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AMYLOIDOSIS IN CAPTIVE EUROPEAN EASTERN BONGO (TRAGELAPHUS EURYCERUS ISAACI): PREVALENCE, PREDICTIVE FACTORS, ORGAN PREDILECTION, AND SERUM AMYLOID A CONCENTRATIONS
Abstract
Amyloidosis is frequently identified during postmortem examination of captive eastern bongo (Tragelaphus eurycerus isaaci) in the European Endangered Species Programme (EEP). However, its significance and etiopathogenesis are poorly understood. The objective of this study was to investigate the prevalence of amyloidosis within this population and identify potential predictive factors for the presence of disease. Postmortem reports obtained from 24 EEP institutions were analyzed and assessed for evidence of amyloidosis. Seventy-two individuals had histopathological assessment performed after gross postmortem examination and were included in the study. Further histopathological analysis was performed on Congo red-stained slides from 26 individuals, and organ predilection sites were identified. Immunohistochemical analysis was performed in six individuals to identify the type of amyloid present. Serum amyloid A (SAA) analysis was performed on blood samples from 34 individuals, and concentrations in affected and unaffected individuals were compared. Amyloidosis was reported in 26 animals (36%). The association between the presence of amyloidosis and sex, age, or body condition was not statistically significant. However, amyloidosis was not identified in any individuals under the age of 6 yr. The presence of chronic inflammatory conditions was the only statistically significant predictive factor for the presence of amyloidosis (P = 0.03). Chronic inflammatory conditions present included nephritis, enteritis, and pneumonia. The majority of affected animals presented with amyloid deposition in multiple organs, with the liver and kidneys being most commonly affected. Immunohistochemistry confirmed the presence of AA amyloid. The association between the presence of amyloidosis and SAA values measured on a single occasion was not statistically significant. This study identified a high prevalence of amyloidosis within the captive European eastern bongo population associated with chronic inflammatory conditions. Antemortem diagnosis of amyloidosis remains challenging, and this study indicates that SAA protein concentrations are not a reliable indicator for the presence of amyloidosis.
... Biomarkers of immune function have been growing in popularity for evaluation of both general health and reproductive fitness in wildlife species [43,[452][453][454][455][456]. Research in humans and domestic animal species has investigated the role of the immune system in normal reproductive processes [457,458], reproductive pathologies [459,460], and reproductive failure [461]. ...
Historically, reproductive health in wildlife species has been evaluated primarily via immunoassay detection of fecal and urinary steroid hormone metabolites. This combination of sample type, biomarker category, and assay has been preferred for decades due to the ease of assessing reproductive health through the evaluation of stable compounds in easily collected biological samples using a cost-effective method. Increasingly, beginning with high performance liquid chromatography (HPLC) and more recently with convergence chromatography and ultra HPLC coupled with mass spectrometry (MS), wildlife studies are incorporating more sensitive and specific high-throughput technologies for the assessment of not only steroid hormone metabolites but proteins as well. Of note, a comprehensive health evaluation requires the measurement of biological readouts that modulate reproduction such as: glucocorticoids, leptin, insulin, thyroid hormones, melatonin, the microbiome, and markers of inflammation. Emerging modulatory biomarkers of reproductive health include acute phase proteins, microRNAs, and reactive oxygen species. Several of these biomarkers require application of newer technologies such as LC-MS/MS and sequencing, which demonstrates the need for the field of wildlife reproductive biology to diversify from its reliance on immunoassays. Importantly, endocrine disrupting chemicals adversely affect many aspects of reproductive function and evaluation of these compounds requires high throughput technology such as LC-MS/MS. The application of sequencing, particularly Next Generation Sequencing of bulk RNA (RNA-Seq) and single cell RNA-Seq, is uncommon in studies of wildlife reproductive health. However, as the cost of these methods decreases and consortiums of wildlife researchers band together to raise funds in support of studies using these technologies, their use will become more routine. Future research should focus on integration of known biomarkers of related systems into comprehensive reproductive assessments and the development of new biomarkers which are sensitive, precise, and employ non-invasive methodologies for the assessment of reproductive health of wildlife species.
The term “amyloidosis” encompasses the heterogeneous group of diseases caused by the extracellular deposition of autologous fibrillar proteins. The global incidence of amyloidosis is estimated at five to nine cases per million patient-years. While amyloid light-chain (AL) amyloidosis is more frequent in developed countries, amyloid A (AA) amyloidosis is more common in some European regions and in developing countries. The spectrum of AA amyloidosis has changed in recent decades owing to: an increase in the median age at diagnosis; a percent increase in the frequency of primary AL amyloidosis with respect to the AA type; and a substantial change in the epidemiology of the underlying diseases. Diagnosis of amyloidosis is based on clinical organ involvement and histological evidence of amyloid deposits. Among the many tinctorial characteristics of amyloid deposits, avidity for Congo red and metachromatic birefringence under unidirectional polarized light remain the gold standard. Once the initial diagnosis has been made, the amyloid subtype must be identified and systemic organ involvement evaluated. In this sense, the ¹²³I-labeled serum amyloid P component scintigraphy is a safe and noninvasive technique that has revolutionized the diagnosis and monitoring of treatment in systemic amyloidosis. It can successfully identify anatomical patterns of amyloid deposition throughout the body and enables not only an initial estimation of prognosis, but also the monitoring of the course of the disease and the response to treatment. Given the etiologic diversity of AA amyloidosis, common therapeutic strategies are scarce. All treatment options should be based upon a greater control of the underlying disease, adequate organ support, and treatment of symptoms. Nevertheless, novel therapeutic strategies targeting the formation of amyloid fibrils and amyloid deposition may generate new expectations for patients with AA amyloidosis.
Amyloidosis refers to a group of protein misfolding diseases characterized by deposition of a particular amyloid protein in various organs and tissues of animals and humans. Various types and clinical forms of amyloidosis, in which the pathology and pathogenesis is diverse depending upon the underlying causes and species affected, are reported in domestic and wild animals. The clinical findings are also quite variable consequent to the variation of the tissues and organs involved and the extent of functional disruption of the affected organs in various animal species. The affected organs may be enlarged and exhibit variable pallor grossly, or the amyloid deposit may be discernible only after microscopic examination of the affected tissues. Amyloid appears as a pale eosinophilic homogenous extracellular deposit in tissues. However, microscopic examination and Congo red staining with green birefringence under polarized light are needed to confirm amyloid and differentiate it from other apparently similar extracellular deposits such as collagen and fibrin. Identifying the type of amyloid deposit needs immunohistochemical staining, ultrastructural characterization of the amyloid fibril, and if feasible also genetic studies of the involved species for clinical and prognostic purposes. This paper provides a concise review of the occurrence of amyloidosis in domestic and wild animals.
Generalized amyloidosis with predominant renal medullary amyloid deposition was found in four closely related Siberian tigers (Panthera tigris altaica) suffering from end stage kidney diseases. Only minimal to mild amounts of amyloid were deposited in various organs outside the kidneys with individually variable organ involvement. The Congo red staining affinity of amyloid deposits was sensitive to potassium permanganate oxidation. The deposits were further characterized as being of the amyloid-A (AA) type by immunohistochemistry using the mouse monoclonal antibody mc4 directed against a conserved region of the human AA-protein. A combination of immunohistochemistry and Congo red staining was much more sensitive for the diagnosis of amyloid deposits than Congo red staining alone. With this combination, even minimal amyloid deposits were detected that had been missed in the first reading using Congo-red-stained slides alone. Since no common primary cause was identified, the amyloidosis was classified as idiopathic generalized AA-amyloidosis with a potential familial predisposition.
Renal amyloidosis was diagnosed in 14 young Chinese Shar Pei dogs, all of which were related. Clinical signs were those of renal failure and included vomiting, anorexia, lethargy, polydipsia, polyuria, weight loss, and dehydration. Some dogs had a history of intermittent fever and joint swelling. Laboratory findings also were compatible with renal failure and included azotemia, hyperphosphatemia, low total CO2 content in serum, isosthenuria, proteinuria, and hypercholesterolemia. All dogs had medullary deposition of amyloid, and 9 of 14 (64%) had glomerular involvement. The remaining renal lesions were typical of end-stage renal disease. In some dogs, amyloid deposits were found in other tissues (eg, liver, spleen, stomach, small intestine, myocardium, lymph node, prostate gland, thyroid gland, and pancreas). Amyloid deposits were sensitive to potassium permanganate oxidation, suggesting the presence of amyloid protein AA.
Between January 1976 and September 1987 renal medullary amyloidosis (RMA) was diagnosed in 17 Dorcas gazelles; the necropsy prevalence rate was 17/32 (53%). The most severe amyloid deposits were in the renal medulla; glomeruli were spared. Renal cortical lesions of interstitial fibrosis and tubular atrophy and dilatation significantly correlated with RMA (P less than 0.01) and were considered to be secondary changes. There were varying degrees of lymphoplasmacytic inflammation and tubular cast formation which did not significantly correlate with RMA. Amyloid was confirmed histochemically and by electron microscopy and was identified as AA type by the permanganate method. Progressive renal failure was the cause of death or necessitated euthanasia in 7/17 (41%) gazelles. RMA in Dorcas gazelles does not appear to be familial. A high prevalence of chronic or recurring Actinomyces (Corynebacterium) pyogenes infections may be an important factor.
Abstract
Familial AA amyloidosis is a hereditary trait in Abyssinian cats, with the kidney as the main target organ. The amino acid sequence of the amyloid A protein of the A byssinian cat has been described earlier. Recently, familial amyloidosis has been found in Siamese cats, with the liver as the main target organ. In the present paper, we describe the complete amino amid sequence of the major constituent protein, of two Siamese cats. Siamese hepatic protein AA showed homology with, but was different from all feline SAA and AA sequences hitherto reported. Two substitutions (46QR and 524-Y) from the Abyssinian protein sequence were identified, one of which (46Q-R) is a non- homologous substitution not found in mammalian SAA, but is present in two bird AA amyloid proteins. This shows the presence of an unique amyloidogenic SAA isotype in Siamese cats. Both the Siamese and the Abyssinian sequence are amyloidogenic, thus making identification of amyloidogenic residues difficult. Apart from the apparent inherent amyloidogenicity of SAA, it can not be excluded that certain amino acid substitutions could enhance its amyloidogenicity but also could contribute to tissue predilection in amyloidosis.
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.
This impressive author team brings the wealth of advances in conservation genetics into the new edition of this introductory text, including new chapters on population genomics and genetic issues in introduced and invasive species. They continue the strong learning features for students - main points in the margin, chapter summaries, vital support with the mathematics, and further reading - and now guide the reader to software and databases. Many new references reflect the expansion of this field. With examples from mammals, birds, reptiles, fish, amphibians, plants and invertebrates, this is an ideal introduction to conservation genetics for a broad audience. The text tackles the quantitative aspects of conservation genetics, and has a host of pedagogy to support students learning the numerical side of the subject. Combined with being up-to-date, its user-friendly writing style and first-class illustration programme forms a robust teaching package.
The biological diversity of our planet is being depleted due to the direct and indirect consequences of human activity. As the size of animal and plant populations decrease, loss of genetic diversity reduces their ability to adapt to changes in the environment, with inbreeding depression an inevitable consequence for many species. This textbook provides a clear and comprehensive introduction to the importance of genetic studies in conservation. The text is presented in an easy-to-follow format with main points and terms clearly highlighted. Each chapter concludes with a concise summary, which, together with worked examples and problems and answers, emphasise the key principles covered. Text boxes containing interesting case studies and other additional information enrich the content throughout, and over 100 beautiful pen and ink portraits of endangered species help bring the material to life.
A retrospective histologic study was performed for 96 deceased bongo (Tragelaphus eurycerus) submitted to Northwest ZooPath from 1995 to 2015. Histologic data were assessed for associations with sex, age, cause of death/euthanasia, and affected organ systems. Female bongo lived significantly longer than males. Males were more likely to die from infectious causes (41.2%), whereas most females died from chronic noninfectious conditions (54.4%) and trauma/stress (28.1%). Of those that died from infectious disease, the respiratory tract was the most commonly affected organ system. The most common infectious agents included acid-fast bacteria and fungi. Chronic conditions included amyloidosis (31.0%), inanition/emaciation (23.8%), and neoplasia (21.4%). Of the 31 animals that died with amyloidosis, 58% appeared to be clinically affected, and amyloidosis was likely an underlying cause of death in 42% of the animals. The most commonly affected organs included the liver, kidneys, adrenal glands, and gastrotintestinal tract. Also noteworthy was a high prevalence of adrenal gland hyperplasia and neoplasia, cystic thyroid glands, and aspiration pneumonia, which were not consistently associated with a prior anesthetic event or other obvious predisposing cause.
Thirteen pronghorn antelope (Antilocapra americana) from a single captive herd at the Columbus Zoo and Aquarium underwent complete or partial necropsies between 1997 and 2016. Ten of the 13 animals had histologic evidence of amyloidosis resulting in a 77% prevalence. Histologic and ultrastructural changes were characterized in an attempt to determine the underlying cause of the amyloid. Amyloid detection was performed through histologic examination of hemotoxylin and eosin and Congo red-stained microscopic slides for all 13 animals. Transmission electron microscopy and mass spectrometry was performed on renal tissue from two animals. Pedigree analysis and retrospective investigation into the clinical histories was performed. Histologically, 9/10 animals had amyloid present in the kidneys, 8/10 in the liver, 9/10 in the spleen, 4/10 in the gastrointestinal tract, 3/10 in the adrenal glands, and 2/10 in the thyroid glands. Transmission electron microscopy demonstrated glomerular deposits consistent with amyloid. Mass spectrometry performed on renal specimens from two animals revealed the presence of serum amyloid A. Eight of the 10 animals diagnosed with systemic amyloidosis had a clinical history of haemonchosis (elevated fecal strongyle count), 5/10 were diagnosed with pneumonia postmortem, and 7/10 had postmortem findings consistent with negative energy balance. Serum amyloid A, and β and Î 3 globulin levels were evaluated in four cases of amyloidosis, and all were within normal ranges for healthy domestic cattle. It was possible that the herd's amyloidosis was associated with a hereditary defect that could be exacerbated by chronic inflammation. However, there was no significant association between the mean degree of relatedness and presence of amyloidosis. In conclusion, systemic amyloidosis in this captive population of pronghorn is common. It is likely reactive and secondary to underlying chronic inflammation caused by haemonchosis and/or pneumonia.
Leptospirosis is a re-emerging bacterial zoonosis. North-Central Italy is characterized by a geographic area that promote Leptospira circulation. Data on sero-epidemiological survey carried out from 2002 to 2016 in North-Central Italy were reported and discussed. Overall, 709 out of the 8488 (8.35%) tested sera were positive for Leptospira at the cut-off titer (1:100) and 218 (2.57%) at higher titer (≥1:400). The highest percentages of positivity was recorded for coypus (22.86%), swine (19.74%) and bovine (13.03%). Pomona and Australis resulted the serogroup more often detected, followed by Sejroe and Icterohaemorrhagiae; while, a low number of positive sera was detected for serogroups Ballum, Canicola and Tarassovi. Percentage of positive sera for each year slightly decreased from 2002 to 2008 and rose from 2009. High percentages of positive reactions were recorded in 2014 (17.23%), 2015 (19.61%) and 2016 (38.05%). In conclusion, the results of this investigation reported an increase of leptospirosis in North-Central Italy. Furthermore, several animals resulted infected as accidental hosts by unusual Leptospira serovars. These data could suggest a change in host range for some serovars, that may promote the adaptation to new hosts.
A questionnaire was sent to 39 European institutions holding greater kudus ( Tragelaphus strepsiceros ), in order to determine the causes of captive greater kudu mortality. All reported macroscopic lesions and histopathologic observations, as well as other information regarding individuals that died, were analyzed to determine the most affected body systems and causes of death. Overall response rate was 31%, and 131 individuals were included in the study. The most frequently affected body systems were the digestive system (47%), respiratory system (38%), musculoskeletal system (37%), and cardiovascular system (32%). Most frequent causes of death were infectious diseases (27%) and trauma/accidents (18%); the cause was undetermined in 28% of cases. Nutrition-related disorders were difficult to assess, but results highlight possible nutritional imbalances. This retrospective study represents the first overview of greater kudu mortality in a captive population.
Currently the only captive population of beira antelope (Dorcatragus megalotis) is held at the Al Wabra Wildlife Preservation, Qatar. An outbreak of a severe respiratory disease--fibrinous pleuropneumonia syndrome, most likely caused by Mycoplasma ovipneumoniae--led to a marked population decline. Reactive systemic inflammatory (AA) amyloidosis was noted as a chronic manifestation of the disease. Blood samples had been collected for biochemistry and hematology baseline values prior to the outbreak. Population-level changes were analyzed before and during the course of the outbreak in selected blood parameters (white blood cells [WBC], blood urea nitrogen [BUN], and creatinine). The annual population WBC increased and decreased concurrently with the population size, with a significant correlation between the two measures (R = 0.92; P = 0.001). Both BUN and creatinine values were higher during the outbreak. These values peaked at the same time as mortality, which was 1 yr after the WBC peak. These changes were interpreted as the transition from an acute disease with a primary respiratory manifestation into a chronic condition where renal amyloidosis led to chronic renal failure and death. Also, elevated liver values in diseased animals were attributed to amyloidosis. Parallels to a literature report on a lung disease complex caused by M. ovipneumoniae in bighorn sheep (Ovis canadensis) were found. Trends in population-level blood values of the beira antelopes implicate amyloidosis as a significant, long-term consequence of the putative Mycoplasma infection.
Amyloidosis has been described in a wide range of domestic and wild species and man. A 10-yr-old male Eastern (Mountain) Bongo (Tragelaphus eurycerus isaaci) was submitted for postmortem examination after a period of 24-hr malaise. Gross examination found evidence of biventricular cardiac hypertrophy, congestive heart failure, and focal pulmonary abscessation. Histologic changes in the heart were consistent with hypertrophic change. Amyloid deposits were found within the liver, kidney medulla, heart, adrenal cortex, and pituitary gland and were confirmed as reactive systemic amyloid (AA) by immunohistochemistry. The pulmonary abscessation was thought to be the stimulus for excessive serum amyloid associated protein production leading to the reactive systemic amyloidosis. Colloidal goiter was also identified as an incidental finding.
Acute phase proteins are liver-derived serum proteins, the concentration of which alters in response to infection or inflammation. Cytokines such as interleukin-6, interleukin-1 and tumour necrosis factor- stimulate the liver to produce haptoglobin (Hp), serum amyloid A (SAA), C-reactive protein (CRP), 1-acid glycoprotein (AGP) and fibrinogen (Fb) but limit the production of negative acute phase proteins such as albumin. There are interspecies variations in the pattern of response of the acute phase proteins but they are valuable as markers of inflammatory lesions providing diagnostic information for veterinary medicine.Advances have been made in the study of acute phase protein in pigs, dogs and cattle. In the pig, it is evident that CRP is a major reactant whereas Hp is a moderate acute phase reactant. The use of CRP for the diagnosis of inflammatory disease in dogs has been confirmed with studies relating the canine serum CRP concentration to haematological determination of inflammation. CRP assay in canine serum has been shown to confirm primary infectious or inflammatory conditions but can also detect secondary conditions where the primary condition is non-inflammatory. In cattle, the use of Hp assay is now established as a major aid to the diagnosis of infectious and inflammatory disease. Additional benefit to the diagnosis of disease can be provided by analysis of a profile of acute phase proteins such as a combined analysis of SAA, Hp and AGP. The circulating concentration of AGP is maintained at an increased level for a more extended period than that of SAA or Hp in chronic inflammatory conditions.A major advance would be made in the analysis of animal acute phase protein if internationally recognised standards of the proteins in each species were to become available.
After a survey of the most important literature on amyloidosis the results of the authors own studies on amyloidosis in the bovine kidney are reported. The macroscopical and microscopical features of the various types of bovine renal amyloidosis are described. In most cases predominantly medullary depositions occurred (types A, B, C and D). In a series of over 1000 cases only six kidneys with glomerular amyloid were found (type E). All these, however, contained some medullary amyloid as well. It is questionable whether the different types of kidney lesions contain different forms of amyloid or represent variants of the same disorder. Clinico-pathological studies may solve this problem.
Medullary amyloid may be a subclinical disease. In clinically normal slaughter cattle it occurred in 2.7% of 1326 animals. In clinically normal dairy cattle (including young animals) it occurred in 2.6% of 378 animals and the incidence appeared to increase with age. In the medullary amyloid deposits different amyloid-containing cell types were found. The intracellular amyloid was arranged in parallel fibrils and was localized in lysosomes. Induced phagocytosis of bovine amyloid by rat macrophages appeared to result in similar vacuoles, indicating that phagocytosis may occur in the bovine cells. In the literature parallel intralysosomal amyloid has been interpreted as formation of amyloid in these vacuoles.
An attempt is made to elucidate the pathogenesis of amyloidosis.
In bovine amyloid protein A (AA) amyloidosis, amyloid deposits are typically observed in the kidney and spleen at necropsy. To determine the distribution of amyloid deposits in cows affected with AA amyloidosis, we examined organs known to be sites of amyloid deposits that are also processed for human consumption in 14 cows: 11 with typical clinical symptoms (typical amyloidosis) and three with no typical clinical symptoms (atypical amyloidosis). We found unusually high amounts of amyloid deposits in the tongue and other organs in all 14 cows regardless of the presence or absence of clinical amyloidosis symptoms. Cows with typical amyloidosis had heavier amyloid deposits in the spleen and renal glomeruli than cows with atypical amyloidosis. From clinical symptoms and histological examinations, we found that cows with typical and atypical amyloidosis can be classified into two groups, class I and class II, according to the presence or absence of heavy amyloid deposits in the spleen and renal glomeruli. However, no significant differences were observed between the amyloid fibrils of class I and class II amyloidosis by electron microscopy and Western blot analysis.
Serum amyloid A (SAA), the precursor protein in inflammation-associated reactive amyloidosis (AA-type), is an acute phase reactant whose level in the blood increases in response to various insults. It is expressed in the liver, but its physiological role is not well understood. Recently, a broader view of SAA expression and function has been emerging. Expression studies show local production of SAA proteins in histologically normal, atherosclerotic, Alzheimer, inflammatory, and tumor tissues. Binding sites in the SAA protein for high density lipoproteins, calcium, laminin, and heparin/heparan-sulfate were described. Adhesion motifs were identified and new functions, affecting cell adhesion, migration, proliferation and aggregation have been described. These findings emphasize the importance of SAA in various physiological and pathological processes, including inflammation, atherosclerosis, thrombosis, AA-amyloidosis, rheumatoid arthritis, and neoplasia. In addition, recent experiments suggest that SAA may play a "housekeeping" role in normal human tissues.
Amyloidosis comprises a group of diseases characterized by the extracellular deposition of insoluble fibrillar proteins. This mechanism generates different clinical syndromes depending on the site and extent of organ involvement. Amyloidosis is classified into categories of systemic and localized disease. Systemic amyloidosis is further subdivided into a hereditary familial form (for example, ATTR amyloidosis), a reactive form (AA amyloidosis), dialysis-related (Abeta(2)M) amyloidosis and immunoglobulin light chain (AL) amyloidosis. Treatment can be symptomatic, directed at the affected organ, or can be directed at reducing the production of the abnormal proteins with different strategies. Despite advances in treatment, the prognosis is still poor and depends on the underlying disease as well as the type and degree of dysfunction in involved organs. Early diagnosis is essential because patients with advanced disease are generally unable to undergo intensive therapy. Patients with systemic amyloidosis often present to a rheumatologist not only because the disease can include musculoskeletal and articular symptoms but also because it can be associated with chronic rheumatic diseases. This Review discusses the clinical features of amyloidosis and its rheumatic manifestations. The various types of amyloidosis, as well their prognosis and treatment, are also presented.
Clinical and clinico-pathological observations were made on three cattle affected with generalized amyloidosis. The results obtained are as follows. 1. The main clinical symptoms of the three cattle were anorexia, continued watery diarrhea, edema of the subcutaneous tissue, and rapid emaciation. The clinical duration was 13 to 34 days. Prognosis was bad without any therapeutic effect in all the cattle. 2. The characteristic biochemical findings were advanced hypoproteinemia accompanied by hypoalbuminemia, hypobetaglobulinemia, hypogammaglobulinemia and hyperalphaglobulinemia. In the immunoelectrophoretic pattern of serum, precipitin lines were strong for alpha 1 lipoprotein and alpha 2 macroglobulin and mild for albumin and IgG. 3. Advanced renal proteinuria was shown by the urine which contained such protein components as albumin, alpha-, beta- and gammaglobulin. In the urinary sediment, there were renal epithelial cells, hyaline casts and leukocytes in all cases. 4. Severe amyloidosis was observed in all the affected cattle. Amyloid deposits were found in the wall of small blood vessels in almost all the organs, including the liver, spleen, pancreas, adrenal cortex, lymph nodes, alimentary tract and thyroid gland. The alimentary tract showed serious edematous changes in the submucosal tissue. In addition, there were multiple abscesses in the lungs (Case No.1), chronic mastitis and suppurative peritonitis (Case No.2) and chronic mastitis (Case No.3). 5. No incidental causes of generalized amyloidosis were unknown in any case. It was suggested that the disease might follow the chronic infections described above.
Acute phase proteins are serum proteins which increase in concentration during the acute phase response to inflammation or infection. The response occurs in all animals, but in different species the response of individual proteins can be significantly different. Of the numerous acute phase proteins which have been identified in humans, a number have been examined in cattle and dogs but usually on an individual basis with little reference to their part in the acute phase response. Biochemical, physiological and clinical investigations into haptoglobin, fibrinogen, alpha 1-proteinase inhibitor, ceruloplasmin, seromucoid and C-reactive protein of cattle and dogs have therefore been reviewed with the emphasis on their role in this response to tissue damage.
Generalized amyloidosis was diagnosed post-mortem in a mountain gazelle (Gazella gazella). To test whether the amyloid deposits consisted of amyloid-A fibril protein a series of monoclonal and polyclonal antibodies directed against amyloid-A fibril protein of different species was applied to formalin-fixed paraffin sections using the indirect immunoperoxidase technique. The immunohistochemical results showed a moderate cross-reaction of gazelle amyloid with human, murine, hamster, and canine amyloid-A fibril protein. A strong cross-reaction, however, was found with one of two monoclonal anti-human amyloid-A antibodies and with an antiserum against bovine amyloid-A fibril protein, the amyloid fibril protein of another ungulate. These results demonstrate the presence of amyloid-A fibril protein in the gazelle amyloid and illustrate the diagnostic value of cross-reacting anti-amyloid-A antibodies for the identification of amyloid-A-amyloidosis in species and in individuals in which amyloid has not yet been examined.
The tissue distribution of amyloid deposits was studied in 15 related Abyssinian cats with familial amyloidosis. There was interstitial medullary amyloidosis in the kidneys of all 15 cats but only 11 had detectable glomerular involvement. The thyroid glands, stomach and colon were affected in all cats examined. Most of the cats also had amyloid deposits in the small intestine, spleen, heart, adrenals, pancreas, liver, lymph nodes and bladder. In 50 per cent or fewer of the cats examined, there was involvement of the parathyroids, lung and gonads. The central nervous system was not involved in any of the 3 cats evaluated. In 8 of the cats, no concurrent inflammatory disease could be detected. The tissue distribution of amyloid deposits resembled that found in other breeds of domestic cats with systemic amyloidosis. Despite the wide tissue distribution of amyloid deposits, clinical signs were related to renal amyloidosis. Familial amyloidosis in the Abyssinian cat may represent a valuable spontaneous animal model for the study of Familial Mediterranean Fever in man and the pathogenesis of reactive amyloidosis in general.
The onset and course of disease in a captive herd of Rocky Mountain big- horn sheep (Otis camiademisis) were studied. Major clinical signs were diarrhea, persistent coughs, mucopurulent nasal discharges, loss of weight, poor pelage appear- ance, and delayed pelage shedding. Primary pathological findings in 16 of 17 deaths were related to pneumonia. Mycoplasmna argimiini, Pasteurella sp., and Streptococcus sp. were isolated and considered probable etiologic agents. Parasites were not considered to be a primary cause of the clinical signs or the lung disease observed. Hematological changes indicated the chronicity of the disease and had prognostic and limited diagnostic value. Amyloidosis was observed in seven animals, suggesting a high susceptibility of the bighorn to secondary amyloidosis.
The clinical and pathologic implications of leptospirosis caused by organisms of the Hebdomadis serogroup were tested on 8 pregnant cows. The animals were inoculated after their 5th month of pregnancy, 2 with serovar szwajizak and 6 with serovar hardjo. During the acute phase of the infection, the cows had mild signs of clinical illness; however, mastitis was observed in all cows that calved. One cow aborted, and 2 delivered premature and weak calves. By bacteriologic cultural examination, a short leptospiremic phase was observed. Leptospires were isolated from milk of 5 cows during early phases of mastitis; these isolations were obtained only when using solid media. Leptospiruria was determined by culture and direct examination. Only hardjo-inoculated cows had detectable urinary shedding which was observed to extend past 450 days in 1 cow. Leptospires were isolated from tissues of all cows and from 2 calves at necropsy. Interstitial nephritis was observed in all cows necropsied. Histologically, leptospires were demonstrated in silver-stained sections of kidney, liver, and lung of most calves. Leptospires were also observed in sections of kidney of all cows necropsied and in the cotyledons, placenta, and liver of some. Agglutinating titers were detected in the serum of cows as early as 4 days after inoculation and reached maximum titer (81,920) after 20 days. Significant serum titers persisted for the duration of the experiment only in hardjo-inoculated cows. At birth, all calves had no detectable agglutinins, but seroconverted within 24 hours; the serum titers were similar to those found in the dam's milk.
The influence of physical stress on the plasma concentration of the acute‐phase proteins serum amyloid‐A (SAA) and haptoglobin (Hp) was studied in 10 calves. Two different stress levels were created by housing two groups of five calves, each on different types of floor. The stress level was assessed by studying videotapes of the animals, and, subsequently, by quantifying the problems related with moving across the pens and the time the calves spent lying down and standing. Plasma concentrations of Hp, SAA, aldolase, and cortisol were measured in blood samples obtained by jugular venepuncture.
Plasma SAA concentrations were significantly (p<0.001) elevated in animals housed on the floor type associated with the highest level of physical stress, although the concentrations were within the normal range for healthy adult cattle. Hp concentrations were not elevated. The floor type did not alter the stress related biochemical variables aldolase and cortisol.
It is concluded that plasma SAA concentrations rise upon physical stress, whereas Hp concentrations do not change. The absence of a significant difference in aldolase or cortisol concentrations indicates that the difference in the level of neuro‐endocrine stress between the animals housed on the two floor types is only minimal. Consequently, SAA is suggested to be a sensitive variable to assess physical welfare in calves.
Ongoing disease surveillance of necropsied captive cheetahs (Acinonyx jubatus) (n = 141) revealed a high prevalence of renal amyloidosis (n = 54 [38%]; age 1 to 16 years). The prevalence increased from 20% in pre- 1990 necropsies to 70% of cheetahs necropsied in 1995. In 74% of the cheetahs with amyloidosis, renal failure was determined to be the sole or partial cause of death. Papillary necrosis was seen only in affected cheetahs and involved 25% of these animals. Amyloid was present predominantly in the medullary interstitium, with minimal glomerular involvement. The amyloid deposits were immunohistochemically identified as AA type using antisera to both human and canine protein AA. A high percentage (52%) of animals with renal amyloid also had subsinusoidal hepatic AA amyloid deposits. Inflammatory diseases were identified in 100% of affected cheetahs. The most common inflammatory disease was chronic lymphoplasmacytic gastritis. The prevalence and severity of gastritis was higher in cheetahs with amyloidosis, and the prevalence of severe gastritis increased from 16% to 43%, coinciding with the increase in prevalence of amyloidosis. These findings suggest that cheetahs have a high prevalence of systemic amyloidosis in response to inflammation and that renal amyloidosis is an increasingly significant cause of morbidity and mortality in captive cheetah populations. Factors of potential importance in the apparent high prevalence of AA amyloidosis in cheetahs are currently being investigated in our laboratories.
This study was designed to investigate the role of leptospirae in interstitial nephritis. Sixty-eight white-spotted kidneys and 30 grossly normal kidneys from slaughtered cattle were examined histologically and immunohistochemically for the presence of Leptospira interrogans antigens. The presence of L. interrogans antigens was found in 21 of 68 white-spotted kidneys and in four of 30 normal kidneys. In conclusion, the detected incidence of infection with L. interrogans was not high, but there was a relationship between the presence of interstitial nephritis and leptospiral antigens.
The association of inflammatory diseases such as traumatic reticuloperitonitis (TRP), mastitis, metritis, and pododermatitis with renal amyloidosis in cattle is poorly described.
Serum amyloid A (SAA) levels are elevated during inflammatory diseases, and renal amyloidosis is formed as a complication.
This study was conducted with 82 crossbred cattle with mastitis (n = 18 cows), metritis (n = 11 cows), TRP (n = 30 cows), and pododermatitis (n = 23 : 15 cows and 8 beef cattle). Ten clinically healthy cows served as controls. Methods: Hematological, urinary, and blood parameters, including SAA, were measured by an automated procedure provided with trade kits. Determination of amyloidal structures was made by histopathological examination of renal biopsy specimens.
At the end of this trial, amyloidosis was detected in 5 cows displaying typical nephrotic syndrome, with hypoproteinemia and proteinuria in combination with polyuria and weight loss. Furthermore, it was observed that cows with renal amyloidosis had significantly higher (P < .01) total leukocyte counts, serum and urine enzyme activities, and urea and creatinine concentrations, with lower serum total protein concentrations, when compared with animals without renal amyloidosis.
The incidence of AA amyloidosis in cattle in this study suggests that cattle with mastitis, metritis, and pododermatitis have a high prevalence of systemic amyloidosis in response to inflammation.
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Accepted for publication 11 August 2022