Myocardial protein aggregates in pet guinea pigs. Issue 1 (January 2022)

• Record Type: Journal Article
• Authors: Southard, Teresa; Kelly, Kathleen; Armien, Anibal G.
• Is Part Of: Veterinary pathology. Volume 59:Issue 1(2022)
• Page Start: 157
• Page End: 163
• Publication Date: 2022-01
• Subjects: alpha B crystallin -- cardiovascular -- guinea pig -- porcupine -- chinchilla -- heart -- myofibrillary myopathy -- protein aggregate myopathy -- proteostasis; Veterinary pathology -- Periodicals; Pathology, Veterinary -- Periodicals; 636.089607
• DOI: 10.1177/03009858211042586
• Languages: English
• ISSNs: 0300-9858

Abstract

A retrospective study of guinea pigs submitted for necropsy revealed intracytoplasmic inclusions in the cardiomyocytes of 26 of 30 animals. The inclusions were found with approximately the same frequency in male and female guinea pigs and were slightly more common in older animals. In most cases, the animals did not have clinical signs or necropsy findings suggestive of heart failure, and the cause of death or reason for euthanasia was attributed to concurrent disease processes. However, the 4 guinea pigs with the highest inclusion body burden all had pulmonary edema, sometimes with intra-alveolar hemosiderin-laden macrophages, suggestive of heart failure. The inclusions were found in both the left and right ventricular myocardium, mainly in the papillary muscles, but were most common in the right ventricular free wall. No inclusions were detected in the atrial myocardium or in skeletal muscle. The inclusions did not stain with Congo red or periodic acid–Schiff. Electron microscopy revealed dense aggregates of disorganized myofilaments and microtubules that displaced and compressed the adjacent organelles. By immunohistochemistry, there was some scattered immunoreactivity for desmin and actin at the periphery of the inclusions and punctate actin reactivity within the aggregates. The inclusions did not react with antibodies to ubiquitin or cardiac myosin, but were variably reactive for alpha B crystallin, a small heat shock chaperone protein. The inclusions were interpreted as evidence of impaired proteostasis.