, Maroteaux P, Cormier-Daire V (2000) Exclusion of chromosome 9 helps to identify mild variants of acromesomelic dysplasia Maroteaux type J Med Genet 37: 52–54. https://doi.org/10.1136/jmg.37.1.52
  13. Wu J, Wang M, Jiao Z, Dou B, Li B, Zhang J, Zhang H, Sun Y, Tu X, Kong X, Bai Y (2022) Novel loss-of-function mutations in NPR2 cause acromesomelic dysplasia, Maroteaux type. Front Genet 13:823861. https://doi.org/10.3389/fgene.2022.823861
  14. Bartels CF, Bukulmez H, Padayatti P, Rhee DK, van Ravenswaaij-Arts C, Pauli RM, Mundlos S, Chitayat D, Shih LY, Al-Gazali LI, Kant S, Cole T, Morton J, Cormier-Daire V, Faivre L, Lees M, Kirk J, Mortier GR, Leroy J, Zabel B, Kim CA, Crow Y, Braverman NE, van den Akker F, Warman ML (2004) Mutations in the transmembrane natriuretic peptide receptor NPR-B impair skeletal growth and cause acromesomelic dysplasia, type Maroteaux. Am J Hum Gen 75: 27–34. https://doi.org/10.1086/422013
  15. Thomas JT, Lin K, Nandekar M, Camargo M, Cervenka J, Luyten FP (1996). A human chondrodysplasia due to a mutation in a TGF-beta superfamily member. Nature Genet. 12: 315–317. https://doi.org/10.1038/ng0396-315
  16. Mortier GR, Kramer PPG, Giedion A, Beemer FA (2003) Acrocapitofemoral dysplasia: A newly recognized autosomal recessive skeletal dysplasia. J Med Genet 40: 201–207. https://doi.org/10.1136/jmg.40.3.201
  17. Cubuk PO, Duz MB (2021) Acrocapitofemoral dysplasia: Novel mutation in IHH in two adult patients from the third family in the literature and progression of the disease. Eur J Med Genet 64: 104343. https://doi.org/10.1016/j.ejmg.2021.104343
  18. Hellemans J, Coucke PJ, Giedion A, De Paepe A, Kramer P, Beemer F, Mortier GR (2003) Homo-zygous mutations in IHH cause acrocapitofemoral dysplasia, an autosomal recessive disorder with cone-shaped epiphyses in hands and hips. American Journal of Human Genetics 72:1040–1046. https://doi.org/10.1086/374318
  19. Saeed T, Bibi N, Ahmad A, Khan S, Ansar M, Wasif N, Kalsoom U (2025) A novel biallelic variant in IHH causing acrocapitofemoral dysplasia in a Pakistani family. Mol Genet Genomic Med 13: e70085. https://doi.org/10.1002/mgg3.70085
  20. Stattin EL, Lindén B, Lönnerholm T, Schuster J, Dahl N (2009) Brachydactyly type A1 associated with unusual radiological findings and a novel Arg158Cys mutation in the Indian hedgehog (IHH) gene. Eur J Med Genet 52(5): 297–302. https://doi.org/10.1016/j.ejmg.2009.05.008
  21. Vasques GA, Funari MFA, Ferreira FM, Aza-Carmona M, Sentchordi-Montané L, Barraza-García J, Lerario AM, Yamamoto GL, Naslavsky MS, Duarte YA O, Bertola DR, Heath KE, Jorge AAL (2018) IHH gene mutations causing short stature with nonspecific skeletal abnormalities and response to growth hormone therapy. J Clin Endocrinol Metabol 103: 604–614. https://doi.org/10.1210/jc.2017-02026”
  22. Yang J, Yan R, Roy A, Xu D, Poisson J, Zhang Y (2015) The I-TASSER suite: Protein structure and function prediction. Nature Methods 12: 7–8. https://doi.org/10.1038/nmeth.3213
  23. Emsley P, Lohkamp B, Scott WG, Cowtan K (2010) Features and development of Coot. Acta Crystallographica Section D: Biological Crystallography, 66: 486–501. https://doi.org/10.1107/S0907444910007493
  24. Gopalakrishnan K, Sowmiya G, Sheik SS, Sekar K (2007) Ramachandran plot on the web (2.0). Prot Peptid Lett 14: 669–671. https://doi.org/10.2174/092986607781483847
  25. Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PRO-CHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8: 477–486. https://doi.org/10.1007/BF00228148
  26. Lüthy R, Bowie JU, Eisenberg D (1992) Assessment of protein models with three-dimensional profiles. Nature 356: 83–85. https://doi.org/10.1038/356083a0
  27. Venselaar H, TeBeek TA, Kuipers RK, Hekkelman ML, Vriend G (2010) An e-science approach with life scientist friendly interfaces. BMC Bioinformat 11: 548. https://doi.org/10.1186/1471-2105-11-548
  28. Duan Y, Wu C, Chowdhury S, Lee MC, Xiong G, Yang R, Cieplak P, Luo R, Lee T, Caldwell J, Wang, J, Kollman PA (2003) A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. Comput Chem 24: 1999–2012. https://doi.org/10.1002/jcc.10349
  29. Zlenko DV (2012) Diffusion factor calculation for TIP4P model of water. Biofizika, 57:197–204. https://doi.org/10.1134/S0006350912020200
  30. Richards S, Aziz N, Bale S et al (2015) Standards and guidelines for the interpretation of sequence variants: A joint consensus recommendation of the American College of Medical Genetics and Genomics and the Association for Molecular Pathology. Genet Med 17: 405–424. https://doi.org/10.1038/gim.2015.30
  31. Chung UI, Schipani E, McMahon AP, Kronenberg HM (2001) Indian hedgehog couples chondrogenesis to osteogenesis in endochondral bone development. J Clin Invest 107: 295–304. https://doi.org/10.1172/JCI11706
  32. Karp SJ, Schipani E, St-Jacques B, Hunzelman J, Kronenberg H, McMahon AP (2000) Indian hedgehog coordinates endochondral bone growth and morphogenesis via parathyroid hormone related-protein-dependent and -independent pathways. Development, 127: 543–548. https://doi.org/10.1242/dev.127.3.543
  33. Long F, Chung UI, Ohba S, McMahon J, Kronenberg HM, McMahon AP (2004) Ihh signaling is directly required for the osteoblast lineage in the endochondral skeleton. Development 131: 1309–1318. https://doi.org/10.1242/dev.01006
  34. Klopocki E, Lohan S, Brancati F, Koll R, Brehm A, Seemann P, Dathe K, Stricker S, Hecht J, Bosse K, Betz RC, Garaci FG, Dallapiccola B, Jain M, Muenke M, Ng VC, Chan W, Chan, D, Mundlos S (2011) Copy-number variations involving the IHH locus are associated with syndactyly and craniosynostosis. A J Hum Genet 88: 70–75. https://doi.org/10.1016/j.ajhg.2010.11.006
  35. Burke R, Nellen D, Bellotto M, Hafen E, Senti KA, Dickson BJ, Basler K (1999) Dispatched, a novel sterol-sensing domain protein dedicated to the release of cholesterol-modified hedgehog from signalling cells. Cell 99: 803–815. https://doi.org/10.1016/S0092-8674(00)81677-3
  36. Díaz-González F, Sentchordi-Montané L, Lucas-Castr E, Modamio-Høybjør S, Heath K E (2024) Variants in both the N- or C-terminal domains of IHH lead to defective secretion causing short stature and skeletal defects. Eur J Endocrinol 19: 38–46. https://doi.org/10.1093/ejendo/lvae072
Language: English
Page range: 29 - 40
Published on: May 14, 2026
In partnership with: Paradigm Publishing Services
Publication frequency: 2 issues per year

© 2026 M Hanif, B Ahmad, S Farman, S Hassan, A Hayat, N Bibi, U Kalsoom, B Khan, published by Macedonian Academy of Sciences and Arts
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.