Expanding the clinical and molecular spectrum of PRMT7 mutations: three additional patients and review

Abstract

Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues. Arginine methylation is involved in multiple biological processes, such as signal transduction, mRNA splicing, transcriptional control, DNA repair, and protein translocation. Currently, seven patients have been described harboring compound heterozygous or homozygous variants in the PRMT7 gene, causing a novel intellectual disability syndrome, known as SBIDDS syndrome (Short Stature, Brachydactyly, Intellectual Developmental Disability, and Seizures).

We report on three additional patients from two consanguineous families with severe/moderate intellectual disability, short stature, brachydactyly and dysmorphisms. Exome sequencing revealed two novel homozygous mutations in PRMT7. Our findings expand the clinical and molecular spectrum of homozygous PRMT7 mutations, associated to the SBIDDS syndrome, showing a possible correlation between the type of mutation and the severity of the phenotype.

We describe 3 patients from 2 unrelated families with SBIDDS syndrome, displaying two novel homozygous mutations in the PRMT7 gene. The patients reported in this study extend the clinical and mutational spectrum of the PRMT7-related disorder, showing a possible genotype/phenotype correlation that can have an impact on clinical management of patients. A clinical review of currently reported SBIDDS patients is provided.

http://ift.tt/2x1c8Zs