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Biomedical subjects

A Pusztai

Publications and source records attributed to A Pusztai.

At least 37 records · Page 2Linked to original sources
PubMed1999

A combination of dietary protein depletion and PHA-induced gut growth reduce the mass of a murine non-Hodgkin lymphoma.

The results presented in this study show that a switch from a non-protein diet (NPD) to one of a normal protein content (LA) on the day of subcutaneous injection of non-Hodgkin lymphoma tumour cells greatly favoured the development and growth of the tumour. Interestingly, however, inclusion of the plant lectin phytohaemagglutinin (PHA) in the LA diet appeared to compete with the effect of switch to the protein-rich diet, resulting in decreased tumour size and an increased incidence of necrosis. PHA was shown to induce hyperplasia of the gut even in the presence of the growing tumour. This observation together with the fact that gut hyperplasia also occurred in animals which were fed NPD supplemented with PHA, indicated the strength of PHA as a growth signal. It would seem likely that this 'normal' growth is able to compete with the tumour for important growth factors and nutrients, including polyamines, effectively starving the tumour for these molecules and resulting in its decreased rate of proliferation.

Animals↗
PubMed1999

In vivo degradation and stimulating effect of phaseolin on nitrogen secretion in rats.

In short-term feeding experiments, about 78% of the phaseolin administered to rats was degraded regardless of the amounts of phaseolin intubated. In contrast, the total N found in the feces increased rapidly and exceeded the original administered amounts. The bulk of N output was not immunologically related to the glycoprotein. The effects of phaseolin on the stimulation of endogenous N secretion in the small intestine were confirmed from the results of acute experiments. Phaseolin fragments, derived from the breakdown of the native protein, when reapplied intragastrically to rats, were broken down further and to a similar extent as the original glycoprotein and were even more potent related to stimulation of N secretion. It is suggested that this secretagogue biological activity of phaseolin and not its resistance to gut proteolysis, is the main reason for the poor nutritional value of this glycoprotein.

Animals↗
PubMed1999

Expression of the insecticidal bean alpha-amylase inhibitor transgene has minimal detrimental effect on the nutritional value of peas fed to rats at 30% of the diet.

The effect of expression of bean alpha-amylase inhibitor (alpha-AI) transgene on the nutritional value of peas has been evaluated by pair-feeding rats diets containing transgenic or parent peas at 300 and 650 g/kg, respectively, and at 150 g protein/kg diet, supplemented with essential amino acids to target requirements. The results were also compared with the effects of diets containing lactalbumin with or without 0.9 or 2.0 mg bean alpha-AI, levels equivalent to those in transgenic pea diets. When 300 and 650 g peas/kg diet were fed, the daily intake of alpha-AI was 11.5 or 26.3 mg alpha-AI, respectively. At the 300 g/kg level, the nutritional value of the transgenic and parent line peas was not significantly different. The weight gain and tissue weights of rats fed either of the two pea diets were not significantly different from each other or from those of rats given the lactalbumin diet even when this was supplemented with 0.9 g alpha-AI/kg. The digestibilities of protein and dry matter of the pea diets were slightly but significantly lower than those of the lactalbumin diet, probably due to the presence of naturally occurring antinutrients in peas. The nutritional value of diets containing peas at the higher (650 g) inclusion level was less than that of the lactalbumin diet. However, the differences between transgenic and parent pea lines were small, possibly because neither the purified recombinant alpha-AI nor that in transgenic peas inhibited starch digestion in the rat small intestine in vivo to the same extent as did bean alpha-AI. This was the case even though both forms of alpha-AI equally inhibited alpha-amylase in vitro. Thus, this short-term study indicated that transgenic peas expressing bean alpha-AI gene could be used in rat diets at 300 g/kg level without major harmful effects on their growth, metabolism and health, raising the possibility that transgenic peas may also be used at this level in the diet of farm animals.

Animals↗
PubMed1999

Secretion of pancreatic digestive enzymes induced in rats by first-time oral exposure to kidney bean E2L2 lectin is mediated only in part by cholecystokinin (CCK).

The acute effects of kidney bean (Phaseolus vulgaris) E2L2 lectins (PHA) given orally to conscious rats or continually infused into the duodenum of anesthetized rats on blood cholecystokinin (CCK), secretin, and gastrin and on secretion of pancreatic digestive enzymes have been evaluated. PHA increased circulating levels of CCK and secretin but did not alter gastrin. In addition, PHA induced dose-dependent secretion of trypsinogen, chymotrypsinogen, and alpha-amylase by the pancreas in vivo. This pancreas output appeared to be modulated only in part through CCK. Thus pretreatment of rats with a CCK-A receptor antagonist (L-364718) attenuated the immediate (< or = 90 min) pancreas secretory response to PHA but could not prevent a PHA-associated increase in digestive enzyme output in the longer term (after 90 min). In contrast, treatment of rats with L-364718 abolished the stimulatory effects of soyabean trypsin inhibitors on digestive enzyme secretion in both the short and long term. Additional mechanisms or hormones, such as secretin, may play a role in modulating later exocrine pancreas responses to PHA.

Animals↗
PubMed1999

Gastrointestinal responses to a panel of lectins in rats maintained on total parenteral nutrition.

Total parenteral nutrition (TPN) causes atrophy of gastrointestinal epithelia, so we asked whether lectins that stimulate epithelial proliferation can reverse this effect of TPN. Two lectins stimulate pancreatic proliferation by releasing CCK, so we asked whether lectins that stimulate gastrointestinal proliferation also release hormones that might mediate their effects. Six rats per group received continuous infusion of TPN and a once daily bolus dose of purified lectin (25 mg. rat-1. day-1) or vehicle alone (control group) for 4 days via an intragastric cannula. Proliferation rates were estimated by metaphase arrest, and hormones were measured by RIAs. Phytohemagglutinin (PHA) increased proliferation by 90% in the gastric fundus (P < 0.05), doubled proliferation in the small intestine (P < 0.001), and had a small effect in the midcolon (P < 0.05). Peanut agglutinin (PNA) had a minor trophic effect in the proximal small intestine (P < 0.05) and increased proliferation by 166% in the proximal colon (P < 0.001) and by 40% in the midcolon (P < 0.001). PNA elevated circulating gastrin and CCK by 97 (P < 0.05) and 81% (P < 0.01), respectively, and PHA elevated plasma enteroglucagon by 69% and CCK by 60% (both P < 0.05). Only wheat germ agglutinin increased the release of glucagon-like peptide-1 by 100% (P < 0.05). PHA and PNA consistently reverse the fall in gastrointestinal and pancreatic growth associated with TPN in rats. Both lectins stimulated the release of specific hormones that may have been responsible for the trophic effects. It is suggested that lectins could be used to prevent gastrointestinal atrophy during TPN. Their hormone-releasing effects might be involved.

Animals↗
PubMed1999

Identification of acute intermittent porphyria carriers by molecular biologic methods.

Acute intermittent porphyria (AIP) is an autosomal dominant disease caused by mutations of the gene coding for hydroxymethylbilane synthase. Acute attack of AIP is a potentially life-threatening condition precipitated by certain drugs, alcohol, fasting and stress. Biochemical diagnosis before the manifestation of the symptoms is problematic, and genetic screening is required to identify asymptotic carriers. The aim of this study was to establish a fast, reproducible and reliable genetic method to detect mutations causing AIP. Exon 10 of one healthy individual and 12 AIP patients was studied using a recently developed method, temporal temperature gradient electrophoresis (TTGE). Mutation of exon 10 was detected using TTGE in one patient, DNA sequence analysis confirmed the presence of a heterozygous point mutation causing substitution of the arginine in position 173 of the gene with glutamine. These results were also confirmed using restriction enzyme analysis, and this method and TTGE identified a child of this patient as an asymptotic carrier of AIP.

Antisense Elements (Genetics)↗
PubMed1998

Oxidative degradation of polyamines in rat pancreatic hypertrophy.

In the hypertrophic pancreas, we studied the oxidative degradation of polyamines, which are endogenous polycations important for cell division, growth and differentiation. To induce pancreatic hypertrophy, rats were fed on a semi-synthetic diet containing a daily dose of 42 mg phytohaemagglutinin per rat for 5 or 10 days. In the model, the activities of polyamine oxidase (the enzyme that degrades spermidine, spermine and mainly their acetyl derivatives) and diamine oxidase (the key enzyme of terminal catabolism of polyamines in vivo) increased by 100-180% and 90-100%, respectively, parallel to an elevation in polyamine content (40-100%). The results suggest that in pancreas hypertrophy, which does not exhibit stimulation of spermidine/spermine N1-acetyltransferase activity, increases in the activity of polyamine and diamine oxidases are related events that lead to putrescine formation and removal of excess polyamines.

Administration, Oral↗
PubMed1998

Attachment of different Escherichia coli strains to cultured rumen epithelial cells.

The attachment to fully characterized primary rumen epithelial cell cultures of Escherichia coli strains isolated from different animal species and expressing F1-F4 or F17 fimbriae was examined. As the cell cultures contained stratified (keratinized) and non-stratified (non-keratinized) cells which grew either confluently or non-confluently, the strength of attachment of the different bacterial strains was assessed in relation to the differentiation state of the cells. Thus, strains having F1 fimbriae attached to all types of cultured cells, while strains with F2 and F3 fimbriae did not bind at all. E. coli strains having F4 or F17 fimbriae attached only to non-keratinized cells, particularly to confluent areas. As membrane glycosylation is known to change with differentiation (keratinization), our results suggest that the attachment of fimbriated E. coli strains which were capable of binding to rumen cells was more likely to be dependent on differentiation than the host specificity of the bacteria.

Animals↗
PubMed1998

Lipid accumulation in obese Zucker rats is reduced by inclusion of raw kidney bean (Phaseolus vulgaris) in the diet.

The effects of inclusion of different levels of raw kidney bean (Phaseolus vulgaris) of high lectin content (27 g/kg meal) in a high-quality (lactalbumin) control diet were tested in nutritional trials on the growth and metabolism of obese Zucker (fafa) rats and their lean littermates in comparison with pair-fed controls. All diets contained 100 g total protein/kg and either 50 g lipids/kg (low fat) or 150 g lipids/kg (moderate fat). The growth of both obese and lean rats on bean diets was retarded by the daily bean intake in a dose-dependent manner. However, most of this was because bean-fed rats contained less body fat than the controls after 10 d. Thus, after feeding low-fat diets containing up to 130 g kidney bean/kg (lectin intake < or = 0.2 g/kg body weight (BW) per d) in both 10 d and 70 d trials, the bodies of obese rats contained less fat but not protein than their pair-fed controls. Moreover, by increasing the lipid content of the diet to 150 g/kg, the level of bean inclusion could be increased to 280 g/kg (lectin intake > or = 0.4 g/kg BW per d) without loss of body protein and skeletal muscle. Although these rats contained more body fat than those which were fed on low-fat diets, their weight reduction could be accounted for exclusively by reduced lipid content. In contrast, significant body protein loss occurred when the same diet of high lectin content was fed to lean littermates. Plasma insulin levels were significantly depressed in the obese Zucker rats on bean diets but the pancreas was not significantly enlarged nor its insulin content changed in 10 d trials. However, significant pancreatic growth occurred on long-term (70 d) bean feeding compared with pair-fed controls. The results suggest that, in addition to animal nutrition, it may also be possible to use the bean lectin as a dietary adjunct or therapeutic agent to stimulate gut function and ameliorate obesity if a safe and effective dose-range can be established for human subjects.

Animals↗
PubMed1998

Nutritional utilization by rats of chickpea (Cicer arietinum) meal and its isolated globulin proteins is poorer than that of defatted soybean or lactalbumin.

The effects on performance, digestibility, N utilization and plasma amino acid concentrations of dietary chickpea (Cicer arietinum, var. Kabuli) seed meal, globulin proteins or buffer-insoluble residue [starch + non-starch polysaccharides (NSP) + lignin] were studied in growing rats. Chickpea meal, defatted soybean meal, chickpea globulins and lactalbumin were each incorporated into diets as the sole source of dietary protein (100 g/kg). In addition, chickpea insoluble residue was included in a control diet in the same proportion found in the chickpea meal. Rats were killed while under halothane anesthesia after 10 d of consuming the diets, and ileal contents were washed out and freeze-dried for digestibility measurements. Weight gains and gain:feed ratios of rats fed chickpea diets for 10 d did not differ from those of rats fed defatted soybean but were significantly lower than those of rats given the control (lactalbumin) diet. However, ileal and fecal N digestibilities and N retention by rats fed the chickpea diet were significantly lower than those obtained with the lactalbumin or soybean diet. The inclusion of both chickpea meal or its globulin proteins in the diet significantly increased the amount of N excreted, primarily as urea, through the urine. However, although ileal N digestibility values for chickpea meal were significantly lower, those for its constituent globulins did not differ from control values. Urea levels in plasma in rats fed diets containing chickpea meal, globulins or soybean meal were significantly higher than in those fed lactalbumin. Furthermore, the concentrations of glycine, phenylalanine, histidine, arginine and ornithine in the plasma of rats fed chickpea meal, its globulins or defatted soybean were significantly higher, whereas those of threonine, leucine, lysine and tryptophan were significantly lower than lactalbumin-fed controls. The chickpea insoluble residue had no adverse effects on performance or N utilization by rats. We conclude that the low nutritional value of chickpea meal is likely to be due mainly to adverse effects of its globulin proteins on growth and N metabolism rather than to the action of any known antinutritional factor present in the diet.

Amino Acids↗
PubMed1998

Putrescine as a source of instant energy in the small intestine of the rat.

BACKGROUND AND AIMS: It has been suggested that putrescine acts as a growth factor in the gut, but its exact function in some aspects of cellular metabolism is still in question. The aim of the present work was to identify some functions of putrescine in small bowel metabolism. ANIMALS: Rats (about 80 g), in groups of five, were given either phytohaemagglutinin- or lactalbumin-containing diets, fed ad libitum or were fasted for 48 hours and re-fed for six or twelve hours before being killed. METHODS: Uptake of intraperitoneally or intragastrically administered [14C]putrescine and its conversion to succinate by the rat small bowel mucosa was measured. Tissue polyamine and succinate contents were measured by high performance liquid chromatography and amino acid analysis respectively. RESULTS: Uptake of putrescine by the small bowel mucosa from the systemic circulation and conversion of about 30% of this to succinate occurs in the epithelium of the healthy small bowel. Compared with rats given food ad libitum, putrescine uptake was doubled in fasted animals and more than 70% of it was converted to succinate. All these changes returned to control values on refeeding. Using phytohaemagglutinin induced gut growth as a model, the uptake of putrescine from the systemic circulation by the serosal side of the small intestinal epithelium was increased immediately after growth was stimulated. During phytohaemagglutinin induced growth of the gut, putrescine was converted to succinate in the same proportion as in the healthy small bowel. CONCLUSIONS: The experiments identified a novel function for putrescine in gut metabolism: it can be used as an instant energy source when required.

Analysis of Variance↗
PubMed1998

The induction of gut hyperplasia by phytohaemagglutinin in the diet and limitation of tumour growth.

The growth of a transplantable murine non-Hodgkin lymphoma tumour, developing either intraperitoneally as an ascites tumour or subcutaneously as a solid tumour, has been shown to be markedly diminished by including phytohaemagglutinin (PHA), a lectin present in raw kidney bean (Phaseolus vulgaris) in the diet. In NMRI mice fed PHA within the range 0.45-7.0 mg/g diet, tumours which developed during a 10 day period after subcutaneous injection of cells were about 35% of the dry weight of those in lactalbumin-fed (control) animals. The reduced rate of growth occurred in a dose-dependent manner within the range 0.45-3.5 mg/g diet. Based on these observations it has been suggested that a competition between the gut epithelium undergoing hyperplasia and the developing tumour may occur for nutrients from a common body pool, and this may be an important factor with regard to the observed initial low level of tumour growth following the feeding of a PHA-containing diet. Observations which showed that the level of hyperplasia of the small bowel in response to feeding the PHA diets was higher in non-injected mice compared to those which had been injected with tumour cells substantiated the concept of competition between gut and tumour for nutrients etc. required for growth. Experiments with a second murine tumour cell line (a plasmacytoma) in Balb/c mice gave similar results indicating that the effect of PHA was not restricted to a single tumour system.

Animals↗
PubMed1997

Intracellular levels of polyamines in Krebs II lymphosarcoma cells in mice fed phytohaemagglutinin-containing diets are coupled with altered tumour growth.

The number of Krebs II tumour cells recovered from the ascitic fluid of mice fed for 8 days on a lactalbumin (La) control diet was about three times higher than that in animals fed a phytohaemagglutinin-containing (PHA) diet. Feeding a PHA diet for less than 8 days after tumour cell injection also led to a reduction in tumour cell growth. There was an apparent inverse relationship between the total tumour cell count and the intracellular content of putrescine, spermidine and spermine. Hyperplasia of the small intestine occurred in the mice during the development of the ascites. A series of other organs were not affected in the same manner. The results indicate that the polyamine content of Krebs II ascites cells must increase by more than three-fold in order to achieve the intracellular concentration necessary to be able to enter the S-phase. A partial synchronization of the tumour cell population is suggested. Hyperplastic growth of the small intestine would appear to compete with tumour cells for polyamines from a common body pool.

Animals↗
PubMed1997

Kidney bean and soybean lectins cause enzyme secretion by pancreatic acini in vitro.

The responses of pancreas acini from Hooded-Lister rats to kidney bean E2L2 lectin or soybean agglutinin have been studied in vitro. Both lectins induced secretion of alpha-amylase from acini in a dose dependent manner. However, the concentrations of lectin required to cause enzyme secretion were approximately 14-fold higher than that necessary with CCK-8. In addition, the responsiveness of pancreas acini to lectins in vitro was significantly altered by the age and sex of the rats from which the acini were derived.

Animals↗
PubMed1997

Effects of short-term feeding of rats with a highly purified phaseolin preparation.

Rats fed a diet containing a highly purified preparation of phaseolin, the main globulin from the seeds of Phaseolus vulgaris, rapidly lost weight. Fecal nitrogen outputs were elevated and the N digestibility, based on conventional method estimation, was only 37.5%. By using immunological techniques, however, it was shown that the bulk of the nitrogen recovered in the feces was not chemically related to phaseolin. After correction for this non-phaseolin N, the true digestibility of phaseolin was estimated to be 74.3%. It is suggested that phaseolin and/or undigested fragments derived from the native molecule may, as reported for the lectins, stimulate the secretion of endogenous N, possibly mucins.

Animals↗
PubMed1997

Novel dietary strategy for overcoming the antinutritional effects of soyabean whey of high agglutinin content.

A diet-switching experiment, which aimed to improve the utilization of soyabean whey was carried out for 61 d with young rats. Feeding was arranged in such a way that after a few days on the soyabean diet, the rats were switched to a high-quality lactalbumin diet for a short period, after which the cycle was repeated several times. The weights of the rats at the end of the soyabean phases were significantly less than those of animals pair-fed on a high-quality diet throughout. However, the test group regained the weight loss after switching to the lactalbumin diet. After three cycles there were no significant differences between the weights of the test rats fed on a poor soyabean diet for over a third of the experiment and those fed on the lactalbumin diet throughout. Feed conversion was always significantly higher with test rats in the lactalbumin period than with continually pair-fed controls. Similarly, faecal N losses were significantly higher for test rats in the soyabean phase, but these differences disappeared after switching to the lactalbumin diet. At the end of the experiment there were no significant differences in body protein or lipids between the groups although the pancreas was significantly heavier while the liver was lighter in soyabean-fed rats. The high destruction of trypsin inhibitors in the gut suggests that they probably had little effect on protein digestion in the gut. In contrast, as selective depletion of the agglutinin from soyabean whey removed the nutritional benefit in the lactalbumin part of the cycle, the improved feed conversion in this period must have been the result mainly of the survival and functionality of soyabean agglutinin and the benefits due to the hyperplastic growth and faster renewal of the gut surface it induced. As processing is unnecessary, this novel method is cheap and can be easily adapted for the use of soyabean whey, regarded as a waste product.

Animal Nutritional Physiological Phenomena↗
PubMed1997

Salmonella enterica var Typhimurium and Salmonella enterica var Enteritidis express type 1 fimbriae in the rat in vivo.

In a series of experiments rats were dosed with purified type 1 fimbriae from Salmonella enterica var Enteritidis or with fimbriated cultures of either S. enterica var Typhimurium or S. enterica var Enteritidis. Paraffin-wax embedded histological sections of jejunal and ileal tissue were taken and stained by the streptavidin biotin complex (sABC) staining technique for the detection of salmonella and type 1 fimbriae. On oral infection with Enteritidis and Typhimurium both bacteria were shown to be closely associated with the rat ileal epithelium and expressed type 1 fimbriae, thus clearly demonstrating that type 1 fimbriae are expressed by salmonellae in vivo. Moreover, association with the ileum was also shown to occur when purified type 1 fimbriae were orally administered to rats. Our results suggest that type 1 fimbriae alone or in combination with other fimbriae may play an important role in the early stages of infection with these pathogenic bacteria.

Animals↗