Thiaminase activity of crucian carp Carassius carassius injected with a bacterial fish pathogen, Aeromonas salmonicida subsp. salmonicida.
Dietary thiaminase I is a cause of thiamine deficiency in animals. The physiological significance of thiaminase in the organisms containing this enzyme is not known, nor are the factors causing variation in their thiaminase activity. Tests were performed to evaluate the effect a pathogen might have on thiaminase activity in fish, when analyzed both with a cosubstrate added (CATA tests) and no cosubstrate added (NCATA tests). Pyridine is known as a cosubstrate specific for thiaminase I activity that does not accelerate thiaminase II activity. Crucian carp Carassius carassius known to harbor thiaminase I activity were injected intramuscularly with live Aeromonas salmonicida, a pathogenic bacterium of fish. For comparison, other groups were injected with formalin-killed bacteria and phosphate-buffered saline, respectively; an untreated group of fish was kept as a control. The bacteria did not contain any thiaminase activity. Significantly higher thiaminase activities (CATA and NCATA) were measured in all tissues (whole blood, injected muscle, uninjected muscle, and whole fish homogenates) of fish injected with live bacteria than in the saline-injected and the uninjected groups. The thiaminase activity of blood and that in the injected, inflamed muscle tissue followed different allocation patterns in fish injected with live A. salmonicida. The amount of thiaminase I enzyme appeared to be elevated in the whole blood of injected fish in the absence of natural cosubstrate(s). The thiaminase activity of the injected, inflamed muscle suggested that both the amount of thiaminase enzyme and some yet-unidentified natural cosubstrate(s) were elevated. This suggests that in addition to the enzyme, some cosubstrate(s) of fish or pathogen origin play a regulatory role in the so-farunknown physiological significance of thiaminase I activity in vivo. It is suggested that the health of fish should be considered when searching for factor(s) affecting its thiaminase activity.
Wistbacka
Svante
S
Laboratory of Aquatic Pathobiology, Department of Biology, Abo Akademi University, BioCity, Artillerigatan 6, FIN 20520 Turku/Abo, Finland. swistbac@abo.fi
Lönnström
Lars-Gustaf
LG
Bonsdorff
Erik
E
Bylund
Göran
G
D048409:Aeromonas salmonicida / Q000502:physiology*; D019883:Alkyl and Aryl Transferases / Q000378:metabolism*; D000818:Animals; D002347:Carps / Q000378:metabolism*; D005393:Fish Diseases / Q000378:metabolism* / Q000382:microbiology; D016905:Gram-Negative Bacterial Infections / Q000378:metabolism / Q000382:microbiology / Q000662:veterinary*; D018482:Muscle, Skeletal / Q000378:metabolism / Q000473:pathology
D019883:Alkyl and Aryl Transferases; C022737:thiamin pyridinylase