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Localized chondro-ossification underlies joint dysfunction and motor deficits in the Fkbp10 mouse model of osteogenesis imperfecta.

Joohyun LimCaressa D LietmanMatthew William GrolAlexis CastellonBrian DawsonMary AdeyeyeJyoti RaiMaryAnn WeisDouglas R KeeneRonen SchweitzerDongsu ParkDavid R EyreDeborah KrakowBrendan H Lee
Published in: Proceedings of the National Academy of Sciences of the United States of America (2021)
Osteogenesis imperfecta (OI) is a genetic disorder that features wide-ranging defects in both skeletal and nonskeletal tissues. Previously, we and others reported that loss-of-function mutations in FK506 Binding Protein 10 (FKBP10) lead to skeletal deformities in conjunction with joint contractures. However, the pathogenic mechanisms underlying joint dysfunction in OI are poorly understood. In this study, we have generated a mouse model in which Fkbp10 is conditionally deleted in tendons and ligaments. Fkbp10 removal substantially reduced telopeptide lysyl hydroxylation of type I procollagen and collagen cross-linking in tendons. These biochemical alterations resulting from Fkbp10 ablation were associated with a site-specific induction of fibrosis, inflammation, and ectopic chondrogenesis followed by joint deformities in postnatal mice. We found that the ectopic chondrogenesis coincided with enhanced Gli1 expression, indicating dysregulated Hedgehog (Hh) signaling. Importantly, genetic inhibition of the Hh pathway attenuated ectopic chondrogenesis and joint deformities in Fkbp10 mutants. Furthermore, Hh inhibition restored alterations in gait parameters caused by Fkbp10 loss. Taken together, we identified a previously unappreciated role of Fkbp10 in tendons and ligaments and pathogenic mechanisms driving OI joint dysfunction.
Keyphrases
  • mouse model
  • oxidative stress
  • binding protein
  • gene expression
  • genome wide
  • traumatic brain injury
  • poor prognosis
  • type diabetes
  • metabolic syndrome
  • dna methylation
  • insulin resistance
  • type iii