Showing papers by "Fabrizio Salvi published in 1988"

Familial amyloidotic polyneuropathy: transthyretin (prealbumin) variants in kindreds of Italian origin

Abstract: As part of an epidemiological study that aims to characterize chemically the mutation(s) in transthyretin (TTR) related to familial amyloidotic polyneuropathy (FAP) of different ethnic origins, studies were carried out on TTR from two FAP kindreds of Italian origin. Two different criteria were employed in the characterization of TTR from these kindreds: (1) immunoblotting of cyanogen bromide fragments for screening of TTR(Met30) and (2) isoelectric focusing. TTR(Met30) was not detected but other substitutions were demonstrated using isoelectric focusing techniques. One of the variants found is a basic TTR variant. The substitutions occurring in the variant TTRs of these two kindreds are not known and are presently under study.

Demonstration of Transthyretin (Prealbumin) Variants in Italian Kindreds with Familial Amyloidotic Polyneuropathy

Abstract: A prominent peripheral neuropathy is observed in patients with type I familial amyloidotic polyneuropathy (FAP) of different ethnic origins and geographic locations. Differences are seen, however, in clinical expression among these FAP kindreds. A variant transthyretin (TTR) with a methionine-for-valine substitution at position 30 has been demonstrated in blood plasma, amyloid deposits and cerebrospinal fluid of Portuguese patients with FAP (1,2). The same variant TTR has been demonstrated in FAP patients of Swedish and Greek ancestries (3,4) and in Japanese patients with FAP (5). In contrast, the major protein of amyloid in a Jewish patient was reported to be a TTR variant with a glycine — for threonine substitution of position 49 (6) and later found to have also an isoleucine for phenylalanine substitution at position 33 (7).