ArticleThe Histochemical journal1998
Immunohistochemical localization of arginase II and other enzymes of arginine metabolism in rat kidney and liver.
Article in The Histochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 63 citations in OpenAlex.
- The Role of Urea Cycle Functional Studies in Preclinical Research.Journal of inherited metabolic disease · 2026Review
- Biochemistry, pharmacology, and in vivo function of arginases.Pharmacological reviews · 2025Review
- Metabolic reprogramming: A driver of cigarette smoke-induced inflammatory lung diseases.Free radical biology & medicine · 2021Review
- Hypoxia Induces Renal Epithelial Injury and Activates Fibrotic Signaling Through Up-Regulation of Arginase-II.Frontiers in physiology · 2021Article
- Is the Arginase Pathway a Novel Therapeutic Avenue for Diabetic Retinopathy?Journal of clinical medicine · 2020Review
- L-Norvaline, a new therapeutic agent against Alzheimer's disease.Neural regeneration research · 2019Article
- Arginase 1 promotes retinal neurovascular protection from ischemia through suppression of macrophage inflammatory responses.Cell death & disease · 2018Article
- Article
- Arginase-2 mediates renal ischemia-reperfusion injury.American journal of physiology. Renal physiology · 2017Article
- Pharmacokinetics and Pharmacodynamics of Promising Arginase Inhibitors.European journal of drug metabolism and pharmacokinetics · 2017Review
- Effects of the Hydroalcoholic Extract ofInternational journal of endocrinology and metabolism · 2017Article
- Arginase 2 promotes neurovascular degeneration during ischemia/reperfusion injury.Cell death & disease · 2016Article
- An Optimized Method for Protein Extraction from OCT-Embedded Human Kidney Tissue for Protein Quantification by LC-MS/MS Proteomics.Drug metabolism and disposition: the biological fate of chemicals · 2016Article
- Arginase inhibition augments nitric oxide production and facilitates left ventricular systolic function in doxorubicin-induced cardiomyopathy in mice.Physiological reports · 2014Article
- Arginase in retinopathy.Progress in retinal and eye research · 2013Review
- Effect of arginase II on L-arginine depletion and cell growth in murine cell lines of renal cell carcinoma.Journal of hematology & oncology · 2008Article
- Interpretation of plasma amino acids in the follow-up of patients: the impact of compartmentation.Journal of inherited metabolic disease · 2008Article
- Localization and differential expression of arginase II in the kidney of male and female mice.Pflugers Archiv : European journal of physiology · 2005Article
- Arginase acts as an alternative pathway of L-arginine metabolism in experimental colon anastomosis.Journal of gastrointestinal surgery : official journal of the Society for Surgery of the Alimentary TractArticle
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arginine is a precursor for the synthesis of urea, polyamines, creatine phosphate, nitric oxide and proteins. It is synthesized from ornithine by argininosuccinate synthetase and argininosuccinate lyase and is degraded by arginase, which consists of a liver-type (arginase I) and a non-hepatic type (arginase II). Recently, cDNAs for human and rat arginase II have been isolated. In this study, immunocytochemical analysis showed that human arginase II expressed in COS-7 cells was localized in the mitochondria. Arginase II mRNA was abundant in the rat small intestine and kidney. In the kidney, argininosuccinate synthetase and lyase were immunostained in the cortex, intensely in proximal tubules and much less intensely in distal tubules. In contrast, arginase II was stained intensely in the outer stripes of the outer medulla, presumably in the proximal straight tubules, and in a subpopulation of the proximal tubules in the cortex. Immunostaining of serial sections of the kidney showed that argininosuccinate synthetase and arginase II were colocalized in a subpopulation of proximal tubules in the cortex, whereas only the synthetase, but not arginase II, was present in another subpopulation of proximal tubules. In the liver, all the enzymes of the urea cycle, i.e. carbamylphosphate synthetase I, ornithine transcarbamylase, argininosuccinate synthetase and lyase and arginase I, showed similar zonation patterns with staining more intense in periportal hepatocytes than in pericentral hepatocytes, although zonation of ornithine transcarbamylase was much less prominent. The implications of these results are discussed.
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