Degradation and deposition of amyloid AA fibrils are tissue specific.
The complete amino acid sequences of two related AA proteins (Mr 9700 and 5300) derived from thyroid tissue from a patient, NOR, with the autosomal recessive disease familial Mediterranean fever were determined. Heterogeneity found at position 52 indicates these proteins are fragments of two allelic or isotypic SAA precursor molecules similarly degraded at unusual sites and deposited in the thyroid. Degradation appears to be tissue and/or enzyme(s) specific since the carboxy terminus of both fragments is Ala-Ala and is different from other AA amyloid fibrils extracted from various tissues in different patients. Electron micrographic studies reveal these fragments retain the characteristics of native amyloid fibrils under physiological conditions even after exposure to dissociating agents.
Department of Pathology, New York University Medical Center, New York 10016.
F
F
Prelli
M
M
Pras
B
B
Frangione
D000483:Alleles; D000595:Amino Acid Sequence; D000686:Amyloidosis / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D000685:Serum Amyloid A Protein / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D013961:Thyroid Gland / Q000378:metabolism; D014357:Trypsin
D010446:Peptide Fragments; D000685:Serum Amyloid A Protein; D014357:Trypsin