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Identification of a novel ANO5 missense mutation in a Chinese family with familial florid osseous dysplasia.
Lv, Mingming; You, Guoling; Wang, Jinbing; Fu, Qihua; Gupta, Anand; Li, Jun; Sun, Jian.
Afiliação
  • Lv M; Department of Oral Maxillofacial-Head Neck Oncology, Shanghai Ninth People's Hospital, College of Stomatology, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
  • You G; National Clinical Research Center for Oral Diseases, Shanghai Key Laboratory of Stomatology & Shanghai Research Institute of Stomatology, Shanghai, China.
  • Wang J; Department of Laboratory Medicine, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
  • Fu Q; Department of Oral Maxillofacial-Head Neck Oncology, Shanghai Ninth People's Hospital, College of Stomatology, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
  • Gupta A; National Clinical Research Center for Oral Diseases, Shanghai Key Laboratory of Stomatology & Shanghai Research Institute of Stomatology, Shanghai, China.
  • Li J; Department of Laboratory Medicine, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
  • Sun J; Department of Dentistry, Government Medical College Hospital, Chandigarh, India.
J Hum Genet ; 64(7): 599-607, 2019 Jul.
Article em En | MEDLINE | ID: mdl-30996299
Familial florid osseous dysplasia (FFOD) is an autosomal dominant disorder of connective tissue, characterized by lobulated cementum-like masses scattered throughout the jaws and the alveolar process. This study aimed to identify the genetic etiology of a three-generation Chinese family affected with FFOD. A novel missense mutation p.C356W in anoctamin 5 (ANO5) gene was successfully identified as the pathogenic mutation by whole-exome sequencing (WES). The p.C356W mutation is located in the first loop between the first and second transmembrane domain of ANO5 protein. Sequence alignment of ANO5 protein among many different species revealed that this position is highly conserved. The p.C356W mutation may damage the predicted protein stability of ANO5 by altering the structure of several extracellular loops of ANO5 and affecting the formation of the disulfide bond, thereby disrupting the correct folding of ANO5 protein. Thus, the amino acid at position 356 appears to play a key role in the protein structural stability and function of ANO5 protein. Our results may also provide new insights into the cause and diagnosis of FFOD and may have implications for genetic counseling and clinical management.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Osteomielite / Mutação de Sentido Incorreto / Displasia Fibrosa Óssea / Anoctaminas Tipo de estudo: Diagnostic_studies / Prognostic_studies Limite: Female / Humans / Male / Middle aged País/Região como assunto: Asia Idioma: En Revista: J Hum Genet Assunto da revista: GENETICA MEDICA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Osteomielite / Mutação de Sentido Incorreto / Displasia Fibrosa Óssea / Anoctaminas Tipo de estudo: Diagnostic_studies / Prognostic_studies Limite: Female / Humans / Male / Middle aged País/Região como assunto: Asia Idioma: En Revista: J Hum Genet Assunto da revista: GENETICA MEDICA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: China