Cellular and Subcellular Localization of Catalase in the Heart of Transgenic Mice

Abstract

Previous studies have described a cardiac-specific, catalase-overexpressing transgenic mouse model that was used to study myocardial oxidative injury. This study was undertaken to demonstrate cellular and subcellular localization of catalase in the hearts of transgenic mice. By the light microscopic immunoperoxidase method, we found that the overexpressed catalase was exclusively localized in cardiomyocytes. The ratios of immunoreactive cardiomyocytes in the heart were quite different among three transgenic lines examined but agreed with the elevated levels of catalase activity. In the cardiac blood vessels, positive cells were found in the walls of pulmonary veins and the vena cava, which consist of cardiomyocytes, but not in the pulmonary arteries, aorta, or cardiac valves. The electron microscopic immunogold method revealed that the elevated catalase was in sarcoplasm, nucleus, and peroxisomes, but not in mitochondria. In contrast to these distributions, catalase in the non-transgenic cardiomyocytes was in peroxisomes only. In addition, the number and size of peroxisomes in the transgenic cardiomyocytes were markedly increased, but no other ultrastructural changes were observed in comparison with those of non-transgenic mice. These results demonstrated that the elevated catalase in transgenic mouse heart is localized in cardiomyocytes and is distributed to peroxisomal and extraperoxisomal, but not mitochondrial, compartments.

Melatoninin Fare Böbrek Dokusunda Katalaz Enzimi Üzerine Etkisi

“…Our findings are parallel to the findings of Bingöl and Kocamış [17] , Morikawa et al [29] , Zhou and Kang [30] regarding presence of immunoreactivity in the cortex of the kidney, especially in proximal tubuli in the inner cortex portion and absence of reaction in distal tubuli, vascular endothelium and connective tissue. Kidney and especially proximal KORAL TAŞÇI, DEPREM, BİNGÖL ELİŞ YILDIZ, ASLAN [15] .…”

“…Similarly in their study, Morikawa et al [29] studied immunohistochemical localization of catalase in tissues of mammals and they reported that the reaction is in the cytoplasm of proximal tubuli cells of the kidney and that no specific reaction is present in distal tubule epithelium, connective tissue and blood vessels. Zhou and Kang [30] studied immunohistochemical localization of catalase in various tissues in transgenic mice and stated that there is cytoplasmic reaction in proximal tubuli of kidney. They have observed that this present reaction in proximal tubuli is weaker in the outer part of the cortex, stronger in the inner part and not present in distal tubuli, glomeruli, loop of Henle, collector tubes and medulla [30] .…”

“…Zhou and Kang [30] studied immunohistochemical localization of catalase in various tissues in transgenic mice and stated that there is cytoplasmic reaction in proximal tubuli of kidney. They have observed that this present reaction in proximal tubuli is weaker in the outer part of the cortex, stronger in the inner part and not present in distal tubuli, glomeruli, loop of Henle, collector tubes and medulla [30] . Immunohistochemical localization of catalase in geese liver has been reported to be mostly cytoplasmic and that some staining is present in the nuclei of a few hepatocytes [16] .…”

Post-ischemic early acidosis in cardiac postconditioning modifies the activity of antioxidant enzymes, reduces nitration, and favors protein S-nitrosylation

“…Yet, protection with PostC and AB prevents the reduction of the levels of the cytosolic Cu/Zn-SOD, which are otherwise reduced after I/R. The dichotomy on activities and levels between cytosolic and organelle confined enzymes [68], supports a role for compartmentalization of redox-environment in late reperfusion [52].…”

Kidney-specific Overexpression of Sirt1 Protects against Acute Kidney Injury by Retaining Peroxisome Function

“…Indeed, we have recently demonstrated that Sirt1 prevents apoptosis through the induction of catalase in HK-2 cells (7). Catalase is located in peroxisome fraction, which has been shown to promote peroxisome proliferation (26); the supplementation of peroxisome activator nafenopin results in a sustained increase in the number of peroxisomes with concomitant increases in catalase activity (27). Increased catalase therefore may eliminate H 2 O 2 within peroxisome, which possibly leads to the mitigation of the damages to peroxisome.…”