Arginase expression in mouse embryonic development

Yu, Hong; Iyer, Ramaswamy K.; Yoo, Paul K.; Kern, Rita M.; Grody, Wayne W.; Cederbaum, Stephen D.

doi:10.1016/s0925-4773(02)00089-8

Cited by 21 publications

(28 citation statements)

References 14 publications

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“…The mucous gland epithelium was stained reddishpurple, whereas the serous salivary gland was stained blue-purple only by hematoxylin ( Figure 3A2). H&E staining was used for confirmation of leukocytes and other tissues, as demonstrated in our previous study (Yu et al 2002). …”

Section: Histochemistry and Cytochemistrymentioning

confidence: 99%

“…We recently reported the patterns of arginase isozyme expression in mouse brain and embryo (Yu et al 2001(Yu et al ,2002. We began with the idea from prior work in humans and rodents that AI was responsible primarily for urea synthesis and that AII was likely to be primarily responsible for the biosynthesis of ornithine, subsequently leading to the production of other biologically relevant molecules such as polyamine and glutamate or proline.…”

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confidence: 99%

“…AI was found only in human and mouse liver by Northern blotting analysis (Vockley et al 1996;Morris et al 1997) but was detected in mouse brain and embryos by in situ hybridization (ISH) techniques (Yu et al 2001(Yu et al ,2002. A possible explanation for this discrepancy is the higher sensitivity of ISH, which is capable of detecting mRNA in single cells and relating microscopic topological information to mRNA expression.…”

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confidence: 99%

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Widespread Expression of Arginase I in Mouse Tissues: Biochemical and Physiological Implications

Yoo

Aguirre

et al. 2003

J Histochem Cytochem.

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Arginase I (AI), the fifth and final enzyme of the urea cycle, detoxifies ammonia as part of the urea cycle. In previous studies from others, AI was not found in extrahepatic tissues except in primate blood cells, and its roles outside the urea cycle have not been well recognized. In this study we undertook an extensive analysis of arginase expression in postnatal mouse tissues by in situ hybridization (ISH) and RT-PCR. We also compared arginase expression patterns with those of ornithine decarboxylase (ODC) and ornithine aminotransferase (OAT). We found that, outside of liver, AI was expressed in many tissues and cells such as the salivary gland, esophagus, stomach, pancreas, thymus, leukocytes, skin, preputial gland, uterus and sympathetic ganglia. The expression was much wider than that of arginase II, which was highly expressed only in the intestine and kidney. Several co-localization patterns of AI, ODC, and OAT have been found: (a) AI was co-localized with ODC alone in some tissues; (b) AI was co-localized with both OAT and ODC in a few tissues; (c) AI was not co-localized with OAT alone in any of the tissues examined; and (d) AI was not co-localized with either ODC or OAT in some tissues. In contrast, AII was not co-localized with either ODC or OAT alone in any of the tissues studied, and co-localization of AII with ODC and OAT was found only in the small intestine. The co-localization patterns of arginase, ODC, and OAT suggested that AI plays different roles in different tissues. The main roles of AI are regulation of arginine concentration by degrading arginine and production of ornithine for polyamine biosynthesis, but AI may not be the principal enzyme for regulating glutamate biosynthesis in tissues and cells.

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Section: Histochemistry and Cytochemistrymentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Widespread Expression of Arginase I in Mouse Tissues: Biochemical and Physiological Implications

Yoo

Aguirre

et al. 2003

J Histochem Cytochem.

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“…These arginase isoforms differ in terms of tissue distribution, subcellular localization, immunologic cross-reactivity, and physiologic functions. During early developmental stages, Arg 1 is expressed predominantly in the peripheral nervous system, the digestive system and in tissue leukocytes, whereas Arg 2 is found only in the intestines (16). Cytosolic Arg 1 is involved in ammonia degradation in the urea cycle, and its absence in deficient patients leads to hyperammonemia.…”

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Aging alters the production of iNOS, arginase and cytokines in murine macrophages

Cecílio¹,

Costa²,

Simioni³

et al. 2011

Braz J Med Biol Res

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The limited amount of information on the primary age-related deficiencies in the innate immune system led us to study the production of inducible nitric oxide synthase (iNOS), arginase, and cytokines in macrophages of young (8 weeks old) and old (72 weeks old) female BALB/c mice. We first evaluated iNOS and arginase inducers on peritoneal (PMΦ) and bone marrow-derived (BMMΦ) macrophages of young BALB/c and C57BL/6 mice, and then investigated their effects on macrophages of old mice. Upon stimulation with lipopolysaccharide (LPS), resident and thioglycolate-elicited PMΦ from young mice presented higher iNOS activity than those from old mice (54.4%). However, LPS-stimulated BMMΦ from old mice showed the highest NO levels (50.1%). Identical NO levels were produced by PMΦ and BMMΦ of both young and old mice stimulated with interferon-γ. Arginase activity was higher in resident and elicited PMΦ of young mice stimulated with LPS (48.8 and 32.7%, respectively) and in resident PMΦ stimulated with interleukin (IL)-4 (64%). BMMΦ of old mice, however, showed higher arginase activity after treatment with IL-4 (46.5%). In response to LPS, PMΦ from old mice showed the highest levels of IL-1α (772.3 ± 51.9 pg/mL), whereas, those from young mice produced the highest amounts of tumor necrosis factor (TNF)-α (937.2 ± 132.1 pg/mL). Only TNF-α was expressed in LPS-treated BMMΦ, and cells from old mice showed the highest levels of this cytokine (994.1 ± 49.42 pg/mL). Overall, these results suggest that macrophages from young and old mice respond differently to inflammatory stimuli, depending on the source and maturity of the cell donors

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“…There is no arginase II in rodent islets, whereas exocrine tissue contains weak arginase I and no arginase II (37). Arginase I is widely expressed in mouse tissues, especially in the upper gastrointestinal tract, and is seen also during embryonic development in pancreas and is much more pronounced in glandular cells in early development (39). Studies with Western blots demonstrated that rat islets and RINm5F cells express mainly arginase I (37).…”

Section: Discussionmentioning

confidence: 99%

Arginase Increases Total Pancreatic and Islet Blood Flow in Anaesthetized Mice

Jansson

Bodin

Källskog

2007

Upsala Journal of Medical Sciences

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Background. Previous studies have demonstrated that the high basal pancreatic islet blood perfusion is crucially dependent on nitric oxide formation. Arginase can interfere with the formation of nitric oxide by limiting substrate availability. The aim of the present study was to evaluate the influence of arginase on islet blood perfusion in anasthetized mice.Methods. The blood perfusion of the pancreatic islets was measured with a microsphere technique in anaesthetized NMRI mice after administration of arginase.Results: Arginase administration increased both total pancreatic and islet blood flow to the same degree. Also adrenal blood flow was increased, whereas other organ blood flow values were unaffected.Conclusion. Arginase induces a paradoxical increase in pancreatic and islet blood flow, the reasons for which are still unknown.

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Arginase expression in mouse embryonic development

Cited by 21 publications

References 14 publications

Widespread Expression of Arginase I in Mouse Tissues: Biochemical and Physiological Implications

Widespread Expression of Arginase I in Mouse Tissues: Biochemical and Physiological Implications

Aging alters the production of iNOS, arginase and cytokines in murine macrophages

Arginase Increases Total Pancreatic and Islet Blood Flow in Anaesthetized Mice

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