Familial amyloidosis in cats: Siamese and Abyssinian AA proteins differ in primary sequence and pattern of deposition

被引:30
作者
Niewold, TA
Van der Linde-Sipman, JS
Murphy, C
Tooten, PCJ
Gruys, E
机构
[1] Inst Anim Sci & Hlth, ID, DLO, NL-8200 AB Lelystad, Netherlands
[2] Univ Utrecht, Dept Vet Pathol, Utrecht, Netherlands
[3] Univ Tennessee, Med Ctr, Dept Med, Knoxville, TN USA
来源
AMYLOID-INTERNATIONAL JOURNAL OF EXPERIMENTAL AND CLINICAL INVESTIGATION | 1999年 / 6卷 / 03期
关键词
feline AA-amyloidosis; Siamese cats; amino acid sequence;
D O I
10.3109/13506129909007328
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Familial AA amyloidosis is a hereditary trait in Abyssinian cats, with the kidney as the main target organ. The amino acid sequence of the amyloid A protein of the Abyssinian cat has been described earlier. Recently, familial amyloidosis has been found in Siamese cats, with the liver as the main target organ. In the present paper, we describe the complete amino amid sequence of the major constituent protein, of two Siamese cats. Siamese hepatic protein AA showed homology with, but was different from all feline SAA and AA sequences hitherto reported. Two substitutions (46Q-R and 52A-V) from the Abyssinian protein sequence were identified one of which (46Q-R) is a non-homologous substitution not found in mammalian SAA, but is present in two bird AA amyloid proteins. This shows the presence of an unique amyloidogenic SAA isotype in Siamese cats Both the Siamese and the Abyssinian sequence are amyloidogenic, thus making identification of amyloidogenic residues difficult. Apart from the apparent inherent amyloidogenicity of SAA, it can not be excluded that certain amino acid substitutions could enhance its amyloidogenicity but also could contribute to tissue predilection in amyloidosis.
引用
收藏
页码:205 / 209
页数:5
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