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2
*
Northern Advancement Center for Science and Technology, Colabo-Hokkaido, Sapporo 001-0021, Japan and
Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan
2To whom correspondence should be addressed. E-mail: hara{at}chem.agr.hokudai.ac.jp.
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ABSTRACT |
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 TOP ABSTRACT MATERIALS AND METHODSRESULTSDISCUSSIONLITERATURE CITED |
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KEY WORDS: • ß-conglycinin • peptone • cholecystokinin • food intake • gastric emptying
Excess food intake causes obesity, a serious risk factor in several lifestyle-related diseases, such as diabetes and hyperlipemia. Thus, the control of food intake has implications for leading a healthy life. Also, the suppression of increased appetite is very important for preventing the development of diabetes complications.
The gut hormone cholecystokinin (CCK) is produced in the so-called "I-cell" of enteroendocrine cells and is secreted into the bloodstream (1
). Endogenous CCK has some important physiologic roles, such as in pancreatic enzyme secretion (2
). Pharmacologic studies with exogenous CCK demonstrated that CCK suppresses food intake by inducing a feeling of satiety (3
–5
) and by reducing gastric emptying (5
,6
). Studies with CCK receptor antagonists indicated that a peripheral CCK receptor is involved in food intake suppression (3
,7
).
In rats, dietary protein and its hydrolysate stimulate CCK secretion (8
–10
). It is thought that CCK release by dietary protein is regulated by endogenous, trypsin-sensitive CCK-releasing peptides (11
). Dietary protein increases the bioavailability of the CCK-releasing peptides by competing for intraluminal trypsin. Further, some studies both in vivo and in vitro found that dietary protein and its peptide react on CCK cells directly to regulate CCK release (12
,13
).
We showed previously that plasma CCK levels increase after the intraluminal administration of guanidinated protein hydrolysate through a luminal trypsin activity–independent mechanism (14
). A further study showed that this peptic hydrolysate increases CCK release from dispersed rat intestinal mucosal cells through direct stimulation by the peptide (15
). We demonstrated recently that several dietary protein peptic hydrolysates (peptones) also stimulate CCK release by direct reaction on small intestinal mucosal cells (16
). In particular, we found that soy peptone stimulated CCK release more strongly than did other dietary peptones.
Feeding a raw soy protein diet has been shown to reduce body weight gain (17
), whereas the administration of soybean trypsin inhibitor decreased food intake and weight gain (18
). However, the effects of the major components of soy protein on the suppression of food intake and CCK release were not clearly defined.
Recently, it was found that feeding ß-conglycinin, one of the major components of soy protein, is effective in reducing plasma triglyceride and cholesterol levels in rats (19
). The purpose of the present study was to examine the effects of ß-conglycinin on food intake suppression and gastric emptying inhibition, and to explore the physiologic role of ß-conglycinin. We determined the involvement of endogenous CCK on food intake reduction with ß-conglycinin by using the selective CCK-A receptor antagonist, devazepide. We also demonstrated the direct interaction of ß-conglycinin peptone on intestinal mucosal cells to stimulate CCK release by in vitro experiments.
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MATERIALS AND METHODS |
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TOPABSTRACTMATERIALS AND METHODSRESULTSDISCUSSIONLITERATURE CITED |
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Isolation of ß-conglycinin from defatted soybean meal was performed using the method of Morita et al. (20
) with slight modifications. Briefly, defatted soybean flour was mixed with 30 mmol/L Tris-HCl buffer (pH 8.0) and centrifuged (19,000 x g, 20 min). The supernatant was brought to pH 6.0 and centrifuged again (12,000 x g, 20 min, 4°C); then the supernatant was adjusted to pH 4.8 to precipitate the 7S fraction. The crude 7S was dissolved in 35 mmol/L potassium of phosphate buffer, pH 7.6, containing 0.4 mol/L of NaCl and 10 mmol/L of 2-mercaptoethanol. Then, further fractionation with ammonium sulfate was performed to purify the ß-conglycinin fraction in the 7S fraction. The extract was dissolved in Milli-Q water (Millipore, Bedford, MA) and dialyzed. To confirm purity of the ß-conglycinin, SDS-PAGE was performed. The existence of three bands of subunits in the ß-conglycinin (
, ' and ß) (20
) was confirmed by the SDS-PAGE (Fig. 1
). The ß-conglycinin was hydrolyzed by pepsin at pH 1.8 and 37°C for 10 min as previously described (16
).
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Animal preparation.
Male Sprague-Dawley rats, weighing 250–330 g (Japan SLC, Hamamatsu, Japan) were kept in individual stainless steel cages in a room maintained at 23 ± 2°C and a 12-h light:dark cycle, and provided with a semipurified basal stock diet (Table 1
) during the acclimation period.
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Food intake studies. The duodenal cannula was connected to a 50-cm length of SP 28 polyethylene tubing that was passed through a protective steel pipe and filled with peptone solution in advance; ß-conglycinin peptone in distilled water was infused into the duodenum for 5 min at a flow rate of 0.5 mL/min. Ten minutes after the end of the infusion, the rats were given 15 g of basal stock diet for 30 or 60 min. After the ingestion period, the diet was collected and the weight of the uneaten portion was measured. The weight of the ingested diet was calculated by the subtraction of the weight of the uneaten portion from the weight of the total diet given. Each peptone solution (2 g/L) of ß-conglycinin, soy protein and wheat gluten (Wako Pure Chemical, Osaka, Japan) was also infused duodenally and the weight of the diet ingested by the rats in 1 h was measured.
To confirm the effects of the ß-conglycinin peptone-induced reduction of luminal trypsin activity on suppression of food intake, a camostat solution (0.25 mg/L) was also infused into the duodenum under the same conditions. We confirmed that 0.25 mg/L of camostat, a synthetic trypsin inhibitor, had the same inhibitory activity as 2 g/L of ß-conglycinin peptone, i.e., 
63% inhibition of trypsin activity, by a previously described method using benzoil-L-arginine p-nitroanilide (22
).
In a separate experiment, rats received a bolus intravenous injection of 500 µg/kg of the selective CCK-A receptor antagonist, devazepide, which was supplied by ML Laboratories, Liverpool, UK, or its vehicle (5% dimethyl sulfoxide/5% Tween 80/90% saline) 10 min before intraduodenal infusion of ß-conglycinin peptone, to determine the involvement of endogenous CCK on food intake with ß-conglycinin.
Plasma CCK levels after intraduodenal infusion of ß-conglycinin peptone.
ß-Conglycinin peptone solution (2 g/L), 0.25 mg/L camostat and distilled water were infused into the duodenum for 5 min at 0.5 mL/min. The portal blood was collected under anesthesia 45 min after the start of infusion. The plasma separated from the portal blood by centrifugation (20 x g, 20 min, 4°C) was stored at -40°C. Plasma CCK was extracted using a Sep-pak C18 cartridge (Waters, Milford, MA) and measured by bioassay using rat acini (22
). Synthetic CCK-8 was used as a standard, and CCK concentration in the supernatant was estimated as a CCK-8 equivalent.
Gastric emptying study.
Rats fitted with duodenal and gastric tubing were deprived of food overnight and water for 3 h before the experiment. The ß-conglycinin peptone solution (2 g/L) or distilled water was infused into the duodenum for 5 min at 0.5 mL/min. Fifteen or 30 min after the onset of infusion, 3 mL of phenol red (60 mg/L in saline) was infused into the stomach through the gastric cannula as a nonabsorbable dilution marker. Gastric contents were collected 5 min later through the gastric cannula. To wash the interior of the stomach, 3 mL of saline was infused into the stomach twice and then collected. The gastric contents and wash-out solution were pooled, filtrated and absorbance was measured at 560 nm after adequate dilution and alkalization with NaOH. The level of gastric emptying was calculated using the formula of Smith et al. (23
).
In vitro experiments
CCK release from dispersed rat intestinal mucosal cells.
Preparation of dispersed rat intestinal mucosal cells and the experimental procedure were performed as previously described (16
). Briefly, 20 cm of the proximal small intestine was removed from male Sprague-Dawley rats (250–350 g) and everted after washing with saline. It was then incubated in oxygenated calcium-free Krebs-Henseleit bicarbonate buffer containing 2.5 mmol/L of EDTA, pH 7.4, at 37°C for 5 min. The mucosa was peeled, dispersed and centrifuged (50 x g, 3 min). The pellets containing mucosal cells from three rats were pooled, resuspended in HEPES buffer and incubated at 37°C. Cell suspension (1 mL) was added to a plastic vial containing 200 or 500 µg ß-conglycinin or its peptone and incubated for 30 min at 37°C with slight stirring. After incubation, the supernatant was collected and CCK concentration in the supernatant was measured by bioassay using rat acini, as described above.
Evaluation of binding of ß-conglycinin peptone to rat intestinal brush border membrane.
Binding of ß-conglycinin and its peptone to rat intestinal brush border membrane was estimated using a BIACORE 3000 system (BIACORE AB, Uppsala, Sweden). Preparation of the soluble components of rat jejunal brush border membrane was performed using a previously described method (24
) and the solubilized membrane proteins were immobilized on the flow cell of a CM5 sensor chip by an amine-coupling procedure (a test cell) (25
). Ethanolamine was immobilized on the reference flow-cell of a sensor chip. Various concentrations of ß-conglycinin and its peptone (10–500 mg/L) in HEPES buffer containing 150 mmol/L of NaCl and 3 mmol/L of EDTA, pH 7.4, were injected over the test and reference flow cells at a rate of 10 µL/min for 2 min. The relative increases in response between the soluble brush border membrane and the reference flow-cell was measured and the amount of protein bound to the soluble brush border membrane was represented in resonance units.
Statistical analyses. All results were expressed as means ± SEM. Food intake after intraduodenal infusion of dietary peptones and camostat was measured separately and these data were expressed as relative values, with the control (water group) as 100. Data were analyzed by one- or two-way ANOVA and significant differences between groups were determined by Duncan’s multiple range test. Differences of P < 0.05 were considered significant.
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RESULTS |
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TOPABSTRACTMATERIALS AND METHODSRESULTSDISCUSSIONLITERATURE CITED |
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2 g lower than that in rats in which water was infused into the duodenum (4.45 ± 0.41 g vs. 6.44 ± 0.45 g, P < 0.05, n = 8). In contrast, the food intake from 30 min to 60 min was very low and was similar between the two groups; rats in the ß-conglycinin peptone group did not consume more food to compensate for the decrease in food intake during the first 30-min period (0.83 ± 0.23 g vs. 0.78 ± 0.18 g, P > 0.05, n = 8).
In the devazepide-treated group, food intake was not lower after intraduodenal infusion of ß-conglycinin peptone compared with that of the control (5.88 ± 0.56 g vs. 5.73 ± 0.24 g, P > 0.05), whereas intravenous pretreatment with the vehicle lowered food intake (4.04 ± 0.16 g vs. 5.73 ± 0.24 g, P < 0.05). Food intake was not influenced by the intraduodenal infusion of water regardless of devazepide treatment (Fig. 2
).
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).
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).
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).
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3–4 times higher than that of intact ß-conglycinin (Fig. 5
).
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DISCUSSION |
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TOPABSTRACTMATERIALS AND METHODSRESULTSDISCUSSIONLITERATURE CITED |
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The duodenal infusion of 2 g/L ß-conglycinin peptone decreased food intakes, whereas whole soy peptone containing ß-conglycinin did not (Table 2)
. ß-Conglycinin had a potent inhibitory effect on food intake, but the other components in soy protein, such as glycinin, did not. The content of ß-conglycinin in whole soy protein is reported to be 27% (26
); 5 g/L of soy peptone includes 1.35 g ß-conglycinin peptide. Although 1 g/L of ß-conglycinin peptone tended to reduce food intake (P = 0.06), 5 g/L of soy peptone infusion did not suppress food intake. Phytate, which affects the solubility and digestibility of protein, exists in soy protein and forms a protein-phytate complex (27
). Accordingly, it seems that the level of intact ß-conglycinin in soy protein is < 27%. Thus, the concentration of the active ß-conglycinin fragment in the 5 g/L of soy peptone infused into the duodenum may have been too low to suppress food intake.
The effect of ß-conglycinin peptone on food intake suppression was completely abolished by intravenous injection of the selective peripheral CCK receptor (CCK-A receptor) antagonist, devazepide (Fig. 2)
. Thus, endogenous CCK mediates the reduction of food intake by luminal ß-conglycinin peptone and CCK-A receptors are involved in the reduction. Some reports showed previously that proteins and peptones suppress food intake via CCK-A receptors (28
–30
), and our results from this experiment are in agreement. CCK receptors exist on the vagus nerve (31
), and the suppression of food intake by CCK has been blocked by vagotomy (32
) or the destruction of visceral afferent neurons by capsaicin treatment (33
). Therefore, it is possible that the regulation of food intake by CCK depends on vagal innervation. However, it has also been observed that CCK-induced food intake suppression was not inhibited by vagotomy (34
). Therefore, the mechanism of food intake control by endogenous CCK remains controversial. Further studies are required to determine whether the nervous system is involved in the food intake suppression by intraduodenal infusion of ß-conglycinin peptone.
ß-Conglycinin peptone not only suppressed food intake but also inhibited gastric emptying. It was shown previously that CCK is involved in the inhibition of gastric emptying by a peptone (35
), and CCK-induced suppression food intake is caused in part by inhibition of gastric emptying (5
,36
). In the present study, food intake was reduced until 30 min after the infusion of ß-conglycinin peptone and gastric emptying was inhibited at 15 min, but not at 30 min after the intraduodenal infusion (Fig. 3)
. These results suggest that the inhibition of gastric emptying induced by CCK is involved in the reduction of food intake by ß-conglycinin.
Intraduodenal infusion of ß-conglycinin peptone raised plasma CCK concentrations remarkably, but infusion of camostat did not (Table 2)
. After intraduodenal infusion of ß-conglycinin peptone, luminal trypsin digests the ß-conglycinin peptone and apparent trypsin activity might be reduced. Reduction of intraluminal trypsin activity causes the secretion of endogenous CCK (2
). Therefore, we examined effects of the intraduodenal infusion of camostat, a synthetic trypsin inhibitor, on food intake and in vivo CCK secretion in this study. The camostat concentration (0.25 mg/L) was adjusted to have the same trypsin-inhibition activity as did 2 g/L of ß-conglycinin peptone. However, camostat infusion did not increase plasma CCK concentration or suppress food intake, as did ß-conglycinin peptone. It is possible that the decrease in luminal trypsin activity induced by this concentration of camostat was too low to induce CCK secretion, or that camostat induced only a temporal rise in CCK after the infusion. These findings indicate that the regulation of endogenous CCK release after intraduodenal infusion of ß-conglycinin peptone is independent of the reduction in intraluminal trypsin activity. The infusion of wheat peptone did not decrease food intake (Table 2)
. We previously demonstrated that the potency of wheat peptone–induced CCK release from rat intestinal cells was weaker than that of soy peptone (16
), suggesting that CCK release activity is involved in the suppression of food intake by dietary peptone.
In the present study, ß-conglycinin peptone increased CCK release from dispersed rat small intestinal mucosal cells. ß-Conglycinin peptone directly stimulates the intestinal cells to release CCK, thus supporting the above hypothesis that the endogenous CCK release by ß-conglycinin peptone infusion does not depend on the reduction in intraluminal trypsin activity. This hypothesis is supported by the results of the binding study using a Biacore biosensor (Fig. 5)
. That is, ß-conglycinin peptone bound strongly to the mucosal membrane and stimulated CCK release from the mucosal cells; however, intact ß-conglycinin did not bind to the cell membrane or increase CCK release. In the present study, it is not known whether ß-conglycinin peptone reacted directly with I-cells because the intestinal cells used in this experiment consisted of several kinds of cells in addition to I-cells. In rats, two types of endogenous CCK-releasing peptides are produced in the intestinal mucosa and released into the lumen (37
,38
). There is a possibility that ß-conglycinin peptone stimulates these endogenous CCK-releasing peptide producing-cells, but not I-cells.
As described above, ß-conglycinin peptone bound to the components of the intestinal cell membrane and stimulated CCK release from the cells in a dose-dependent manner. Intact ß-conglycinin showed less binding to the intestinal cells and induced less CCK release from the cells than did the ß-conglycinin peptone. Previously, we demonstrated that a peptide structure including guanidyl residue, which also contains a native amino acid, L-arginine, participates in the binding to the cell membrane (24
) and in CCK release (15
). Peptic hydrolysis of ß-conglycinin exposes the arginine-containing parts buried in intact ß-conglycinin, which may then be involved in the increase in binding activity to the component of the intestinal cell membrane and in CCK release from the cells. However, we previously showed that there was no correlation between arginine content in dietary protein and CCK release from the intestinal cells (16
). This earlier result suggests that the binding activity of the ß-conglycinin peptone to the cell membrane does not depend on the number of arginine residues, but on particular structures containing arginine in ß-conglycinin. The segments of ß-conglycinin that bind to the intestinal cell membrane must be clarified and their structures characterized.
In conclusion, the present study demonstrated that duodenal ß-conglycinin peptone suppressed food intake in a CCK-dependent manner and that the inhibition of gastric emptying was associated with this suppression. We also showed that ß-conglycinin peptone binds to components of the rat intestinal cell membrane directly and stimulates CCK release from the cells. These results suggest that ß-conglycinin peptone in the lumen interacts directly with the intestinal mucosal cells to stimulate CCK release, and this CCK leads to a suppression of food intake via peripheral CCK receptors.
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FOOTNOTES |
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Manuscript received 13 August 2002. Initial review completed 23 September 2002. Revision accepted 13 November 2002.
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LITERATURE CITED |
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TOPABSTRACTMATERIALS AND METHODSRESULTSDISCUSSIONLITERATURE CITED |
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