scholarly journals Phenotypic Heterogeneity in a Congenital Disorder of Glycosylation Caused by Mutations in STT3A

2017 ◽  
Vol 32 (6) ◽  
pp. 560-565 ◽  
Author(s):  
Arunabha Ghosh ◽  
Jill Urquhart ◽  
Sarah Daly ◽  
Anne Ferguson ◽  
Diana Scotcher ◽  
...  

STT3A encodes the catalytic subunit of the oligosaccharyltransferase complex. A congenital disorder of glycosylation caused by mutations in STT3A has only been reported in one family to date, associated with a Type I congenital disorder of glycosylation pattern of transferrin glycoforms. The authors describe a further 5 related individuals with a likely pathogenic variant in STT3A, 2 of whom also had variants in TUSC3. Common phenotypic features in all symptomatic individuals include developmental delay, intellectual disability, with absent speech and seizures. Two individuals also developed episodic hypothermia and altered consciousness. The family were investigated by autozygosity mapping, which revealed both a homozygous region containing STT3A and, in addition, a homozygous deletion of TUSC3 in one child. A likely pathogenic variant in STT3A was confirmed on Sanger sequencing of all affected individuals: the authors discuss the molecular findings in detail and further delineate the clinical phenotype of this rare disorder.

2014 ◽  
Vol 2 ◽  
pp. 232640981455052 ◽  
Author(s):  
Yasser Al-Sarraj ◽  
Tawfeg Ben-Omran ◽  
Mohammed Tolefat ◽  
Yosra Bejaoui ◽  
Hatem El-Shanti ◽  
...  

Glycobiology ◽  
2009 ◽  
Vol 19 (12) ◽  
pp. 1554-1562 ◽  
Author(s):  
Weston B Struwe ◽  
Bethany L Hughes ◽  
David W Osborn ◽  
Erica D Boudreau ◽  
Kristin M D Shaw ◽  
...  

Author(s):  
Matthew P. Wilson ◽  
Alejandro Garanto ◽  
Filippo Pinto e Vairo F ◽  
Bobby G. Ng ◽  
Wasantha K. Ranatunga ◽  
...  

Glycobiology ◽  
2005 ◽  
Vol 15 (11) ◽  
pp. 1084-1093 ◽  
Author(s):  
Erik A. Eklund ◽  
Nabyl Merbouh ◽  
Mie Ichikawa ◽  
Atsushi Nishikawa ◽  
Jessica M. Clima ◽  
...  

1989 ◽  
Vol 62 (03) ◽  
pp. 897-901 ◽  
Author(s):  
Hans K Ploos van Amstel ◽  
Pieter H Reitsma ◽  
Karly Hamulyák ◽  
Christine E M de Die-Smulders ◽  
Pier M Mannucci ◽  
...  

SummaryProbands from 15 unrelated families with hereditary protein S deficiency type I, that is having a plasma total protein S concentration fifty percent of normal, were screened for abnormalities in their protein S genes by Southern analysis. Two probands were found to have a deviating DNA pattern with the restriction enzyme Mspl. In the two patients the alteration concerned the disappearance of a Mspl restriction site, CCGG, giving rise to an additional hybridizing Mspl fragment.Analysis of relatives of both probands showed that in one family the mutation does not co-segregate with the phenotype of reduced plasma protein S. In the family of the other proband, however, complete linkage between the mutated gene pattern and the reduced total protein S concentration was found: 12 heterozygous relatives showed the additional Mspl fragment but none of the investigated 26 normal members of the family. The mutation is shown to reside in the PSβ gene, the inactive protein S gene. The cause of type I protein S deficiency, a defect PSα gene has escaped detection by Southern analysis. No recombination has occurred between the PSα gene and the PSβ gene in 23 informative meioses. This suggests that the two protein S genes, located near the centromere of chromosome 3, are within 4 centiMorgan of each other.


2009 ◽  
Vol 30 (5) ◽  
pp. 795-803 ◽  
Author(s):  
Ana I. Vega ◽  
Celia Pérez-Cerdá ◽  
Lourdes R. Desviat ◽  
Gert Matthijs ◽  
Magdalena Ugarte ◽  
...  

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