We report a new transthyretin (ATTR) gene c.272C>G mutation and variant protein, 
p.Leu32Val, in a kindred of Bolivian origin with a rapid progressive peripheral 
neuropathy and cardiomyopathy. Three individuals from a kindred with peripheral 
nerve and cardiac amyloidosis were examined. Analysis of the TTR gene was 
performed by Sanger direct sequencing. Neuropathologic examination was obtained 
on the index patient with mass spectrometry study of the ATTR deposition. Direct 
DNA sequence analysis of exons 2, 3, and 4 of the TTR gene demonstrated a c.272 
C>G mutation in exon 2 (p.L32V). Sural nerve biopsy revealed massive amyloid 
deposition in the perineurium, endoneurium and vasa nervorum. Mass spectrometric 
analyses of ATTR immunoprecipitated from nerve biopsy showed the presence of 
both wild-type and variant proteins. The observed mass results for the wild-type 
and variant proteins were consistent with the predicted values calculated from 
the genetic analysis data. The ATTR L32V is associated with a severe course. 
This has implications for treatment of affected individuals and counseling of 
family members.