CARDIAC AMYLOIDOSIS - A REVIEW AND REPORT OF A NEW TRANSTHYRETIN (PREALBUMIN) VARIANT

• Type: Another Publication in an International Scientific Journal
• Date: 1993

Authors

HESSE, A (Author) Other; ALTLAND, K (Author) Other; LINKE, RP (Author) Other; ALMEIDA, MR (Author) ICBAS; SARAIVA, MJM (Author) ICBAS; STEINMETZ, A (Author) Other; MAISCH, B (Author) Other

Journal

Title: British Heart Journal

Vol. 70

Pages: 111-115

ISSN: 0007-0769

Publisher: BMJ PUBLISHING GROUP

Indexing

ISI Web of Knowledge - 38 Citations

Scopus - 44 Citations

Scientific classification

FOS: Medical and Health sciences > Clinical medicine

Other information

Authenticus ID: P-001-MSR

Abstract (EN): Cardiac amyloidosis is caused by amyloid deposits derived from different human plasma proteins. It can lead to cardiac conduction disturbances, restrictive cardiomyopathy, and low output heart failure. The heart is variably involved during the development of systemic amyloidosis and seems to be more frequently affected in immunoglobulin (primary) than in reactive (secondary) amyloidosis. Amyloid is common in the elderly. Isolated atrial amyloid, for which a major subunit is the atrial natriuretic peptide, seems to be three times more frequent than senile cardiac amyloid, which is derived from normal prealbumin (transthyretin). Like polyneuropathy, cardiac amyloidosis is a prominent clinical feature of hereditary amyloidosis, namely of the autosomal dominant transthyretin (TTR) type. All 28 cases of TTR amyloidoses reported so far were heterozygotes for a single nucleotide change in the gene for TTR that resulted in amino acid substitutions in the mature protein. A new TTR genetic variant is reported in a German family where the index patient presented at the age of 63 with anginal pain and arrhythmia. Electrocardiography was suggestive of a pseudoinfarction pattern, and echocardiography and cardiac catheterisation showed signs of hypertrophic nonobstructive cardiomyopathy with increased ventricular filling pressures and a prominent ''a'' wave. Amyloid of the TTR type was identified by immunohistochemistry in the endomyocardial biopsy specimen. Hybrid isoelectric focusing established heterozygosity by showing normal TTR protein and an electrically neutral TTR variant differing from all known TTR variants so far. The patient died in an accident before investigations were complete. Electrophoretic analysis of the plasma from his first degree relatives (son, daughter, brother, and mother) identified the asymptomatic 22 year old son as an apparently heterozygous carrier of the mutant TTR protein. Comparative tryptic peptide mapping and sequencing showed that isoleucine at position 68 of the amino acid sequence was replaced by leucine.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5