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Atrial amyloid deposits in the failing human heart display both atrial and brain natriuretic peptide‐like immunoreactivity
Author(s) -
Pucci Angela,
Wharton John,
Arbustini Eloisa,
Grasso Maurizia,
Diegoli Marta,
Needleman Philip,
Viganò Mario,
Polak Julia M.
Publication year - 1991
Publication title -
the journal of pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.964
H-Index - 184
eISSN - 1096-9896
pISSN - 0022-3417
DOI - 10.1002/path.1711650307
Subject(s) - atrial natriuretic peptide , medicine , prohormone , amyloid (mycology) , npr2 , brain natriuretic peptide , peptide , heart failure , natriuretic peptide , endocrinology , npr1 , amyloidosis , peptide hormone , hormone , chemistry , pathology , biochemistry
Atrial amyloid deposits are common in the ageing human heart and contain α‐atrial natriuretic peptide (proANP 99–126 ) immunoreactivity. However, atrial myocytes secrete both amino and carboxy terminal fragments of the ANP prohormone (proANP 1–126 ) and also express an homologous, but separate brain natriuretic peptide (BNP). Characteristic amyloid deposits were identified in the atria of 9/22 patients (26–63 years of age) with end‐stage heart failure. Amyloid fibrils displayed immunoreactivity for both amino and carboxy terminal fragments of proANP 1–126 and for the distinct BNP sequence. As in other endocrine organs, both mature and precursor peptide sequences appear to be constituents of amyloid fibrils. Whilst immunoreactivity for cardiac peptide hormones is co‐localized in atrial amyloid deposits, it is uncertain whether the increase in natriuretic peptide expression which accompanies cardiac failure contributes to the incidence of isolated atrial amyloidosis.