Distribution of arginase in tissues of cat (Felis catus)

Journal of Feline Medicine and Surgery

Volumn 9, Issue 2, 2007, Pages 133-139

  Aminlari, Mahmoud ^a   Shahbazkia, Homayoon R ^a   Esfandiari, Azadeh ^a  

^a SHIRAZ UNIVERSITY   (Iran)

Author keywords

[No Author keywords available]

Indexed keywords

ARGINASE;

ANIMAL; ARTICLE; CAT; ENZYMOLOGY; GASTROINTESTINAL TRACT; KIDNEY; METABOLISM; SPECIES DIFFERENCE;

ANIMALS; ARGINASE; CATS; GASTROINTESTINAL TRACT; KIDNEY; SPECIES SPECIFICITY;

ANIMALIA; FELIS CATUS;

EID: 33947319822     PISSN: 1098612X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfms.2006.10.001     Document Type: Article

References (54)

1. Alican I., and Kubes P. A critical role for nitric oxide in intestinal barrier function and dysfunction. American Journal of Physiology 270 (1996) G225-G237
2. Aminlari M., and Vaseghi T. Arginase distribution in tissues of domestic animals. Compendium of Biochemical Physiology 103B (1992) 385-389
3. Aminlari M., Vaseghi T., Sajedianfard M.J., and Samsami M. Changes in arginase, aminotransferases and rhodanese in sera of domestic animals with experimentally induced liver necrosis. Journal of Comparative Pathology 110 (1994) 1-9
4. del Ara Rangel M., Gonzalez-Polo R.A., Caro A., del Amo E., Palomo L., Hernndez E., Soler G., and Fuentes J.M. Diagnostic performance of arginase activity in colorectal cancer. Clinics in Experimental Medicine 2 (2002) 53-57
5. Beidler L.M., and Smallman R.L. Renewal of cells within taste buds. Journal of Cell Biology 27 (1965) 263-279
6. Bonfoco E., Krainc D., Ankarcrona M., Nicotera P., and Lipton S.A. Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with n-methyl-d-aspartate or nitric oxide/superoxide in cortical cell cultures. Proceedings of the National Academy of Science USA 92 (1995) 7162-7166
7. Castillo L., Derojas T.C., Chapman T.E., Vogt J., Burke J.F., Tannenbaum S.R., and Young V.R. Splanchnic metabolism of dietary arginine in relation to nitric oxide synthesis in normal adult men. Proceedings of the National Academy of Science USA 90 (1993) 193-197
8. Cederbaum S.D., Yu H., Grody W.W., Kern R.M., Yoo P., and Lyer R.K. Arginase I and II: do their functions overlap?. Molecular Genetics and Metabolism 81 (2004) S38-S44
9. Davis P.K., and Wu G. Compartmentation and kinetics of urea cycle enzymes in porcine enterocytes. Compendium of Biochemistry and Physiology 119 (1998) 527-537
10. Dhanakoti S.N., Brosnan J.T., Herzberg G.R., and Brosnan M.E. Renal arginine synthesis: studies in vitro and in vivo. American Journal of Physiology 259 (1990) E437-E442
11. Elgun S., Kacmaz M., Sen I., and Durak I. Seminal arginase activity in infertility. Urology Research 28 (2000) 20-23
12. Elgun S., Keskinee A., Yilmaz E., Baltaci S., and Beduk Y. Evaluation of serum arginase activity in benign prostatic hypertrophy and prostatic cancer. International Urology and Nephrology 31 (1999) 95-99
13. Gilbertson T.A., Damak S., and Margolskee R.F. The molecular physiology of taste transduction. Current Opinions in Neurobiology 10 (2000) 519-527
14. Greenberg D.M. Enzymes of urea cycle. In: Boyer P.D., Lardy H., and Myrback K. (Eds). Enzymes. 2nd edn Vol 4 (1960), Academic Press, New York 257-267
15. Hakovirta H., Keiski A., Toppari J., Halmekyto M., Alhonen L., Janne J., and Parvinen M. Polyamines and regulation of spermatogenesis: selective stimulation of late spermatogonia in transgenic mice overexpressing the human ornithine decarboxylase gene. Molecular Endocrinology 7 (1993) 1430-1436
16. Heby O., and Emanuelsfon H. Role of the polyamines in germ cell differentiation and in early embryonic development. Medical Biology 59 (1981) 417-422
17. Hendriks W.H., Moughan P.J., and Tarttelin M.F. Urinary excretion of endogenous nitrogen metabolites in adult domestic cats using a protein free diet and the regression technique. Journal of Nutrition 127 (1997) 623-627
18. Ishii N., Ikenaga H., Carmines P.K., Aoki Y., Ogawa Z., Saruta T., and Suga T. High glucose augments arginase activity and nitric oxide production in the renal cortex. Metabolism 53 (2004) 868-874
19. Kepka-Lenhart D., Mistry S.K., Wu G., and Morris Jr. S.M. Arginase I: a limiting factor for nitric oxide and polyamines synthesis by activated macrophages?. American Journal of Physiology, Regulation, Integration and Comparative Physiology 279 (2000) R2237-R2242
20. Konarska L., and Tomaszewski L. Studies on arginase of the small intestine. I: Topographical distribution and some properties of the small intestine arginase in the rat. Biochemistry of Medicine 14 (1975) 250-262
21. Levillain O., Parvy P., and Hus-Citharel A. Arginine metabolism in cat kidney. Journal of Physiology 491 (1996) 471-477
22. Li X., Li W., Wang H., Cao J., Maehashi K., Huang L., Bachmanov A.A., Reed D.R., Legrand-Defretin V., Beauchamp G.K., and Brand G.J. Pseudogenization of a sweet-receptor gene accounts for cats' indifference toward sugar. PLoS Genetics 1 1 (2005) e3
23. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall A.J. Protein measurement with the folin phenol reagent. Journal of Biological Chemistry 193 (1951) 265-275
24. Luk G.D., Marton L.J., and Baylin S.B. Ornithine decarboxylase is important in intestinal mucosal maturation and recovery from injury in rats. Science 270 (1980) 195-198
25. Maarsingh H., Tio M.A., Zaagsma J., and Merus H. Arginase attenuates inhibitory non-adrenergic non-cholinergic nerve-induced nitric oxide generation and airway smooth muscle relaxation. Respiratory Research 6 (2005) 23-28
26. Mistry S.K., Zheng M., Rouse B.T., and Morris S.M. Induction of arginase I and II in cornea during herpes simplex virus infection. Virus Research 73 (2001) 177-182
27. Mori M., and Gotoh T. Regulation of nitric oxide production by arginine metabolic enzymes. Biochemistry and Biophysics Research Communications 275 (2000) 715-719
28. Morris J.G., and Rogers Q.R. Arginine: an essential amino acid for the cat. Journal of Nutrition 108 (1978) 1944-1953
29. Morris J.G., and Rogers Q.R. Why is the nutrition of cats different to that of dogs. Tijdschr Diergeneeskd 116 (1991) 64S-67S
30. Natelson S. Arginase. Techniques in Clinical Chemistry. 3rd edn (1971), Charlles C Thomas, Illinois, U.S.A 146-148
31. Nathan C. Inducible nitric oxide synthase: what differences does it make?. Journal of Clinical Investigation 100 (1997) 2417-2423
32. Porembska Z., Baranczyk A., and Jachimowicz J. Arginase isoenzymes in liver and kidney of some mammals. Acta Biochimica Polonica 18 (1971) 77-85
33. Porembska Z., Luboinski G., Chrzanowska A., Mielczarek M., Magnuska J., and Kuzma A.B. Arginase in patient with breast cancer. Clinica Chimica Acta 328 (2003) 105-111
34. Que L.G., Kantrow S.P., Jenkinson C.P., Piantadosi C.A., and Huang Y.C.T. Induction of arginase isoforms in the lung during hyperoxia. American Journal of Physiology 275 (1998) L96-L102
35. Ratner S. Enzymes of arginine and urea synthesis. Advances in Enzymology 39 (1973) 1-90
36. Ratner S., and Petrack B. The mechanism of arginine synthesis from citrulline in kidney. Journal of Biological Chemistry 200 (1953) 175-185
37. Reece W.O. The kidneys. In: Swenson M.J., and Reece W.O. (Eds). Dukes Physiology of Domestic Animals. 11th edn (1996), Cornell University Press 573-576 U.S.A.
38. Rogers Q.R., and Phang J.M. Deficiency of pyrroline-5-carboxylate synthase in the intestinal mucosa of the cat. Journal of Nutrition 115 (1985) 146-150
39. Russel K., Lobley G.E., Rawlings J., Millward D.J., and Harper E.J. Urea kinetics of a carnivore, Felis Silvestris Catus. British Journal of Nutrition 84 (2000) 597-604
40. Spector E.B., Rice S.C.H., Moedjono S., Bernard B., and Cederbaum S.D. Biochemical properties of arginase in human adult and fetal tissues. Biochemistry Journal 28 (1982) 165-175
41. Spencer T., and Filbin M.T. A role for cAMP in regeneration of the adult mammalian CNS. Journal of Anatomy 204 (2004) 49-55
42. Spolaris Z., and Bond J.C. Multiple molecular forms of mouse liver arginase. Archives in Biochemistry and Biophysics 260 (1988) 469-479
43. Tabor C.W., and Tabor H. Polyamines. Annual Reviews in Biochemistry 53 (1984) 749-790
44. Taneli F., Vatansever S., Ulman C., Yilmaz O., Giray G., Genc A., and Taneli C. The effect of spermatic vessel ligation on testicular nitric oxide levels and germ cell-specific apoptosis in rat testis. Acta Histochemica 106 (2005) 459-466
45. Vockley J.G., Jenkinson C.P., Shuklal H., Kern R.M., Groby W.W., and Cederbaum S.D. Cloning and characterization of the human type II arginase gene. Genomics 38 (1996) 118-123
46. Weiner C.P., Knowless R.G., Stegink L.D., Dawson J., and Moncada S. Myometrial arginase activity increases with advancing pregnancy in the guinea pig. American Journal of Obstetrics and Gynecology 174 (1996) 779-789
47. Williams K. Interaction of polyamines with ion channels. Biochemistry Journal 325 (1997) 289-297
48. Windmuller H.G., and Spaeth A.E. Metabolism of absorbed aspartate, asparagine and arginine by rat small intestine in vivo. Archives in Biochemistry and Biophysics 175 (1976) 670-676
49. Wu G. Intestinal mucosal amino acid catabolism. Journal of Nutrition 128 (1998) 1249-1252
50. Wu C.W., Chi C.W., Lin E.C., Lui W.Y., Peng F.K., and Wang S.R. Serum arginase level in patients with gastric cancer. Journal of Clinical Gastroenterology 18 (1994) 84-85
51. Wu G., Knabe D.A., Flynn N.E., Yan W., and Flynn S.P. Arginine degradation in developing porcine enterocytes. American Journal of Physiology 271 (1996) G913-G919
52. Yip M.C.M., and Knox W.E. Function of arginase in lactating mammary gland. Biochemistry Journal 127 (1972) 893-899
53. Zamecka E., and Porembska Z. Five forms of arginase in human tissues. Biochemical Medicine and Metabolic Biology 39 (1988) 258-266
54. Zoran D.L. The carnivore connection to nutrition in cats. Journal of the American Veterinary Medical Association 221 (2002) 1559-1567