The distribution of amyloid deposits was histopathologically and immunohistochemically examined in 25 cows aged 5 to 10 years that had been diagnosed with systemic AA amyloidosis. This examination revealed that amyloid deposits were also present in the hypophysis, ovary, uterus, mammary gland and skeletal muscle, in addition to the liver, kidney, spleen, pancreas, thyroid gland, adrenal gland, gastrointestinal mucosa, heart, lung and lymph nodes. The examined cows tended to have chronic inflammations, including chronic mastitis (six cases) or chronic pneumonia (four cases), which is thought of as a causative agent of AA amyloidosis. In contrast, five cases did not exhibit any chronic inflammation.
"Amyloid is a pathologic substance deposited between cells in various tissues and organs of the body in a wide variety of clinical settings including chronic inflammatory and neoplastic processes (Johnson & Jamison 1984; DiBartola et al. 1989; Fernández et al. 2003). Amyloidosis was determined in cattle with mastitis, pneumonia, TRP, traumatic pericarditis, salpingitis, and metritis (Johnson & Jamison 1984; Yamada et al. 2006). Although amyloidosis was reported in sheep with gangrenous pneumonia, purulent polyarthritis, pseudotuberculosis and abdominal abscess (Ménsua et al. 2003), to the best of our knowledge amyloidosis has not been reported together with TRP (Ménsua et al. 2003). "
[Show abstract][Hide abstract] ABSTRACT: (The objective of this study was to describe the clinical, ultrasonographical, and pathological findings of traumatic reticuloperitonitis (TRP) with its complications in a flock of sheep. Thirteen sheep in a flock died within one month's duration before two sheep were admitted to the Firat University Veterinary Medical Teaching Hospital. Three additional dead sheep were submitted for necropsy. A tentative diagnosis of TRP on two of the sheep was made based on clinical and ultrasonographic findings. A needle perforating the reticulum was removed from each sheep by surgery. The two sheep improved after the surgery. The necropsy revealed fibrous adhesions and a fistular connection between the dorso-ventral face of the reticulum to diaphragma and pericardium with 3 cm syringe needles in the other three sheep. There were congophylic amyloid deposits in the glomerular tufts, Bowman capsule and vascular walls of the liver, kidneys and spleen. Additionally, there was centrilobular necrosis indicating heart failure.Taken together; TRP is rarely seen in sheep; however, TRP and its complications may cause economic losses in sheep flocks. Ultrasonographic examination of the reticular area in sheep may be used as an ancillary diagnostic technique.
Journal of Applied Animal Research 04/2015; DOI:10.1080/09712119.2015.1031786 · 0.44 Impact Factor
[Show abstract][Hide abstract] ABSTRACT: Acceleration of amyloid deposition by administration of amyloid fibrils and transmissibility of disease have been reported for several types of amyloidosis. Reactive amyloidosis (AA) occurs in a wide variety of domestic animal species and is characterized by amyloid deposition mainly in spleen, liver, and kidneys. Because the visceral organs of domestic animals have traditionally been used in Asian cuisines, it is important to examine whether dietary ingestion of the organs themselves (rather than purified amyloid fibrils) accelerates AA amyloid deposition. Herein, we show that murine AA amyloidosis develops rapidly after intraperitoneal or oral administration of purified amyloid fibrils or homogenates of amyloid-laden bovine liver. The amyloidosis development in mice was dependent on the concentration of amyloid fibrils or amyloidotic liver homogenates. We found that experimental murine AA amyloidosis was accelerated by dietary ingestion of both purified amyloid fibrils and tissue homogenates that contain amyloid fibrils. We also investigated livers of beef cattle and food chickens to examine whether they contain amyloid-enhancing factor activity. By microscopic examination of hematoxylin and eosin- and Congo red-stained sections, no amyloid deposition was detected in these livers, and no effective activity for experimental induction of AA amyloidosis in mice was detected in homogenates of these livers.
Amyloid: the international journal of experimental and clinical investigation: the official journal of the International Society of Amyloidosis 07/2008; 15(2):77-83. DOI:10.1080/13506120802005833 · 2.01 Impact Factor
[Show abstract][Hide abstract] ABSTRACT: We report the experimental amyloidosis associated with administration of bovine amyloid fibrils in rabbits afflicted by Sore Hock (SH), which is ulcerative pododermatitis. Two groups of SH-afflicted rabbits were subjected to five inflammatory stimulations at intervals of 4 days by intraepithelial injection of a mixture consisting of Freund's complete adjuvant and lipopolysaccharide. One group of rabbits was administered amyloid in conjunction with the last inflammatory stimulation and the other group was not. For additional control, two groups were designed. A third group consisted of rabbits without SH, which were subjected to five stimulations and were administered amyloid. A fourth group consisted of SH-afflicted rabbits, subjected to 0-4 stimulations and administered amyloid. Amyloid depositions were observed in SH-afflicted rabbits, which had been stimulated five times and given amyloid (18/18). In the 4th group, only one rabbit, which had been subjected to four stimulations, showed amyloid depositions. No amyloid depositions were observed in the other rabbits. These results suggest that bovine AA amyloid fibrils have an amyloid-enhancing factor-like effect on SH-afflicted rabbits.
Amyloid: the international journal of experimental and clinical investigation: the official journal of the International Society of Amyloidosis 07/2008; 15(2):84-8. DOI:10.1080/13506120802005882 · 2.01 Impact Factor
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