Topic:Amyloidosis
Amyloidosis in horses is a condition characterized by the abnormal deposition of amyloid proteins in various tissues and organs, leading to impaired function and potential organ failure. In equines, amyloidosis is relatively rare but can have significant clinical implications when present. The condition arises when misfolded proteins aggregate into insoluble fibrils, which are then deposited extracellularly in tissues such as the liver, kidneys, and spleen. This deposition disrupts normal tissue architecture and function, potentially leading to clinical signs such as weight loss, edema, and organ dysfunction. Diagnosis is typically confirmed through biopsy and histopathological examination, revealing the characteristic amyloid deposits. This page compiles peer-reviewed research studies and scholarly articles that explore the pathophysiology, clinical presentation, diagnostic challenges, and management strategies for amyloidosis in horses.
Amyloid in the horse: a report of nine cases. Out of approximately 16,000 horses referred for clinical examination, nine had amyloidosis. Six of these horses had localised amyloid deposits in the wall of the nasal meatus and ventral turbinates associated with epistaxis. Horse 1 also developed malignant histiolymphocytic lymphosarcomas. The amyloid deposits were potassium permanganate-resistant and tryptophan-positive. Gel filtration of solubilised amyloid fibrils from Horse 1 revealed a major retarded fraction with an apparent molecular weight of 20 kD. This protein had an amino acid composition similar to human AL-amyloid proteins and ho...
AA amyloid-associated gastroenteropathy in a horse. Systemic amyloidosis involving the digestive tract is described in an 11-year-old Morgan stallion. The disease was characterized clinically by weight loss, ptyalism, anaemia, persistent mature neutrophilia, hypoalbuminaemia and hypergammaglobulinaemia. The D-xylose absorption test indicated malabsorption. Necropsy revealed oral, oesophageal and gastric ulcers and reddened segments of small bowel mucosa with scant haemorrhages. Microscopically, amyloid deposits were found throughout all tissue layers of the digestive tract, except the serosa. Deposits of amyloid were most apparent in the small ...
The amino acid sequence of an amyloid fibril protein AA isolated from the horse. The amino acid sequence of the amyloid fibril protein AA from horse was established from characterization of cyanogen bromide fragments, tryptic peptides, and a peptide derived from a digest with Staphylococcus aureus V8 proteinase. The protein was found to consist of 80 amino acid residues. Sequence homologies with protein AA from other species were very striking, and revealed an insertion of two amino acid residues between positions 72 and 73. In position 44, two amino acid residues were found which provide further evidence for a polymorphism in the amyloid fibril protein AA.
Characterization of amyloid protein AA and its serum precursor SAA in the horse. Amyloid was extracted from the liver of a horse that had developed amyloidosis after being used for several years for the production of antibodies to bacterial antigens. The amyloid fibrils were shown to be of the AA type. Two AA proteins with molecular weights of 9000 and 11,000 and with identical partial N-terminal amino acid sequences were identified. Marked structural homology with AA from other species including man was seen, although clear species-related antigenic specificity was observed. SAA isolated from an acute phase (septic abortion) horse serum was identical to AA with respect to...
Definition of diabetes mellitus. The nomenclature of human diabetes mellitus (DM) has been revised, and this classification has been accepted throughout the medical world and literature. The major categories of diabetes are: insulin-dependent DM, type I or IDDM; noninsulin-dependent DM, type II or NIDDM; secondary DM or type S; impaired glucose tolerance, IGT; gestational diabetes; and previous abnormality of glucose tolerance, PrevAGT. A review of the literature has shown that over half of the documented diabetic dogs, with a single medical diagnosis, appear to be type I, IDDM, with a substantial proportion being type S, and...
[Systemic cutaneous and subcutaneous amyloidosis in the horse]. A 9-year-old horse had numerous firm, painless nodules of the skin and subcutis. Moderately vascular granulation tissue with numerous uni- or multinuclear reticuloendothelial cells was in the nodules and the regional lymph nodes but not in the viscera. By using special stains and electron microscopy, widespread amyloid deposits, mainly in the cytoplasm of reticuloendothelial cells, were identified. Amyloid was probably produced within the reticuloendothelial cells, then expelled from the dying cell and deposited in the intercellular space.