Sequential metabolic alterations in the myocardium during influenza and tularemia in mice.
Mice with generalized influenza or tularemia of similar lethality were studied in an effort to compare biochemical responses of the myocardium during infections of viral and bacterial etiology. A progressive loss of body weight characterized the course of both infections. Accompanying this, the myocardial content of protein and the activities of lactate dehydrogenase, citrate synthase, and cytochrome c oxidase all decreased. However, myocardial protein degradation appeared earlier and was more pronounced in influenza, and the protein changes were accompanied by a rapid decline of myocardial RNA. Activation of acid hydrolases, such as cathepsin D and beta-glucuronidase, occurred in tularemia but not in influenza, whereas leakage of beta-glucuronidase into the plasma occurred in both infections. Conversely, there was a considerably greater activation of myocardial catalase in influenza. These findings suggested that different control mechanisms or metabolic pathways were operative in the degradation of myocardial constituents in influenza as compared with tularemia. The absence of histological signs of myocarditis in either infection appeared to exclude any direct local effects of an inflammatory process on myocardial cells. Since the infections were of comparable lethality (based upon the inoculated dose of organisms), the observed differences in pattern and extent of metabolic responses of the myocardium to these infections may be attributed to different pathophysiological mechanisms evoked by the different microorganisms.
D000818:Animals; D001831:Body Temperature; D001835:Body Weight; D008297:Male; D051379:Mice; D009124:Muscle Proteins / Q000378:metabolism; D009206:Myocardium / Q000201:enzymology / Q000378:metabolism*; D009696:Nucleic Acids / Q000378:metabolism; D009929:Organ Size; D009976:Orthomyxoviridae Infections / Q000378:metabolism*; D014406:Tularemia / Q000378:metabolism*
D009124:Muscle Proteins; D009696:Nucleic Acids