Premium
Mouse S amd9l is not a functional paralogue of the human SAMD 9 , the gene mutated in normophosphataemic familial tumoral calcinosis
Author(s) -
Li Qiaoli,
Guo Haitao,
Matsui Hirotaka,
Honda Hiroaki,
Inaba Toshiya,
Sundberg John P.,
Sprecher Eli,
Uitto Jouni
Publication year - 2012
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/j.1600-0625.2012.01524.x
Subject(s) - gene , ectopic calcification , biology , genetics , cancer research , pathology , medicine , calcification
Normophosphataemic familial tumoral calcinosis, charac‐terized by ectopic mineralization of skin, is caused by mutations in the SAMD 9 gene located in human chromosome 7q21, next to a paralogous gene, SAMD 9 ‐like ( SAMD 9 L ). The mouse does not have a SAMD 9 orthologue, S amd9 , because it has been deleted during evolution owing to genomic rearrangements. It has been suggested that the mouse S amd9l gene serves as a functional paralogue of human SAMD 9 . In this study, we examined S amd9l knockout mice with respect to ectopic mineralization. We also crossed these mice with A bcc6 tm1JfK mice, a model system to study pseudoxanthoma elasticum, to see whether the absence of the S amd9l gene modifies the mineralization process. Necropsy analysis of S amd9l tm1Homy mice revealed no evidence of ectopic mineralization, and deletion of the S amd9l gene in mice failed to modify the mineralization process on the A bcc6 tm1JfK background. Collectively, the results suggest that mouse S amd9l is not a functional paralogue of human SAMD 9 .