Amyloid‐like renal lesions in a roughtail stingray <i>Dasyatis centroura</i> (Mitchill 1815)

Camus, A; Brown, Cathy A.; Field, Cara L.; McDermott, Alexa

doi:10.1111/jfd.12397

Cited by 3 publications

(2 citation statements)

References 14 publications

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“…Although there were chronic inflammatory lesions (fibrosis, infiltration of macrophages) in this case, no septicemia and widespread acute inflammatory lesions or neoplastic disease were observed. Amyloidosis has been reported rarely in elasmobranchs (Camus, Brown, Field, & McDermott, 2016) and some teleost fishes (Mashima, Cornish & Lewbart, 1997;Russell et al, 2014). In these previously reported cases, amyloid formation has been attributed to septicemic, neoplastic and idiopathic causes.…”

Section: Discussionmentioning

confidence: 95%

“…SAA has been identified in most vertebrates, including teleosts, but has yet to be identified in elasmobranchs (Uhlar & Whitehead, 1999). Amyloid P, which can make up 14% of the dry weight of amyloid deposits in mammals, has been identified in elasmobranchs (Robey, Tanaka & Liu 1983) and it has been suggested in the pathogenesis of one case (Camus, Brown, Field, & McDermott, 2016). On the other hand, 10 amyloid fibril protein types have been described in animals and the one of the most seen of these amyloid beta (Aβ) fibrils were observed in localized amyloidosis types (Sipe et al., 2012;Westermark et al., 2007).…”

Section: Discussionmentioning

confidence: 99%

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Ulucan¹,

Yüksel²

2020

Turk. J. Fish. Aquat. Sci.

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Amyloidosis is described as collection of extracellular proteins with a characteristic fibrillar form with electron microscopy, a typical X-ray diffraction pattern and a green reflection with Congo red affinity. Zebrafish is an appropriate model organism for studying developmental immunology for modeling many infectious disorders. We observed that localized amyloid-like deposition was in the peritoneal membrane which is showing greenish reflection in the polarized filter with Congo red staining and immuno-positive staining with primary antibody of amyloid precursor protein. Consequently, in this case report, we demonstrated that incidentally detected and rarely seen localized amyloid-like accumulation in a zebrafish.

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Untitled

Ulucan¹,

Yüksel²

2020

Turk. J. Fish. Aquat. Sci.

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Survey of amyloidosis cases among different free-living wild and zoo animals

Penticoff

Hipkiss

Hetak

et al. 2021

Amyloid

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Classification of amyloidosis and protein misfolding disorders in animals 2024: A review on pathology and diagnosis

Iwaide,

Murakami,

Sedghi Masoud

et al. 2024

Vet Pathol

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Amyloidosis is a group of diseases in which proteins become amyloid, an insoluble fibrillar aggregate, resulting in organ dysfunction. Amyloid deposition has been reported in various animal species. To diagnose and understand the pathogenesis of amyloidosis, it is important to identify the amyloid precursor protein involved in each disease. Although 42 amyloid precursor proteins have been reported in humans, little is known about amyloidosis in animals, except for a few well-described amyloid proteins, including amyloid A (AA), amyloid light chain (AL), amyloid β (Aβ), and islet amyloid polypeptide-derived amyloid. Recently, several types of novel amyloidosis have been identified in animals using immunohistochemistry and mass spectrometry–based proteomic analysis. Certain species are predisposed to specific types of amyloidosis, suggesting a genetic background for its pathogenesis. Age-related amyloidosis has also emerged due to the increased longevity of captive animals. In addition, experimental studies have shown that some amyloids may be transmissible. Accurate diagnosis and understanding of animal amyloidosis are necessary for appropriate therapeutic intervention and comparative pathological studies. This review provides an updated classification of animal amyloidosis, including associated protein misfolding disorders of the central nervous system, and the current understanding of their pathogenesis. Pathologic features are presented together with state-of-the-art diagnostic methods that can be applied for routine diagnosis and identification of novel amyloid proteins in animals.

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Amyloid‐like renal lesions in a roughtail stingray Dasyatis centroura (Mitchill 1815)

Cited by 3 publications

References 14 publications

Untitled

Untitled

Survey of amyloidosis cases among different free-living wild and zoo animals

Classification of amyloidosis and protein misfolding disorders in animals 2024: A review on pathology and diagnosis

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