Chicken Joint Amyloid Protein is of the AA‐type. I. Characterization of the Amyloid Protein

Landman, W. J. M.; Sletten, K; Koch, C. A. M.; Tooten, P. C. J.; Gruys, E.

doi:10.1046/j.1365-3083.1996.d01-31.x

Cited by 32 publications

(29 citation statements)

References 34 publications

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“…The decision that these protein bands are the amyloid proteins of the AA amyloidotic animals was based on the results of the N-terminal amino acid sequence analysis of the bands (Table 2), the absence of protein bands in negative control tissues, and the size of the specific animal AA protein. 18,23,32,49,52 In the mice (case Nos. 1-6), hamsters (case Nos.…”

Section: Discussionmentioning

confidence: 99%

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An Ancillary Tool for the Diagnosis of Amyloid A Amyloidosis in a Variety of Domestic and Wild Animals

et al. 2005

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Abstract. Immunohistochemistry, the standard method for diagnosing amyloid A (AA) amyloidosis, is limited in animals because it requires a large array of animal-specific anti-AA antibodies, not commercially available. The Shtrasburg method (SH method) is a highly specific and sensitive technique, helping in the diagnosis and determination of AA amyloidosis in humans. The aim of this study is to determine whether the SH method is applicable in the diagnosis of AA amyloidosis in a variety of animals. Tissue samples were obtained from animals suffering from spontaneous or experimentally induced AA amyloidosis (mice, hamsters, guinea pigs, cheetahs, cats, cows, ducks, a dog, a goose, a chicken, and a turaco). Detection of the amyloid and quantitative evaluation were performed using Congo red staining, and specific AA typing was performed by the potassium permanganate technique. The studied tissues were subjected to the SH method, which confirmed the AA nature of the amyloid deposit, by displaying in polyacrylamide gel electrophoresis protein bands consistent with the molecular weight of the species-specific AA, in all the animals examined, except mice, hamsters, and guinea pigs. N-terminal analysis of these bands corroborated their AA origin. We conclude that the SH method may be used as an ancillary simple tool for the diagnosis of AA amyloidosis in a large number of domestic and wild animals. Moreover, our findings further increase the feasibility of applying this method in humans.

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Section: Discussionmentioning

confidence: 99%

“…3,9,[11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27]. In all, amyloidosis was diagnosed, and the amyloid quantity was evaluated using the regular Congo red (Bennhold's) method.…”

Section: Tissues From Animals With Natural Amyloidosismentioning

confidence: 99%

An Ancillary Tool for the Diagnosis of Amyloid A Amyloidosis in a Variety of Domestic and Wild Animals

et al. 2005

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“…In addition, the falcon sequence was compared with the five published sequences that have been determined from tissue amyloid protein and/or from the nucleotide sequences of ducks, geese, and chickens [27][28][29][30][31] and compared with humans [54].…”

Section: N-terminal Amino Acid Sequencementioning

confidence: 99%

“…The 8-23 segment represents a relatively variable region of avian AA when compared with the other more complete sequences of 109 amino acids of ducks and geese [27][28][29][30], of 106 amino acids in a duck [28] and 57 residues in a chicken AA protein (31). So, within the sequence from position 24 to the C-terminus, only one single amino acid exchange occurs at position 70 between ducks and geese (marked in red) ( Figure 6).…”

Section: N-terminal Amino Acid Sequencementioning

confidence: 99%