01765nas a2200253 4500000000100000008004100001260001300042653001000055653001200065653001600077653001000093653001100103653001100114653000900125653001500134653002300149653002800172100001500200245007800215300001000293490000700303520118700310022001401497 1978 d c1978 Mar10aAdult10aAmyloid10aAmyloidosis10aChild10aFemale10aHumans10aMale10aNew Guinea10aProtein Precursors10aSerum Amyloid A Protein1 aAnders R F00aAmyloid fibril proteins found in Papua New Guinean and other amyloidoses. a79-850 v213 a

Recent studies have established that amyloid fibrils found in different clinical conditions differ in the nature of their constituent proteins. In primary amyloidosis and in amyloidosis associated with multiple myeloma or macroglobulinaemia the amyloid fibrils are usually largely composed of fragments of immunoglobulin light chains. In secondary amyloidosis, protein AA, a unique protein unrelated to immunoglobulins, is the major component of the fibrils. Other chemical types of amyloid have been described in primary medullary carcinoma of the thyroid and in senile cardiac amyloidosis. In Papua New Guinea amyloidosis is seen secondary to chronic infections such as leprosy and tuberculosis as well as in patients without an apparent predisposing disease. The amyloid proteins obtained from a representative range of Papua New Guinean patients have been characterised and in all cases examined the amyloid was found to be of the protein AA or secondary type. Current research into the pathogenesis of secondary amyloidosis centres on the mechanisms whereby protein AA is derived from the presumed precursor molecule, protein SAA, which is a normal acute-phase reactant.

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