Amyloidosis in Caracals (Caracal Caracal)

Greunz, Eva Maria; Lemberger, Karin; Catinaud, Jérôme; Chenet, Baptiste; Linke, Reinhold P.; Bräsen, Jan Hinrich; Schmitz, Jessica; Bertelsen, Mads F.

doi:10.1638/2019-0005

Cited by 8 publications

(5 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The next step was to produce murine monoclonal antibodies against AA and SAA [20]. Their value and merit have been documented by the inventors Köhler and Milstein [38]. Monoclonal antibodies are represented by one amino acid sequence and have the value of a chemical reagent.…”

Section: Application Of Antibodies 41 Polyclonal and Monoclonal Antibodies Prepared Against Aa And Saamentioning

confidence: 99%

The Invariant Peptide Clusters of Serum Amyloid A Are Humoral Checkpoints for Vital Innate Functions as Probed by Monoclonal Antibodies, Including in Sepsis: Induction by Febrile Temperatures and Path of Discoveries

Linke¹

2020

Infectious Process and Sepsis

View full text Add to dashboard Cite

Serum amyloid A (SAA) is the most prominent acute-phase protein in vertebrates and its role in innate immunity has been reviewed. SAA functions are located on special regions of SAA, which are highly conserved in all vertebrates. 1. The discovery of the acute-phase nature of SAA before its existence was known by experimental murine AA amyloidosis induced by septic conditions. 2. Identification of the amyloid substance and its precursor.3. SAA changes its conformation and antigenic presentation when it is separated from HDL during the acute phase. Febrile temperatures activate SAA through the separation from HDL. There is a temperature-specific gradual separation of SAA isotypes or groups of isotypes from HDL. 4. Generic monoclonal AA antibodies mc4 and mc29 assist in elucidating selected SAAs' vital functions (as in defense, platelet functions, female propagation and others). 5. In a murine sepsis model, the monoclonals mc4 and mc29 can cause early death while the intact SAA can prevent this. Through this, a checkpoint ("stop and go") for survival was discovered. Generic monoclonals can also identify the life-saving structures of SAA's vital functions and those of other acute-phase proteins. This principle is essential for the production of novel drugs against sepsis and other innate-related diseases. 6. Some remarks follow.

show abstract

Section: Application Of Antibodies 41 Polyclonal and Monoclonal Antibodies Prepared Against Aa And Saamentioning

confidence: 99%

The Invariant Peptide Clusters of Serum Amyloid A Are Humoral Checkpoints for Vital Innate Functions as Probed by Monoclonal Antibodies, Including in Sepsis: Induction by Febrile Temperatures and Path of Discoveries

Linke¹

2020

Infectious Process and Sepsis

View full text Add to dashboard Cite

show abstract

“…Until now, stomach, gallbladder, urinary bladder, and heart, despite being investigated in other studies on feline systemic AA-amyloidosis, had never been reported as positive. While the stomach, the urinary bladder and the heart have been actually described in other felids, gallbladder deposits are reported only in humans and are still considered uncommon [7,8,[29][30][31]. Considering that in our case series, the gallbladder resulted positive in all the examined samples (6/6), we might explain this high number of positive gallbladders despite the absence of previous reports, by the rare investigation of this organ [10,12,13].…”

Section: Plos Onementioning

confidence: 48%

Histological evaluation of the distribution of systemic AA-amyloidosis in nine domestic shorthair cats

Moccia,

Vogt,

Ricagno

et al. 2023

PLoS ONE

View full text Add to dashboard Cite

Amyloidosis is a group of protein-misfolding disorders characterized by the accumulation of amyloid in organs, both in humans and animals. AA-amyloidosis is considered a reactive type of amyloidosis and in humans is characterized by the deposition of AA-amyloid fibrils in one or more organs. In domestic shorthair cats, AA-amyloidosis was recently reported to be frequent in shelters. To better characterize this pathology, we report the distribution of amyloid deposits and associated histological lesions in the organs of shelter cats with systemic AA-amyloidosis. AA-amyloid deposits were identified with Congo Red staining and immunofluorescence. AA-amyloid deposits were then described and scored, and associated histological lesions were reported. Based on Congo Red staining and immunofluorescence nine shelter cats presented systemic AA-amyloidosis. The kidney (9/9), the spleen (8/8), the adrenal glands (8/8), the small intestine (7/7) and the liver (8/9) were the organs most involved by amyloid deposits, with multifocal to diffuse and from moderate to severe deposits, both in the organ parenchyma and/or in the vascular compartment. The lung (2/9) and the skin (1/8) were the least frequently involved organs and deposits were mainly focal to multifocal, mild, vascular and perivascular. Interestingly, among the organs with fibril deposition, the stomach (7/9), the gallbladder (6/6), the urinary bladder (3/9), and the heart (6/7) were reported for the first time in cats. All eye, brain and skeletal muscle samples had no amyloid deposits. An inflammatory condition was identified in 8/9 cats, with chronic enteritis and chronic nephritis being the most common. Except for secondary cell compression, other lesions were not associated to amyloid deposits. To conclude, this study gives new insights into the distribution of AA-amyloid deposits in cats. A concurrent chronic inflammation was present in almost all cases, possibly suggesting a relationship with AA-amyloidosis.

show abstract

“…In domestic cats, whereas the hereditary AA amyloidosis in Siamese and Abyssinian cats is common, 1,7 sporadic occurrences in other breeds are also frequently reported. 4,32 Aside from domestic cats, AA amyloidosis has been reported in various feline species, including cheetahs, 23,41 black-footed cats, 33 caracals, 8 and tigers. 26 In contrast, systemic amyloidosis other than AA amyloidosis is rare in feline species, with epidermal growth factor (EGF)-containing fibulin-like extracellular matrix protein 1–derived amyloidosis in a Tsushima leopard cat being the only reported non-AA systemic amyloidosis.…”

mentioning

confidence: 99%

Apolipoprotein C-III amyloidosis in white lions (Panthera leo)

Kobayashi,

Iwaide,

Fukui

et al. 2024

Vet Pathol

View full text Add to dashboard Cite

Apolipoprotein C-III (ApoC-III) amyloidosis in humans is a hereditary amyloidosis caused by a D25V mutation in the APOC3 gene. This condition has only been reported in a French family and not in animals. We analyzed a 19-year-old white lion ( Panthera leo) that died in a Japanese safari park and found renal amyloidosis characterized by severe deposition confined to the renal corticomedullary border zone. Mass spectrometry-based proteomic analysis identified ApoC-III as a major component of renal amyloid deposits. Amyloid deposits were also positive for ApoC-III by immunohistochemistry. Based on these results, this case was diagnosed as ApoC-III amyloidosis for the first time in nonhuman animals. Five additional white lions were also tested for amyloid deposition retrospectively. ApoC-III amyloid deposition was detected in 3 white lions aged 19 to 21 years but not in 2 cases aged 0.5 and 10 years. Genetic analysis of white and regular-colored lions revealed that the APOC3 sequences of the lions were identical, regardless of amyloid deposition. These results suggest that ApoC-III amyloidosis in lions, unlike in humans, may not be a hereditary condition but an age-related condition. Interestingly, lion ApoC-III has a Val30 substitution compared with other species of Panthera that have Met30. Structural predictions suggest that the conformation of ApoC-III with Met30 and ApoC-III with Val30 are almost identical, but this substitution may alter the ability to bind to lipids. As with the D25V mutation in human ApoC-III, the Val30 substitution in lions may increase the proportion of free ApoC-III, leading to amyloid formation.

show abstract

Amyloidosis in Caracals (Caracal Caracal)

Cited by 8 publications

References 30 publications

The Invariant Peptide Clusters of Serum Amyloid A Are Humoral Checkpoints for Vital Innate Functions as Probed by Monoclonal Antibodies, Including in Sepsis: Induction by Febrile Temperatures and Path of Discoveries

The Invariant Peptide Clusters of Serum Amyloid A Are Humoral Checkpoints for Vital Innate Functions as Probed by Monoclonal Antibodies, Including in Sepsis: Induction by Febrile Temperatures and Path of Discoveries

Histological evaluation of the distribution of systemic AA-amyloidosis in nine domestic shorthair cats

Apolipoprotein C-III amyloidosis in white lions (Panthera leo)

Contact Info

Product

Resources

About