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*
Graduate School of Science and Technology, Chiba University, 648 Matsudo, Matsudo, Chiba 271-8510, Japan;
Division of Food Science and Biotechnology, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan; and
**
School of Human Cultures, University of Shiga Prefecture, 2500 Hassakacho, Hikone, Shiga 522-8533, Japan
1To whom correspondence should be addressed. E-mail: atanabe{at}i.bekkoame.ne.jp.
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONMATERIALS AND METHODSEffect of high protein...Effect of STZ-induced diabetesRESULTSDISCUSSIONLITERATURE CITED |
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KEY WORDS: • 2-amino-3-carboxymuconate-6-semiardehyde decarboxylase • tryotophan-niacin metabolism • high protein diet • streptozotocin-diabetes • rats
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSEffect of high protein...Effect of STZ-induced diabetesRESULTSDISCUSSIONLITERATURE CITED |
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, 2-amino-3-carboxymuconate-6-semiardehyde (ACMS)2
decarboxylase (ACMSD; picolinic carboxylase, EC 4.1.1.45) catalyzes the decarboxylation of ACMS, which is generated from 3-hydroxyanthranilate (3-HA) by 3-HA 3,4-dioxygenase (EC 1.13.11.6), to 2-aminomuconate-6-semialdehyde (AMS). Subsequently, AMS is cyclized to picolinic acid spontaneously or is oxidized to 2-aminomuconate by AMS dehydrogenase (EC 1.2.1.32), which enters the tricarboxylic acid cycle via the glutarate pathway. ACMS can also be cyclized nonenzymatically to quinolinic acid, which is then modified by quinolinate phosphoribosyltransferase (or nicotinate-nucleotide pyrophosphorylase, EC 2.4.2.19) and metabolized further to NAD. Thus, de novo synthesis of NAD depends on ACMSD to a considerable extent. Moreover, quinolinate and picolinate, the productions of which are postulated to be affected by ACMSD, have been studied in some neuronal system disorders (1
–4
) and in the immune system in macrophages (5
,6
), respectively. The former compound may act as an excitotoxic agonist of the N-methyl-D-aspartate receptor (7
,8
). However, the contribution of ACMSD to these processes has not been investigated and is still unknown.
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). This suggests that the conversion of tryptophan to NAD takes place mainly in the liver because of its low ACMSD activity, and that an alteration of hepatic ACMSD activity may greatly affect the amount of NAD converted in that species.
Several nutritional factors can affect the activity of hepatic ACMSD in rats. The activity has been observed to increase upon feeding a high-protein (30–40% casein) or tryptophan-deficient diet (10
, 11
), and to decrease due to ingestion of polyunsaturated fatty acid (PUFA) (12
–14
). In contrast, in liver of streptozotocin (STZ)-induced diabetic rats, ACMSD activity is increased markedly, and the injection of insulin suppresses this elevation (15
–17
).
Recently, we have cloned the cDNA encoding rat ACMSD (18
). Using the sequence as a probe, the alterations in hepatic ACMSD activity and gene expression were investigated in rats fed a high-protein diet and also in STZ-induced diabetic rats.
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MATERIALS AND METHODS |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSEffect of high protein...Effect of STZ-induced diabetesRESULTSDISCUSSIONLITERATURE CITED |
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Rats were purchased from CLEA Japan (Tokyo, Japan) and housed in individual cages at 22 ± 1°C with a 12-h light:dark cycle (lights on, 0700–1900h). They were allowed free access to food and water until being killed by decapitation at the end of each experiment. All rats were killed between 0900 and 1100 h, and their livers were immediately perfused via the portal vein with ice-cold physiological saline solution (140 mmol/L NaCl) and excised. The liver samples were subjected to measurement of ACMSD activity and competitive reverse-transcription (RT)-polymerase chain reaction (PCR) analysis for determination of ACMSD mRNA expression. For the quantitative determination of glucose in plasma, blood samples were collected from the tail vein immediately before the rats were killed, and Glucose B-Test kit (Wako Pure Chemical Industries, Osaka, Japan) was used. The care and treatment of the rats were carried out according to the guidelines prescribed in Faculty of Horticulture, Chiba University and the National Institutes of Health Guide for the care and use of laboratory animals (19
).
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Effect of high protein diet |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSEffect of high protein...Effect of STZ-induced diabetesRESULTSDISCUSSIONLITERATURE CITED |
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Male Sprague–Dawley rats at the age of 4 wk were fed with a diet containing 20% casein (Table 1)
, as previously reported (10
). After this acclimation period of 7 d, they (body weight 130–138 g) were divided into three groups and fed 5% casein, 20% casein or 40% casein diets (Table 1)
for the next 11 d.
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Male Sprague–Dawley rats at the age of 4 wk were fed a 20% casein diet for 7 d. They were switched to a 40% casein diet and killed at 0, 1, 2, 4, 7 and 11 d after the diet change. One group was fed the 20% casein diet throughout the experiment.
Experiment 3.
Rats were acclimated to the 20% casein diet as in expts. 1 and 2 and then some were fed the 40% casein diet for 11 d, while others continued to consume the 20% casein diet. They were then fed the 20% casein diet and killed at 0, 1, 2, 5 and 7 d after the diet change. One group continued to consume the 40% casein diet.
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Effect of STZ-induced diabetes |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSEffect of high protein...Effect of STZ-induced diabetesRESULTSDISCUSSIONLITERATURE CITED |
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Male Wister rats (7-wk-old), fed a commercial CE-2 diet (CLEA Japan), which is adequate for normal growth, were used in this experiment. According to the supplier, 1 kg of the diet, had a calculated energy value of 14.4 MJ, includes 252 g of crude protein and 183 mg of niacin (the tryptophan content was not available). Diabetes was induced in the rats by a single intraperitoneal injection of STZ (50 mg/kg body), as previously reported (16
). On 0, 1, 2, 4, 8 and 14 d after the STZ-injection, rats were killed. Control, nondiabetic rats, injected with the vehicle (50 mmol/L citrate buffer, pH 4.5) in place of STZ, were killed on d 14.
Experiment 5.
The diabetic rats were produced by STZ, as described in expt. 4. One of the diabetic groups was treated with protamine zinc insulin (Shimizu Pharmaceutical, Shimizu, Japan; 2 U/head) subcutaneously every 12 h (0700 and 1900 h) beginning 4 d after the STZ injection (16
). The other diabetic group and the not diabetic group were injected with physiological saline in place of insulin. On d 14, all rats were killed. The initial (d 0) body weights of the rats were 280–300 g.
Experiment 6.
Beginning at 14 d after the STZ-injection, insulin treatment was initiated as described in expt. 5. Rats were killed at 0, 2, 7 and 18 d after the start of the insulin treatment. A diabetic group without insulin treatment and a nondiabetic group also were investigated.
Assay for ACMSD activity.
Livers were homogenized in the 3 volumes of ice-cold buffer, 50 mmol/L potassium phosphate buffer (pH 7.0) containing 140 mmol/L potassium chloride, 5 mmol/L 2-mercaptoethanol, 1 mmol/L dithiothreitol, 1 mmol/L EDTA-2Na and 1 mmol/L phenylmethanesulfonyl fluoride, with a Potter-Elvehjem homogenizer. The homogenate was centrifuged at 105,000 x g for 1 h at 4°C. The activity of ACMSD in the cytosolic fraction was determined as previously described (18
,21
).
Preparation of nucleic acids.
Total RNA was extracted from rat liver using SV Total RNA Isolation System (Promega Corp., Madison, WI). For the extraction of plasmid DNA, Wizard Plus SV Minipreps DNA Purification System (Promega Corp.) was used. To purify the PCR products from the agarose gel and PCR solution, QIAquick Gel Extraction Kit (QIAGEN GmbH; Hilden, Germany) and QIAquick PCR Purification Kit (QIAGEN GmbH) were used, respectively. For RT-PCR, 1 µg of liver total RNA was reverse-transcribed in a final volume of 20 µL by using first-strand cDNA Synthesis Kit for RT-PCR (AMV; Boehringer Mannheim Corp., Indianapolis, IN), and the solution was diluted to 100 µL with nuclease-free water after the reaction. The PCR solution contained 2.5 U/100 µL TaKaRa Ex Taq (Takara Shuzo, Kyoto, Japan), 200 µmol/L dNTPs, 0.5 µmol/L of each sense and antisense primer and other component (template or competitor) described below. The reactions were conducted at 94°C for 2 min followed by each PCR cycle. RNA and DNA concentrations of the preparations were evaluated by measuring A260 (the ratio of A260:A280 was between 1.7 and 2.0). Synthetic oligonucleotides for PCR primers were purchased from Sawady Technology (Tokyo, Japan).
Synthesis of competitors.
ACMSD and ß-actin competitors were synthesized by PCR using pGEM-T Easy plasmid DNA (Promega Corp.) as the template, and the following composite primers: 5'-CTA CCA AAG GAA TGG CCT GAT AGG TCG TTC GCT CCA AGC T-3' and 5'-TGG TCT CCG ATG GCA TTC CTA AGC CGT AGT TAG GCC ACC AC-3' were used for the ACMSD competitor, 5'-GTG GGC CGC CCT AGG CAC CAG AGG TCG TTC GCT CCA AGC T-3' and 5'-CTC TTT AAT GTC ACG CAC GAT TTC AGC CGT AGT TAG GCC ACC AC-3' were used for the ß-actin competitor (the sequences underlined were the complementary sequences in pGEM-T Easy’s DNA).
Each PCR, containing 0.25 µg of the plasmid DNA and 0.5 µmol/L of each primer in a final volume of 50 µL, was performed for 30 cycles of the program: denaturation for 30 s at 94°C, annealing for 30 s at 58°C and extension for 45 s at 72°C. Each PCR product was separated by electrophoresis on a 20 g/L agarose gel, and extracted from the gel, and its concentration was determined. These cDNA fragments were used as competitors of ACMSD and ß-actin consisting of 246 bp and 249 bp, respectively.
Competitive RT-PCR.
The following primers were synthesized: A1, 5'-CTA CCA AAG GAA TGG CCT GAT-3'; A2, 5'-TGG TCT CCG ATG GCA TTC CTA-3'; B1, 5'-GTG GGC CGC CCT AGG CAC CAG-3'; B2, 5'-CTC TTT AAT GTC ACG CAC GAT TTC-3'.
For the determination of ACMSD mRNA, PCR was performed in a final volume of 50 µL, containing 10 µL of the diluted RT reaction sample, 0.01 attomol of ACMSD competitor and 0.5 µmol/L each A1 and A2 primer, for 45 cycles with a denaturation step for 30 s at 94°C, an annealing step for 30 s at 58°C and an extension step for 45 s at 72°C. For the determination of ß-actin mRNA, PCR was also performed in a final volume of 50 µL containing 2 µL of the diluted RT reaction, 1 attomol of ß-actin competitor and 0.5 µmol/L each B1 and B2 primer, and the program, as described above, was repeated for 35 cycles. The amplified cDNA derived from ACMSD and ß-actin mRNA consist of 571 bp and 540 bp, respectively. The PCR products were electrophoresed on a 20 g/L agarose gel containing ethidium bromide and UV-induced fluorescence intensities of bands were analyzed by Bio Image Intelligent Quantifier (B.I. Systems Corporation, Ann Arbor, MI). The values that were calculated by the application of the ratio of band intensity (target/competitor) to each calibration curve (described below) were estimated to be the amount of the mRNA in each sample. Moreover, to normalize the yields of RNA extraction and reverse transcription between samples, the amount of ACMSD cDNA was corrected with ß-actin cDNA in the same samples, and these corrected values were used to evaluate the ACMSD mRNA expression.
Construction of calibration curves.
The target cDNA of ACMSD and ß-actin were synthesized by RT-PCR using liver total RNA and the primers A1 and A2 for target ACMSD cDNA and B1 and B2 for target ß-actin cDNA. Each cDNA was amplified with the PCR protocol as described above. The PCR products were subjected to agarose gel electrophoresis, and extracted from the gel. The extracted products were subcloned into pGEM-T Easy vector (Promega Corp.) and Escherichia coli, JM109 High efficiency Competent Cells (Promega Corp.), were transformed with this vectors, according to the manufacturer’s instructions. Subsequently, using the prepared plasmids as template, target cDNAs of ACMSD and ß-actin were again amplified by PCR. Furthermore, these PCR products were purified and quantified for use as standard cDNA for the construction of calibration curves.
In the competitive PCR, using standard target cDNA and the competitor of ACMSD, the reaction was performed in a final volume of 50 µL containing 0.01 attomol of the competitor and 0.000610–10 attomol of the target standard. Using standard target cDNA and the competitor of ß-actin, competitive PCR was performed in a final volume of 50 µL containing 1 attomol of the competitor and 0.00381–1000 attomol of the standard target.
After electrophoresis of the PCR products, densitometric analysis was conducted. The ratios of the fluorescence intensities obtained from the target and the competitor cDNA bands were calculated and plotted on a log-log scale against the initial quantity of target cDNA in the PCR solutions (Fig. 2
). The resultant lines were then used to determine the amount of each target cDNA in the samples.
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Data are shown as means ± SD. For comparison of the three groups (in expts. 1 and 5), Tukey’s multiple-range test was used when significant differences were shown by one-way ANOVA. In the time-course studies, the changes within a group were analyzed as well. The differences between two groups killed on the same day were analyzed by Student’s unpaired t test if necessary. Differences with P < 0.05 were considered significant.
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RESULTS |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSEffect of high protein...Effect of STZ-induced diabetesRESULTSDISCUSSIONLITERATURE CITED |
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The final body weight of the rats fed 40% casein were lower (P < 0.05) than that of the 20% casein group. Hepatic ACMSD activity and mRNA expression were higher in the 40% casein-fed rats than in the other groups in expt. 1. In the rats fed 5% casein, body weight gain was suppressed entirely, and hepatic ACMSD activity was undetectable (Table 2)
.
|
). On d 0 and 11, the values were 0.141 ± 0.046 and 1.000 ± 0.217 mU/mg protein, respectively. ACMSD mRNA expression increased at d 1 and 2 after the diet switch and then tended to decrease at d 5 and 7 and then to increase at d 11 (Fig. 3)
. In the rats fed the 20% casein diet throughout the experiment, hepatic ACMSD activity and mRNA expression were unchanged (Fig. 3)
.
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). The elevated ACMSD mRNA expression in rats fed 40% casein was returned to normal within 3 d of switching to the 20% casein diet. A further decrease on d 5 was normalized by d 7 (Fig. 4)
.
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The rats injected with STZ (50 mg/kg) did not gain weight during the experiment, and their plasma glucose levels increased rapidly (in expt. 4; Fig. 5
). Hepatic ACMSD activity initially increased only slightly through d 4 but then markedly increased through14 d after STZ-injection. The values on d 0 and 14 were 0.074 ± 0.058 and 5.027 ± 0.821 mU/mg protein, respectively (Fig. 5)
. ACMSD mRNA expression of the rats had increased by d 2 and continued to increase gradually until d 14. Inconsistent with the changes in enzyme activity ACMSD mRNA did not increase dramatically between d 4 and 14 (Fig. 5)
. In the control rats (no STZ-injection), the activity and the mRNA expression of hepatic ACMSD were not altered (Fig. 5)
.
|
). However, the ACMSD mRNA expression in the insulin-treated diabetic group was not different from that in the nondiabetic control rats.
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). The elevated ACMSD activity of the diabetic rats was decreased gradually by insulin treatment but was still higher than normal (1.09 ± 0.38 vs. 0.37 ± 0.18 mU/mg protein, respectively; P < 0.05) even after they received insulin for 18 d (Fig. 6)
. Elevated ACMSD mRNA expression in the diabetic rats was reduced sharply on d 2 after insulin treatment began and then increased slightly on d 6. On d 18, it reached the normal level of non-diabetic rats (0.0304 ± 0.0050 and 0.0343 ± 0.0071, respectively; Fig. 6
). In the diabetic rats that were not treated with insulin, the increased ACMSD activity and mRNA expression were maintained (Fig. 6)
.
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSEffect of high protein...Effect of STZ-induced diabetesRESULTSDISCUSSIONLITERATURE CITED |
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–14
), hormones (22
–25
) and in experimental models of some diseases (15
–17
, 26
). In these previous studies, only the activity of ACMSD was measured but not its gene expression. This study shows the alteration of mRNA expression of the enzyme in rats using competitive RT-PCR. Elevations of both hepatic ACMSD activity and ACMSD mRNA expression were observed in rats fed a 40% casein diet and in STZ-induced diabetic rats. Insulin treatment suppressed the elevation of ACMSD activity and mRNA expression occurring in development of the diabetes (Table 5) and lowered the activity and mRNA expression, which had been maintained high levels in diabetes (Fig. 6)
. These results indicate that the increase and decrease of ACMSD activity were generally preceded by alterations in ACMSD mRNA expression.
ACMSD activity increased significantly by 2 d after the dietary change to a 40% casein diet and continued to increase gradually until d 11, while ACMSD mRNA expression showed a temporary increase on d 1–2 that declined slightly for a few days before it showed a sustained increase (Fig. 3)
. The elevation of ACMSD activity by STZ treatment was decreased gradually by administration of insulin until d 18, while the mRNA expression was oscillated with an initial decrease (Fig. 6)
. This pattern was also observed in another experiment (data not shown), indicating that insulin treatment blocked the effect of STZ treatment on ACMSD mRNA expression within 1 d. Furthermore, on d 18 after the start of the insulin treatment, the ACMSD activity was still higher than normal but the mRNA level had returned to normal (Fig. 6)
. This suggests that alteration of ACMSD mRNA expression is not reflected quickly in changes in the activity of the enzyme. The apparent biphasic response in ACMSD mRNA expression that was inconsistent with the change of the enzyme activity might be attributed to the transient activation/suppression of transcription or facilitation of mRNA degradation, followed by rapid restoration to the metabolic steady state by some homeostatic mechanisms.
The activities of many enzymes that regulate the metabolism of nutrients in liver are altered in rats fed high protein diet (27
,28
) and in STZ- or alloxan-induced diabetic rats (29
–31
). In this study, when the diet was shifted to 40% casein from 20% casein, hepatic ACMSD activity continued to increase for 11 d (Fig. 3)
. The activity of hepatic glucose-6-phosphatase (EC 3.1.3.9) was reported to increase to the maximum within 24 h by the dietary shift to a 90% casein diet from a 25% casein diet or a protein-free diet (32
). The dietary shift to a 90% casein diet from a protein-free diet increased the activities of hepatic pyruvate kinase (EC 2.7.1.40) and tyrosine aminotransferase (EC 2.6.1.5) to the maximum within 24 h and 3 d, respectively (27
, 32
). Moreover, hepatic ACMSD activity was induced more slowly than tyrosine aminotransferase in rats fed a 40% casein diet (10
). In the diabetic rats, the inductions of hepatic glucose-6-phosphatase and tryptophan 2,3-dioxygenase (EC 1.13.11.11) were facilitated (31
,33
–35
). Insulin administration to diabetic rats normalized the glucose-6-phosphatase activity within 24–48 h (33
). Thus, these previous results suggested that the responses of ACMSD to such stimulations might be slower than those of the enzymes described. The rate of increase or decrease in ACMSD appeared to be very slow compared with the alteration of carbohydrate metabolism, because plasma glucose concentration responded considerably earlier than ACMSD to the administration of STZ and insulin (Figs. 5
and 6)
. It has been reported that glucose-6-phosphatase, pyruvate kinase and tryptophan 2,3-dioxygenase activities transiently fluctuate under the stimuli of a change of the dietary protein content or STZ injection (27
,32
,34
,36
). In this study, a similar pattern was observed in ACMSD mRNA expression but not in the enzyme activity (Figs. 3
, 5
and 6
).
In expt. 6, even 18 d of insulin treatment did not restore the elevated ACMSD activity in the diabetic rats to the normal level while the body weight was increased adequately and the plasma glucose concentration was slightly lower than normal (Fig. 6)
. We presumed that prolongation of the treatment might be required to accomplish its restoration and that certain factors, e.g., other hormones and metabolic changes induced by STZ diabetes and delivery methods of insulin, might be involved. It has also been reported that hepatic glucose metabolism in diabetic rats was differentially affected by the two methods (subcutaneously or intraperitoneally) of insulin administration (37
).
In this study, the increase in hepatic ACMSD activity due to STZ was greater than that due to feeding a high protein diet in spite of the slight difference in ACMSD mRNA expression. In Figure 3
and 6
, the alteration ranges of the mRNA expression were similar but that of the activity were quite different. This indicates that the high protein diet and STZ treatment have different effects on the synthesis/degradation of ACMSD protein, or on activation process of ACMSD that are still unknown. Immunoblot analysis may be required to determine the amount of a protein corresponding to ACMSD. Egashira et al. (14
) have used that approach to investigate the alteration in ACMSD protein in rats using mouse antiserum against porcine ACMSD. However, in this study immunoblot analysis was not performed, because antibody against rat ACMSD with high specificity had not been obtained.
The recent cloning of rat ACMSD cDNA (18
) has allowed us to investigate the expression of ACMSD mRNA. It may now be possible to elucidate the mechanisms regulating this enzyme and related compounds under conditions of altered nutritional status and in certain conditions of morbidity.
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FOOTNOTES |
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Manuscript received 29 November 2001. Initial review completed 14 January 2002. Revision accepted 26 February 2002.
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LITERATURE CITED |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSEffect of high protein...Effect of STZ-induced diabetesRESULTSDISCUSSIONLITERATURE CITED |
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