We present a 3⅓-year-old girl with severe Charcot-Marie-Tooth disease type 1 (Dejerine-Sottas disease), who was a compound heterozygote carrying a deletion of the whole peripheral myelin protein 22 (PMP22) and a deletion of exon 5 in the other PMP22 allele.
We describe a patient with a longstanding history of hypertrophic neuropathy of Dejerine-Sottas type, ultimately diagnosed with CMT1E disease due to a new p.Leu18Arg missense mutation in the first transmembrane domain of the PMP22 gene.
Other mutations of the myelin protein PMP22 and myelin protein P0 genes have been associated with the clinical syndrome known as Dejerine-Sottas disease.
In 5 cases showing neither duplication, deletion, nor a point mutation in the exons of the PMP-22 gene on heteroduplex DNA analysis, the histopathological findings strongly suggested a diagnosis of chronic inflammatory demyelinating polyneuropathy in 2 cases, and HMSN Ib, or HMSN non-a non-b, and HMSN III in 3 cases.
Mutational analysis of the MPZ, PMP22 and Cx32 genes in patients of Spanish ancestry with Charcot-Marie-Tooth disease and hereditary neuropathy with liability to pressure palsies.
Phe 84 deletion of the PMP22 gene associated with hereditary motor and sensory neuropathy HMSN III with multiple cranial neuropathy: clinical, neurophysiological and magnetic resonance imaging findings.
Dejerine-Sottas disease (DSD), also called hereditary motor and sensory neuropathy type III (HMSNIII), is a severe, infantile-onset, demyelinating polyneuropathy syndrome that may be associated with point mutations in either the PMP22 gene or the P0 gene and shares considerable clinical and pathologic features with CMT1.
Here, a sporadic patient affected with DSS is described; nerve biopsy disclosed a picture of hypomyelination/amyelination with basal laminae onion bulbs and no florid demyelination and it was consistent with congenital hypomyelination neuropathy (CHN); molecular analysis disclosed a novel point mutation of PMP22 that causes a non-conservative arginine for cysteine substitution at codon 109, in the third transmembrane domain.