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Is the guinea-pig (Cavia porcellus) a rodent?
Comp. Biochem. Physiol. Vol. 107B, No. 2, pp. 179-182, 1994 Copyright© 1994 Elsevier Science Ltd Printed in Great Britain. All rights reserved 03054)491/94 $6.00 + 0.00
Pergamon
MINI REVIEW Is the guinea-pig
(Cavia porcellus) a
rodent?
Tomoo Noguchi, Satoko Fujiwara, Sueko Hayashi and Haruhiko Sakuraba Department of Biochemistry, Kyushu Dental College, Kokura, Kitakyushu 803, Japan The Rodentia are traditionally divided into three extant suborders: the Sciuromorpha, the Myomorpha and the Hystricomorpha. The guinea-pig (Cavia porcellus) has been classified as a New World hystricomorph rodent. On the basis of the analysis of our previous studies on mammalian alanine:glyoxylate aminotransferase 1, we propose that the classification of the guinea-pig as a rodent is not correct. Key words: Alanine:glyoxylate aminotransferase; Cavia porcellus.
Comp. Biochem. Physiol. I07B, 179-182, 1994.
Introduction The Rodentia are traditionally divided into three extant suborders: the Sciuromorpha (squirrel-like rodents), the Myomorpha (ratlike rodents) and the Hystricomorpha (porcupine-like rodents) (Nowak and Paradiso, 1983). It has been reported that the guinea-pig (Cavia porcellus), classified as a New World hystricomorph rodent (Romer, 1968), shows anomalous biochemical properties in comparison with other rodents. For example, the guinea-pig cannot synthesize L-ascorbic acid because of the deficiency of L-gulono-?-Iactone oxidase, the terminal enzyme of the ascorbate synthesizing system (Burns, 1957; Chaudhuri and Chatterjee, 1969), and clofibrate and other hypolipidemic drugs do not elicit peroxisome proliferation and induction of fl-oxidation enzymes of fatty acids in the guinea-pig (Svoboda et al., 1967; Oesch et al., 1988; Lake et al., 1989). In this review, we propose that the classification of the guinea-pig as a rodent is not suitable on the basis of our previous studies on Correspondence to: T. Noguchi, Department of Biochemistry, Kyushu Dental College, Kokura, Kitakyushu 803, Japan. Tel. 93 582-1131; Fax: 93 582-6000. Received 21 June 1993; accepted 30 July 1993.
properties of alanine:glyoxylate aminotransferase 1 (AGTI) from different rodents, the only aminotransferase in animal peroxisomes. The enzyme is vitamin B6-dependent and catalyses irreversibly the transamination between L-alanine and glyoxylate. Properties of alanine: glyoxylate aminotransferase 1 (AGT1) We have compared physical, enzymatical and immunological properties of AGT1 from different mammals (Noguchi et al., 1978a,b, 1979, 1984; Noguchi, 1987; Noguchi and Takada, 1978a,b, 1979, 1980; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990). All AGTI from different mammals consists of two identical subunits with a molecular weight of about 40 kDa and is immunologically cross-reactive. On the basis of the analysis of our previous data, we noticed that the guinea-pig was remarkably different from other rodents in properties of AGTI: subcellular distribution, substrate specificity, response to hormone and immunological distance (amino acid sequence) of hepatic AGTI, subcellular distribution of
179
Tomoo Noguchi et al.
180
kidney A G T I and organ distribution of A G T I . These data are summarized in Table i. Subcellular distribution o f hepatic A G T I
(Noguchi et al., 1978a,b, 1979, 1984; Noguchi, 1987; Noguchi and Takada, 1978a,b, 1979, 1980; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990). Hepatic A G T I is located both in the mitochondria and in the peroxisomes in the rodents (rat, mouse, syrian hamster and chipmunk) but only in the peroxisomes of the guinea-pig. Subcellular distribution of hepatic A G T I varies among mammals; it is located in the peroxisomes in human, monkey and rabbit, in the mitochondria in dog and cat, and is not detected in pig and cow. Substrate specificity o f hepatic AGT1
(Noguchi et al., 1978a,b, 1979, 1984; Noguchi, 1987; Noguchi and Takada, 1978a,b, 1979, 1980; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990). Hepatic peroxisomal and mitochondrial AGT1 from the same rodent are not distinguishable in their physical, enzymatical and immunological properties. A G T I of the rodents (rat, mouse, Syrian hamster and chipmunk) show identical and very broad substrate specificity;
this is not so for the guinea-pig. With glyoxylate or pyruvate as amino acceptor, effective Lamino acids are alanine, serine, glutamine, methionine, asparagine, leucine, phenylalanine, tyrosine and histidine. Effective amino acceptors are glyoxylate and phenyipyruvate with L-alanine, and glyoxylate, pyruvate and phenyipyruvate with L-serine as amino donor. 2-Oxoglutarate, an effective amino acceptor of general aminotransferases, is inactive with each amino donor. In contrast, guinea-pig A G T ! shows only two enzyme activities, alanine: glyoxylate aminotransferase and serine: pyruvate aminotransferase activities. Substrate specificity of hepatic A G T I from other mammals (dog, cat, rabbit, monkey and human) is identical with that from the guineapig. Response o f (glucagon )
hepatic
AGT!
to
hormone
(Noguchi et al., 1978b; Noguchi, 1987; Takada and Noguchi, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990). In the rodents (rat, mouse, Syrian hamster and chipmunk) except for the guinea-pig, only the mitochondrial A G T I is induced by the injection in vivo of glucagon but the peroxisomal A G T I is not. In contrast, glucagon-inducible A G T I is not present in guinea-pig liver. On the other hand, the mitochondrial or peroxisomal
Table 1. Properties of alanine:glyoxylate aminotransferase I from different mammals Liver Kidney Subcellular Immunological Substrate Response to Subcellular distribution distance specificity glucagon distribution Rodents Rat Mouse Syrian hamster Chipmunk
Peroxisomes Mitochondria Peroxisomes Mitochondria Peroxisomes Mitochondria Peroxisomes Mitochondria Peroxisomes
0 0 32 32 79 79 Not determined Not determined 178
Broad Broad Broad Broad Broad Broad Broad Broad AGT and SPT
Not induced Induced Not induced Induced Not induced Induced Not induced Induced Not induced
Not detected Not detected Not detected
Not detected Peroxisomes Guinea-pig Other mammals Rabbit Peroxisomes Not determined AGT and SPT Not induced Mitochondria Mitochondria 164 AGT and SPT Not induced Mitochondria Dog 169 AGT and SPT Not induced Mitochondria Cat Mitochondria Monkey Peroxisomes 157 AGT and SPT Not examined Not detected 190 AGT and SPT Not examined Not detected Human Peroxisomes Subcellular distribution (Noguchi et al.. 1978a,b, 1979a,b, 1980, 1984, 1987; Noguchi and Takada, 1978a,b; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990), immunological distance (Takada and Noguchi, 1982b; Noguchi, 1987) substrate specificity(Noguchi et al., 1978a,b, 1979a,b, 1980, 1984, 1987; Noguchi and Takada, 1978a,b; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990), response to glucagon of liver AGTI (Noguchi et al., 1978b, 1987; Takada and Noguchi, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990), subcellular distribution (Noguchi and Takada, 1980; Hayashi and Noguchi, 1990) of kidney AGTI and organ distribution of AGT1 have been examined using different mammals. In cow and pig, alanine: glyoxylateaminotransferase 1 is detected neither in the liver nor in the kidney. Hepatic AGTI of rodents (rat, mouse, Syrian hamster and chipmunk) shows identical and broad substrate specificity(see text). In contrast, AGTI of other mammals, including guinea-pig shows only two enzyme activities of alanine:glyoxylate amintransferase and serine:pyruvate aminotransferase. Abbreviations: AGT, alanine:glyoxylate aminotransferase; SPT, serine:pyruvate aminotransferase.
Is the guinea-pig a rodent?
AGT1 of other mammals (dog, cat and rabbit), except for the rodent, are not affected by glucagon injection. These data suggest that liver peroxisomal AGTI of primates such as monkey and human are also not affected by glucagon injection.
Amino acid sequence of hepatic AGTI (Takada and Noguchi, 1982b; Noguchi, 1987) Immunological distances (ID) of heterotopic AGTI in the peroxisomes or mitochondria from different mammalian liver have been determined with rabbit antiserum against rat liver mitochondrial AGTI by microcompliment fixation. For a set of homologous variants of a given protein, ID has been found to correlate linearly with percentage amino acid sequence difference: ID = 5 x percentage of the difference in the amino acid sequence. Immunological distance of rat peroxisomal AGT1 is 0.0, and IDs of the peroxisomai and mitochondrial AGTI from the mouse liver are identical (ID = 32), suggesting that the peroxisomal and mitochondrial AGTI from the same mammalian liver have an identical amino acid sequence. ID of hamster mitochondrial AGTI is 79. ID of hamster peroxisomal AGTI, and the peroxisomal and mitochondrial AGTI of chipmunk have not been determined. Strikingly, ID of guinea-pig peroxisomal AGTI is 178, far different from those of other rodent AGT1. These data suggest that the amino acid sequence of guinea-pig proxisomal AGTI is very different from those of other rodent AGTI. Immunological distances of other mammalian AGTI (monkey, 157; human, 190; dog, 164; cat, 169) are similar to that of guinea-pig AGTI. Organ distribution of AGTI and subcellular distribution of kidney AGTI (Noguchi and Takada, 1980; Hayashi and Noguchi, 1990) Kidney is the only other tissue with alanine:glyoxylate aminotransferase activity in animals. AGTI is not detected in the kidney of the rodents except for the guinea-pig. In contrast, AGTI is present in the peroxisomes of the kidney in the guinea-pig. As described above, guinea-pig AGTI is strikingly different from other rodent AGTI in subcellular distribution, substrate specificity, response to hormone and amino acid sequence of hepatic AGTI, subcellular distribution of kidney AGTI and organ distribution of AGTI. It has been reported that the guinea-pig shows some anomalous biochemical properties in comparison with other rodents (rat and mouse) as described previously (Burns, 1957; Chaudhuri and Chatterjee, 1969; Svoboda et al., 1967; Oesch et al., 1988; Lake et al., 1989). These C'BPB 107/2--B
181
reports and our data suggest that the classification of the guinea-pig as a rodent is not suitable. In our studies, rat, mouse and hamster have been used as the Myomorpha, chipmunk as the Sciuromorpha, and guinea-pig as the Hystricomorpha. However, studies on the comparison of AGTI of the guinea-pig with further rodent species are required.
References Burns J. J. (1957) Missing step in man, monkey and guinea-pig required for the biosynthesis of L-ascorbic acid. Nature 180, 553. Chaudhuri C. R. and Chatterjee I. B. (1969) L-Ascorbic acid synthesis in birds: phylogenetic trend. Science 164, 435~,36. Hayashi S. and Noguchi T. (1990) Alanine: glyoxylate aminotransferase 1 is present in the peroxisomes of guinea-pig kidney. Biochem. biophys. Res. Commun. 166, 1467-1470. Hayashi S., Sakuraba H. and Noguchi T. (1989) Response of hepatic alanine: glyoxylate aminotransferase I to hormone differs among Mammalia. Biochem. biophys. Res. Commun. 165, 372-376. Lake B. G., Evans J. G., Gray T. J. B., K6r6si S. A. and North C. J. (1989) Comparative studies on nafenopin-induced hepatic peroxisome proliferation in the rat, Syrian hamster, guinea-pig and marmoset. Toxicol. Appl. Pharmac. 99, 148-160. Noguchi T. (1987) Amino acid metabolism in animal peroxisomes. In Peroxisomes in Biology and Medicine (Edited by Fahimi H. D. and Sies H.), pp. 234-243. Springer, Heidelberg. Noguchi T., Fujiwara S., Takada Y., Mori T., Nagano M., Hanada N., Saeki, E. and Oota Y. (1984) Enzymatic and immunological comparison of alanine: glyoxylate aminotransferase from different fish and mammalian livers. Comp. Biochem. Physiol. 77B, 279-283. Noguchi T., Minatogawa Y., Takada Y., Okuno E. and Kido R. (1978a) Subcellular distribution of pyruvate (glyoxylate) aminotransferase in rat liver. Biochem. J. 170, 173-175. Noguchi T., Okuno E., Takada Y., Minatogawa Y., Okai K. and Kido R. (1978b) Characteristics of hepatic alanine: glyoxylate aminotransferase in different mammalian species. Biochem. J. 169, 113-122. Noguchi T. and Takada Y. (1978a) Purification and properties of peroxisomal pyruvate (glyoxylate) aminotransferase from rat liver. Biochem. J. 175, 765-768. Noguchi T. and Takada Y. (1978b) Peroxisomal localization of serine: pyruvate aminotransferase in human liver. J. Biol. Chem. 253, 7598-7600. Noguchi T. and Takada Y. (1979) Peroxisomal localization of alanine: glyoxylate aminotransferase in human liver. Arch. Biochem. Biophys. 196, 645-647. Noguchi T. and Takada Y. (1980) Kidney alanine: glyoxylate aminotransferase isoenzymes; species distribution, subcellular distribution and properties. Comp. Biochem. Physiol. 65B, 133-138. Noguchi T., Takada Y. and Oota Y. (1979) Intraperoxisomal and intramitochondrial localization and assay of pyruvate (glyoxylate) aminotransferase from rat liver. Hoppe-Seyler's Z. Physiol Chem. 360, 919-927. Nowak R. M. and Paradiso J. L. (1983) Walker's Mammals of the World. Johns Hopkins University Press, Baltimore, MO. Oesch F., Hartmann R., Timms C. H., Strolin-Benedetti M., Dostert P., Worrier W. and Schladt L. J. (1988) Time-dependence and differential palmitoyl-CoA hydrolase, cytosolic and microsomal epoxide hydrolase after treatment
182
Tomoo Noguchi et al.
with hypolipidemic drugs. J. Cancer Res. Clin. Oncol. 114, 341-346. Romer A. S. (1968) Notes and Comments on Vertebrate Paleontology. University of Chicago Press, Chicago, IL. Svoboda D., Grady H. and Azarnoff D. (1967) Microbodies in experimentally altered cells. J. Cell Biol. 35, 127-152. Takada Y. and Noguchi T. (1982a) Subcellular distribution and physical and immunological properties of hepatic alanine: glyoxylate aminotransferase isoenzymes in different mammalian species. Comp. Biochem. Physiol. 72B, 597-604.
Takada Y. and Noguchi T. (1982b) The evolution of peroxisomal and mitochondrial alanine: glyoxylate aminotransferase I in mammalian liver. Biochem. biophys. Res. Commun. 108, 153-157. Takada Y. and Noguchi T. (1984) The effect of Vitamin B6 deficiency on alanine:glyoxylate aminotransferase isoenzymes in rat liver. Arch. Biochem. Biophys. 229, 1~. Takada Y. and Noguchi T. (1987) Aromatic amino acid:glyoxylate aminotransferase from rat liver. Meth. Enzymol. 142, 273-279.
Pergamon
MINI REVIEW Is the guinea-pig
(Cavia porcellus) a
rodent?
Tomoo Noguchi, Satoko Fujiwara, Sueko Hayashi and Haruhiko Sakuraba Department of Biochemistry, Kyushu Dental College, Kokura, Kitakyushu 803, Japan The Rodentia are traditionally divided into three extant suborders: the Sciuromorpha, the Myomorpha and the Hystricomorpha. The guinea-pig (Cavia porcellus) has been classified as a New World hystricomorph rodent. On the basis of the analysis of our previous studies on mammalian alanine:glyoxylate aminotransferase 1, we propose that the classification of the guinea-pig as a rodent is not correct. Key words: Alanine:glyoxylate aminotransferase; Cavia porcellus.
Comp. Biochem. Physiol. I07B, 179-182, 1994.
Introduction The Rodentia are traditionally divided into three extant suborders: the Sciuromorpha (squirrel-like rodents), the Myomorpha (ratlike rodents) and the Hystricomorpha (porcupine-like rodents) (Nowak and Paradiso, 1983). It has been reported that the guinea-pig (Cavia porcellus), classified as a New World hystricomorph rodent (Romer, 1968), shows anomalous biochemical properties in comparison with other rodents. For example, the guinea-pig cannot synthesize L-ascorbic acid because of the deficiency of L-gulono-?-Iactone oxidase, the terminal enzyme of the ascorbate synthesizing system (Burns, 1957; Chaudhuri and Chatterjee, 1969), and clofibrate and other hypolipidemic drugs do not elicit peroxisome proliferation and induction of fl-oxidation enzymes of fatty acids in the guinea-pig (Svoboda et al., 1967; Oesch et al., 1988; Lake et al., 1989). In this review, we propose that the classification of the guinea-pig as a rodent is not suitable on the basis of our previous studies on Correspondence to: T. Noguchi, Department of Biochemistry, Kyushu Dental College, Kokura, Kitakyushu 803, Japan. Tel. 93 582-1131; Fax: 93 582-6000. Received 21 June 1993; accepted 30 July 1993.
properties of alanine:glyoxylate aminotransferase 1 (AGTI) from different rodents, the only aminotransferase in animal peroxisomes. The enzyme is vitamin B6-dependent and catalyses irreversibly the transamination between L-alanine and glyoxylate. Properties of alanine: glyoxylate aminotransferase 1 (AGT1) We have compared physical, enzymatical and immunological properties of AGT1 from different mammals (Noguchi et al., 1978a,b, 1979, 1984; Noguchi, 1987; Noguchi and Takada, 1978a,b, 1979, 1980; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990). All AGTI from different mammals consists of two identical subunits with a molecular weight of about 40 kDa and is immunologically cross-reactive. On the basis of the analysis of our previous data, we noticed that the guinea-pig was remarkably different from other rodents in properties of AGTI: subcellular distribution, substrate specificity, response to hormone and immunological distance (amino acid sequence) of hepatic AGTI, subcellular distribution of
179
Tomoo Noguchi et al.
180
kidney A G T I and organ distribution of A G T I . These data are summarized in Table i. Subcellular distribution o f hepatic A G T I
(Noguchi et al., 1978a,b, 1979, 1984; Noguchi, 1987; Noguchi and Takada, 1978a,b, 1979, 1980; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990). Hepatic A G T I is located both in the mitochondria and in the peroxisomes in the rodents (rat, mouse, syrian hamster and chipmunk) but only in the peroxisomes of the guinea-pig. Subcellular distribution of hepatic A G T I varies among mammals; it is located in the peroxisomes in human, monkey and rabbit, in the mitochondria in dog and cat, and is not detected in pig and cow. Substrate specificity o f hepatic AGT1
(Noguchi et al., 1978a,b, 1979, 1984; Noguchi, 1987; Noguchi and Takada, 1978a,b, 1979, 1980; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990). Hepatic peroxisomal and mitochondrial AGT1 from the same rodent are not distinguishable in their physical, enzymatical and immunological properties. A G T I of the rodents (rat, mouse, Syrian hamster and chipmunk) show identical and very broad substrate specificity;
this is not so for the guinea-pig. With glyoxylate or pyruvate as amino acceptor, effective Lamino acids are alanine, serine, glutamine, methionine, asparagine, leucine, phenylalanine, tyrosine and histidine. Effective amino acceptors are glyoxylate and phenyipyruvate with L-alanine, and glyoxylate, pyruvate and phenyipyruvate with L-serine as amino donor. 2-Oxoglutarate, an effective amino acceptor of general aminotransferases, is inactive with each amino donor. In contrast, guinea-pig A G T ! shows only two enzyme activities, alanine: glyoxylate aminotransferase and serine: pyruvate aminotransferase activities. Substrate specificity of hepatic A G T I from other mammals (dog, cat, rabbit, monkey and human) is identical with that from the guineapig. Response o f (glucagon )
hepatic
AGT!
to
hormone
(Noguchi et al., 1978b; Noguchi, 1987; Takada and Noguchi, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990). In the rodents (rat, mouse, Syrian hamster and chipmunk) except for the guinea-pig, only the mitochondrial A G T I is induced by the injection in vivo of glucagon but the peroxisomal A G T I is not. In contrast, glucagon-inducible A G T I is not present in guinea-pig liver. On the other hand, the mitochondrial or peroxisomal
Table 1. Properties of alanine:glyoxylate aminotransferase I from different mammals Liver Kidney Subcellular Immunological Substrate Response to Subcellular distribution distance specificity glucagon distribution Rodents Rat Mouse Syrian hamster Chipmunk
Peroxisomes Mitochondria Peroxisomes Mitochondria Peroxisomes Mitochondria Peroxisomes Mitochondria Peroxisomes
0 0 32 32 79 79 Not determined Not determined 178
Broad Broad Broad Broad Broad Broad Broad Broad AGT and SPT
Not induced Induced Not induced Induced Not induced Induced Not induced Induced Not induced
Not detected Not detected Not detected
Not detected Peroxisomes Guinea-pig Other mammals Rabbit Peroxisomes Not determined AGT and SPT Not induced Mitochondria Mitochondria 164 AGT and SPT Not induced Mitochondria Dog 169 AGT and SPT Not induced Mitochondria Cat Mitochondria Monkey Peroxisomes 157 AGT and SPT Not examined Not detected 190 AGT and SPT Not examined Not detected Human Peroxisomes Subcellular distribution (Noguchi et al.. 1978a,b, 1979a,b, 1980, 1984, 1987; Noguchi and Takada, 1978a,b; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990), immunological distance (Takada and Noguchi, 1982b; Noguchi, 1987) substrate specificity(Noguchi et al., 1978a,b, 1979a,b, 1980, 1984, 1987; Noguchi and Takada, 1978a,b; Takada and Noguchi, 1982a,b, 1984, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990), response to glucagon of liver AGTI (Noguchi et al., 1978b, 1987; Takada and Noguchi, 1987; Hayashi et al., 1989; Hayashi and Noguchi, 1990), subcellular distribution (Noguchi and Takada, 1980; Hayashi and Noguchi, 1990) of kidney AGTI and organ distribution of AGT1 have been examined using different mammals. In cow and pig, alanine: glyoxylateaminotransferase 1 is detected neither in the liver nor in the kidney. Hepatic AGTI of rodents (rat, mouse, Syrian hamster and chipmunk) shows identical and broad substrate specificity(see text). In contrast, AGTI of other mammals, including guinea-pig shows only two enzyme activities of alanine:glyoxylate amintransferase and serine:pyruvate aminotransferase. Abbreviations: AGT, alanine:glyoxylate aminotransferase; SPT, serine:pyruvate aminotransferase.
Is the guinea-pig a rodent?
AGT1 of other mammals (dog, cat and rabbit), except for the rodent, are not affected by glucagon injection. These data suggest that liver peroxisomal AGTI of primates such as monkey and human are also not affected by glucagon injection.
Amino acid sequence of hepatic AGTI (Takada and Noguchi, 1982b; Noguchi, 1987) Immunological distances (ID) of heterotopic AGTI in the peroxisomes or mitochondria from different mammalian liver have been determined with rabbit antiserum against rat liver mitochondrial AGTI by microcompliment fixation. For a set of homologous variants of a given protein, ID has been found to correlate linearly with percentage amino acid sequence difference: ID = 5 x percentage of the difference in the amino acid sequence. Immunological distance of rat peroxisomal AGT1 is 0.0, and IDs of the peroxisomai and mitochondrial AGTI from the mouse liver are identical (ID = 32), suggesting that the peroxisomal and mitochondrial AGTI from the same mammalian liver have an identical amino acid sequence. ID of hamster mitochondrial AGTI is 79. ID of hamster peroxisomal AGTI, and the peroxisomal and mitochondrial AGTI of chipmunk have not been determined. Strikingly, ID of guinea-pig peroxisomal AGTI is 178, far different from those of other rodent AGT1. These data suggest that the amino acid sequence of guinea-pig proxisomal AGTI is very different from those of other rodent AGTI. Immunological distances of other mammalian AGTI (monkey, 157; human, 190; dog, 164; cat, 169) are similar to that of guinea-pig AGTI. Organ distribution of AGTI and subcellular distribution of kidney AGTI (Noguchi and Takada, 1980; Hayashi and Noguchi, 1990) Kidney is the only other tissue with alanine:glyoxylate aminotransferase activity in animals. AGTI is not detected in the kidney of the rodents except for the guinea-pig. In contrast, AGTI is present in the peroxisomes of the kidney in the guinea-pig. As described above, guinea-pig AGTI is strikingly different from other rodent AGTI in subcellular distribution, substrate specificity, response to hormone and amino acid sequence of hepatic AGTI, subcellular distribution of kidney AGTI and organ distribution of AGTI. It has been reported that the guinea-pig shows some anomalous biochemical properties in comparison with other rodents (rat and mouse) as described previously (Burns, 1957; Chaudhuri and Chatterjee, 1969; Svoboda et al., 1967; Oesch et al., 1988; Lake et al., 1989). These C'BPB 107/2--B
181
reports and our data suggest that the classification of the guinea-pig as a rodent is not suitable. In our studies, rat, mouse and hamster have been used as the Myomorpha, chipmunk as the Sciuromorpha, and guinea-pig as the Hystricomorpha. However, studies on the comparison of AGTI of the guinea-pig with further rodent species are required.
References Burns J. J. (1957) Missing step in man, monkey and guinea-pig required for the biosynthesis of L-ascorbic acid. Nature 180, 553. Chaudhuri C. R. and Chatterjee I. B. (1969) L-Ascorbic acid synthesis in birds: phylogenetic trend. Science 164, 435~,36. Hayashi S. and Noguchi T. (1990) Alanine: glyoxylate aminotransferase 1 is present in the peroxisomes of guinea-pig kidney. Biochem. biophys. Res. Commun. 166, 1467-1470. Hayashi S., Sakuraba H. and Noguchi T. (1989) Response of hepatic alanine: glyoxylate aminotransferase I to hormone differs among Mammalia. Biochem. biophys. Res. Commun. 165, 372-376. Lake B. G., Evans J. G., Gray T. J. B., K6r6si S. A. and North C. J. (1989) Comparative studies on nafenopin-induced hepatic peroxisome proliferation in the rat, Syrian hamster, guinea-pig and marmoset. Toxicol. Appl. Pharmac. 99, 148-160. Noguchi T. (1987) Amino acid metabolism in animal peroxisomes. In Peroxisomes in Biology and Medicine (Edited by Fahimi H. D. and Sies H.), pp. 234-243. Springer, Heidelberg. Noguchi T., Fujiwara S., Takada Y., Mori T., Nagano M., Hanada N., Saeki, E. and Oota Y. (1984) Enzymatic and immunological comparison of alanine: glyoxylate aminotransferase from different fish and mammalian livers. Comp. Biochem. Physiol. 77B, 279-283. Noguchi T., Minatogawa Y., Takada Y., Okuno E. and Kido R. (1978a) Subcellular distribution of pyruvate (glyoxylate) aminotransferase in rat liver. Biochem. J. 170, 173-175. Noguchi T., Okuno E., Takada Y., Minatogawa Y., Okai K. and Kido R. (1978b) Characteristics of hepatic alanine: glyoxylate aminotransferase in different mammalian species. Biochem. J. 169, 113-122. Noguchi T. and Takada Y. (1978a) Purification and properties of peroxisomal pyruvate (glyoxylate) aminotransferase from rat liver. Biochem. J. 175, 765-768. Noguchi T. and Takada Y. (1978b) Peroxisomal localization of serine: pyruvate aminotransferase in human liver. J. Biol. Chem. 253, 7598-7600. Noguchi T. and Takada Y. (1979) Peroxisomal localization of alanine: glyoxylate aminotransferase in human liver. Arch. Biochem. Biophys. 196, 645-647. Noguchi T. and Takada Y. (1980) Kidney alanine: glyoxylate aminotransferase isoenzymes; species distribution, subcellular distribution and properties. Comp. Biochem. Physiol. 65B, 133-138. Noguchi T., Takada Y. and Oota Y. (1979) Intraperoxisomal and intramitochondrial localization and assay of pyruvate (glyoxylate) aminotransferase from rat liver. Hoppe-Seyler's Z. Physiol Chem. 360, 919-927. Nowak R. M. and Paradiso J. L. (1983) Walker's Mammals of the World. Johns Hopkins University Press, Baltimore, MO. Oesch F., Hartmann R., Timms C. H., Strolin-Benedetti M., Dostert P., Worrier W. and Schladt L. J. (1988) Time-dependence and differential palmitoyl-CoA hydrolase, cytosolic and microsomal epoxide hydrolase after treatment
182
Tomoo Noguchi et al.
with hypolipidemic drugs. J. Cancer Res. Clin. Oncol. 114, 341-346. Romer A. S. (1968) Notes and Comments on Vertebrate Paleontology. University of Chicago Press, Chicago, IL. Svoboda D., Grady H. and Azarnoff D. (1967) Microbodies in experimentally altered cells. J. Cell Biol. 35, 127-152. Takada Y. and Noguchi T. (1982a) Subcellular distribution and physical and immunological properties of hepatic alanine: glyoxylate aminotransferase isoenzymes in different mammalian species. Comp. Biochem. Physiol. 72B, 597-604.
Takada Y. and Noguchi T. (1982b) The evolution of peroxisomal and mitochondrial alanine: glyoxylate aminotransferase I in mammalian liver. Biochem. biophys. Res. Commun. 108, 153-157. Takada Y. and Noguchi T. (1984) The effect of Vitamin B6 deficiency on alanine:glyoxylate aminotransferase isoenzymes in rat liver. Arch. Biochem. Biophys. 229, 1~. Takada Y. and Noguchi T. (1987) Aromatic amino acid:glyoxylate aminotransferase from rat liver. Meth. Enzymol. 142, 273-279.