Identification of novel LFNG mutations in spondylocostal dysostosis.
Abnormalities, Multiple
/ genetics
Amino Acid Sequence
Glucosyltransferases
Glycosyltransferases
/ genetics
Hernia, Diaphragmatic
/ genetics
Hexosyltransferases
/ genetics
Humans
Infant
Intracellular Signaling Peptides and Proteins
/ genetics
Male
Membrane Proteins
/ genetics
Mutation
Prognosis
Sequence Homology
Journal
Journal of human genetics
ISSN: 1435-232X
Titre abrégé: J Hum Genet
Pays: England
ID NLM: 9808008
Informations de publication
Date de publication:
Mar 2019
Mar 2019
Historique:
received:
13
08
2018
accepted:
19
11
2018
revised:
17
10
2018
pubmed:
12
12
2018
medline:
11
4
2019
entrez:
12
12
2018
Statut:
ppublish
Résumé
Spondylocostal dysostosis (SCDO) is a heterogeneous group of skeletal disorders characterized by multiple segmentation defects involving vertebrae and ribs. Seven disease genes have been reported as causal genes for SCDO: DLL3, MESP2, TBX6, HES7, RIPPLY2, DMRT2, and LFNG. Here we report a Japanese SCDO case with multiple severe vertebral anomalies from cervical to sacral spine. The patient was a compound heterozygote for c.372delG (p.K124Nfs*) and c.601G>A (p.D201N) variants of LFNG, which encodes a glycosyltransferase (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase). The missense variant was in the DxD motif, an active-site motif of the glycosyltransferase, and its loss of the enzyme function was confirmed by an in vitro enzyme assay. This is the second report of LFNG mutations in SCDO.
Identifiants
pubmed: 30531807
doi: 10.1038/s10038-018-0548-2
pii: 10.1038/s10038-018-0548-2
doi:
Substances chimiques
Intracellular Signaling Peptides and Proteins
0
Membrane Proteins
0
Glycosyltransferases
EC 2.4.-
Glucosyltransferases
EC 2.4.1.-
Hexosyltransferases
EC 2.4.1.-
LFNG protein, human
EC 2.4.1.-
MFNG protein, human
EC 2.4.1.222
Types de publication
Case Reports
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
261-264Subventions
Organisme : Japan Agency for Medical Research and Development (AMED)
ID : 17ek0109212h0001
Organisme : Japan Agency for Medical Research and Development (AMED)
ID : 17ek0109280h0001
Organisme : Japan Society for the Promotion of Science (JSPS)
ID : 16K08251
Organisme : Japan Society for the Promotion of Science (JSPS)
ID : 17K16710
Références
EMBO J. 1999 Jul 1;18(13):3546-57
pubmed: 10393171
Nat Genet. 2000 Apr;24(4):438-41
pubmed: 10742114
Curr Biol. 2000 Jul 13;10(14):813-20
pubmed: 10899003
Nature. 2000 Jul 27;406(6794):369-75
pubmed: 10935626
Proc Natl Acad Sci U S A. 2003 May 27;100(11):6404-9
pubmed: 12743367
Am J Hum Genet. 2004 Jun;74(6):1249-54
pubmed: 15122512
J Biol Chem. 2005 Dec 23;280(51):42454-63
pubmed: 16221665
Am J Hum Genet. 2006 Jan;78(1):28-37
pubmed: 16385447
Dev Dyn. 2007 Jun;236(6):1456-74
pubmed: 17497699
Hum Mol Genet. 2008 Dec 1;17(23):3761-6
pubmed: 18775957
J Biol Chem. 2009 Jan 30;284(5):3294-305
pubmed: 19028689
Am J Med Genet. 1991 Sep 1;40(3):264-70
pubmed: 1951427
Hum Mol Genet. 2013 Apr 15;22(8):1625-31
pubmed: 23335591
Hum Mol Genet. 2015 Mar 1;24(5):1234-42
pubmed: 25343988
N Engl J Med. 2015 Jan 22;372(4):341-50
pubmed: 25564734
PLoS One. 2015 Apr 09;10(4):e0123776
pubmed: 25856312
Hum Mutat. 2017 Mar;38(3):317-323
pubmed: 28054739
Am J Med Genet A. 2018 May;176(5):1216-1221
pubmed: 29681102
Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):7945-50
pubmed: 9653120
Nature. 1998 Jul 23;394(6691):377-81
pubmed: 9690473