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Amyloidogenic and non‐amyloidogenic transthyretin Asn 90 variants
Author(s) -
Alves I. L.,
Almeida M. R.,
Skare J.,
Skinner M.,
Kurose K.,
Sakaki Y.,
Costa P. P.,
Saraiva M. J. M.
Publication year - 1992
Publication title -
clinical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 102
eISSN - 1399-0004
pISSN - 0009-9163
DOI - 10.1111/j.1399-0004.1992.tb03131.x
Subject(s) - transthyretin , genetics , computational biology , biology , endocrinology
Recently, a new transthyretin (TTR) variant was described in the normal Portuguese and German populations. The same substitution was found associated with familial amyloidotic polyneuropathy (FAP) in an American family of Italian origin. Comparative isoelectric focusing studies showed a difference in the mobility pattern between the non‐pathogenic and pathogenic variants. However, comparative DNA sequencing between them did not reveal any additional mutation. Comparative isoelectric focusing between the variants and TTR Asn 90 produced by recombinant techniques indicated that the non‐pathogenic variant has the electrophoretic behaviour expected for the mutation. We suggest that an as yet unknown post‐translational modification may have occurred in the FAP‐associated Asn 90 variant, turning it into an amyloidogenic molecule.