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PubMed1994

Inhibition of the phosphoenolpyruvate:lactose phosphotransferase system and activation of a cytoplasmic sugar-phosphate phosphatase in Lactococcus lactis by ATP-dependent metabolite-activated phosphorylation of serine 46 in the phosphocarrier protein HPr.

Lactococcus lactis takes up lactose and the nonmetabolizable lactose analogue, thiomethyl-beta-galactoside (TMG), via the phosphoenolpyruvate:sugar phosphotransferase system (PTS) which couples sugar transport to sugar phosphorylation. Earlier studies had shown that TMG-phosphate, previously accumulated in L. lactis cells, is rapidly dephosphorylated in the cytoplasm and effluxes from the cells upon addition of glucose and that glucose inhibits further uptake of TMG. We have developed a vesicular system to analyze this regulatory mechanism and have used electroporation to shock proteins and membrane-impermeable metabolites into the vesicles. Uptake of TMG was dependent on an energy source, effectively provided by intravesicular phosphoenolpyruvate at low concentrations or extravesicular phosphoenolpyruvate at high concentrations. TMG uptake into osmotically shocked vesicles was only weakly inhibited, and expulsion of preaccumulated TMG was only slightly stimulated upon addition of glucose. Intravesicular (but not extravesicular) wild-type HPr of Bacillus subtilis completely restored the regulatory behavior observed in vivo when glucose was present in the external medium. Glucose could be replaced by intravesicular (but not extravesicular) fructose 1,6-diphosphate, gluconate 6-phosphate, or 2-phosphoglycerate, but not by other phosphorylated metabolites, in agreement with the allosteric activating effects of these compounds on HPr(Ser) kinase measured in vitro. Intravesicular mutant HPr(S46A) protein could not promote regulation of lactose permease activity when electroporated into the vesicles regardless of the presence or absence of glucose or the various phosphorylated metabolites, but the HPr(S46D) mutant protein promoted regulation, even in the absence of glucose or a metabolite, and HPr(H15A) was more effective than the wild-type protein in promoting regulation. Intravesicular wild-type and H15A HPrs, but not the S46A or S46D mutant proteins, were found to be phosphorylated by ATP under the conditions which promoted TMG efflux. In toluenized vesicles, the conditions which promoted TMG efflux also promoted TMG-P hydrolysis. These results establish for the first time that HPr serine phosphorylation by the ATP-dependent metabolite-activated HPr kinase regulates the expulsion of intracellular sugar-phosphate as well as the uptake of sugar via the PTS in L. lactis.

Adenosine Triphosphate↗
PubMed1978

Amplification of the lactose carrier protein in Escherichia coli using a plasmid vector.

The isolation and properties of a hybrid plasmid carrying the Y gene of the lac operon of Escherichia coli are described. The lactose carrier protein, coded for by the Y gene, is readily identified upon lac operon induction in strains carrying the plasmid. The protein comprises about 15% of the cytoplasmic membrane protein synthesized in the first generation after induction, compared with a wild type strain induced under the same conditions where lactose carrier protein comprises 1.4% of the cytoplasmic membrane protein.

Carrier Proteins↗
PubMed1983

A model and program for study of a tolerance curve: application to lactose absorption tests.

A method has been devised for the analysis of tolerance curves, and tested on data collected for the diagnosis of lactose malabsorption with lactose tolerance tests. Two different models were fitted to over 100 experimental curves; the need to allow small changes over time in the glucose baseline level became evident, indicating that a model allowing a time trend is preferable. The results are briefly discussed and the biological significance of the quantities estimated by the method is discussed.

Adult↗
PubMed1998

Beta1,4-galactosyltransferase and lactose biosynthesis: recruitment of a housekeeping gene from the nonmammalian vertebrate gene pool for a mammary gland specific function.

Beta1,4-galactosyltransferase (beta4GalT-I) is a constitutively expressed trans-Golgi enzyme, widely distributed in vertebrates, which synthesizes the beta4-N-acetyllactosamine structure commonly found in glycoconjugates. In mammals beta4GalT-I has been recruited for a second biosynthetic function, the production of lactose; this function takes place exclusively in the lactating mammary gland. In preparation for lactose biosynthesis, beta4GalT-I enzyme levels are increased significantly. We show that mammals have evolved a two-step mechanism to achieve this increase. In step one there is a switch to the use of a second transcriptional start site, regulated by a stronger, mammary gland-restricted promoter. The transcript produced is distinguished from its housekeeping counterpart by the absence of approximately 180 nt of 5'-untranslated sequence. In step two, this truncated transcript is translated more efficiently, relative to the major transcript expressed in all other somatic tissues.

Animals↗
PubMed2001

Improvement of symptoms in infant colic following reduction of lactose load with lactase.

Transient lactose intolerance has been identified as a possible causative factor in infant colic. A double-blind randomised placebo-controlled crossover study to investigate this has been undertaken in 53 babies with symptoms of colic. Pre-incubation of the feed with lactase resulted in breath hydrogen levels and total crying time which were both at least 45% lower than figures with placebo treatment, in 26% of the full trial group (95% confidence interval 12.9% to 44.4%), and in 38% of compliers (95% confidence interval 18.8% to 59.4%). The remainder did not respond to the same extent. These findings suggest that infant colic may have a multiple aetiology, and that in a significant number of cases the immediate cause is transient lactose intolerance, in which cases pretreatment of feeds with lactase can result in considerable symptomatic benefits.

Breath Tests↗
PubMed1978

Lactose and major milk proteins are present in secretory vesicle-rich fractions from lactating mammary gland.

Preparations enriched in apparently intact secretory vesicles were isolated from homogenates of lactating rat and bovine mammary tissue by differential and density gradient centrifugation in isoosmotic media. Morphologically these preparations consisted nearly entirely of vesicles of varying sizes, at least some of which contained casein micelles. Endoplasmic reticulum vesicles, Golgi apparatus cisterna and dictyosomes, mitochondria, peroxisomes, lysosomes, and nuclei were not observed in secretory vesicle-rich fractions. Vesicle preparations were enriched in lactose relative to total membrane fractions from mammary gland. The galactosyltransferase of lactose synthase (UDPgalactose: D-glucose 4 beta-galactosyl-transferase, EC 2.4.1.22) was also present in secretory vesicle preparations, alphas1- and beta-caseins, alpha-lactalbumin, and beta-lactoglobulin, the major secretory proteins of differentiated mammary epithelial cells, were identified as constituents of vesicle-rich fractions from bovine mammary gland. These observations suggest that the major carbohydrate and major proteins of milk are compartmentalized into secretory vesicles and are secreted by exocytotic fusion of secretory vesicles with the apical plasma membrane.

Animals↗
PubMed1978

Poor predictability of lactose malabsorption from clinical symptoms for Chilean populations.

Clinical symptoms and lactose malabsorption may occur in persons intolerant to lactose. To predict malabsorption from symptoms and age, the authors used simple regression, multiple regression, and discrimant analysis on data from 436 Chileans. All individual r2 values from simple regression were less than 0.05. For the best stepwise multiple regression program, R2 was only 0.09, indicating that 91% of the variability in malabsorption was "unexplained" by the five best predictor variables. Because of so much unexplained variability, the authors could detect (using multiple regression) only 56 of 90 (62%) malabsorbers and only 14 of 38 (37%) absorbers. In conclusion, for their Chilean populations the authors poorly predicted malabsorption from symptoms.

Adolescent↗
PubMed1984

The effect of dietary lactose on the early recovery from protein-energy malnutrition. II. Indices of nutrient absorption.

Absorption of dietary energy, nitrogen, carbohydrates and calcium, and retention of nitrogen and calcium were studied in 20 children with protein-energy malnutrition of the edematous type, using metabolic balance techniques and breath H2 analysis, to assess the advisability of using lactose-containing formulas in the rehabilitation of severely malnourished children. Ten patients received for 45 days a diet formula based on cows' milk (intact milk) and 10 similar children received the same formula pretreated with beta-galactosidase to hydrolyze the lactose (hydrolyzed milk). Dietary intakes were gradually increased to reach, on the 8th day, 4 g of protein and 150 kcal/kg. There were no differences between groups with respect to absorption or retention of the index nutrients. Postprandial carbohydrate malabsorption was occasionally observed in two patients with servings of the intact milk formula, and in one with the hydrolyzed milk diet. When the nutritional quality of a diet is assessed, the amount of nutrients that are absorbed and utilized are more important than the small, incompletely absorbed fractions that do not have significant metabolic or clinical implications. Therefore, the use of milk as the protein source for recovery diets is not contraindicated in the routine treatment of PEM.

Animals↗
PubMed1990

Comparative absorption of [13C]glucose and [13C]lactose by premature infants.

Oxidation of orally administered [13C]glucose and [13C]lactose and fecal recovery of malabsorbed substrates were determined in two groups of premature infants. Eighteen studies were performed with six infants at Johns Hopkins Hospital (JHH); 24 studies were performed with nine infants at Columbus Children's Hospital (CCH). The two groups differed in that JHH infants had shorter gestations but were older when studied. Fecal 13C loss after [13C]glucose administration did not differ between the two groups. Compared with glucose, the metabolism of lactose appeared to involve more malabsorption and colonic fermentation in JHH infants than in CCH infants and resulted in higher fecal losses of substrate carbon. Maturation appeared to involve increased proximal intestinal absorption and greater retention of absorbed carbohydrate. Simultaneous absorption of substrate from the small and large intestine may limit the usefulness of breath tests for 13C in the premature infant.

Breath Tests↗
PubMed1963

Chelation of calcium by lactose: its role in transport mechanisms.

Lactose, like other sugars and polyols, prevents or delays the precipitation of calcium ion in the presence of bicarbonate buffer. That an uncharged calcium-lactose complex is formed was demonstrated by the use of paper electrophoresis and of calcium-45 as a label for the complex. Enhancement of the intestinal absorption of calcium ion by sugars could result from a complex of low molecular weight.

Biological Transport↗
PubMed1969

An isotope technique for measuring lactose absorption.

Expired radiocarbon dioxide has been collected by a simple autotitration method following the ingestion of lactose-1-(14)C. With this method, which is suitable for clinical use, 12 subjects with alactasia have been readily separated from 24 normals, both groups being defined by strict criteria. This test, which may be used to measure the absorption of other sugars, is especially suitable for population surveys and may be used to investigate the distribution of disaccharidase deficiency.A further advantage is that false low readings resulting from rapid plasma clearance of absorbed sugar do not occur with this method although they may do so in up to one in three lactose tolerance tests, thereby overestimating the prevalence of alactasia.

Adult↗
PubMed2003

Genetics of lactase persistence and lactose intolerance.

The enzyme lactase that is located in the villus enterocytes of the small intestine is responsible for digestion of lactose in milk. Lactase activity is high and vital during infancy, but in most mammals, including most humans, lactase activity declines after the weaning phase. In other healthy humans, lactase activity persists at a high level throughout adult life, enabling them to digest lactose as adults. This dominantly inherited genetic trait is known as lactase persistence. The distribution of these different lactase phenotypes in human populations is highly variable and is controlled by a polymorphic element cis-acting to the lactase gene. A putative causal nucleotide change has been identified and occurs on the background of a very extended haplotype that is frequent in Northern Europeans, where lactase persistence is frequent. This single nucleotide polymorphism is located 14 kb upstream from the start of transcription of lactase in an intron of the adjacent gene MCM6. This change does not, however, explain all the variation in lactase expression.

Gene Frequency↗
PubMed1982

14C-lactose breath tests during pelvic radiotherapy: the effect of the amount of small bowel irradiated.

Thirty patients who were undergoing pelvic radiotherapy had 14C-lactose breath tests performed in the first and fifth weeks of treatment. In Group I (21 patients), a significant portion of the small intestine was irradiated, and in Group II (9 patients), only a small portion of the small intestine was irradiated. In Group I, the average reductions in the excretion of ingested 14C between the first- and fifth-week tests were 41.5% at 1/2 hour postingestion (p less than 0.05), and 21.8% at 1 hour postingestion (p less than 0.05). In Group II, the percentage reductions were 11.8% and 3.7% at 1/2 and 1 hour, respectively (p greater than 0.05). The data suggest that lactose malabsorption is a factor in the etiology of the nausea, vomiting, and diarrhea experienced by patients who are undergoing pelvic radiotherapy, and that the amount of bowel included in the treatment volume significantly influences the degree of malabsorption.

Breath Tests↗
PubMed1984

Faecal weight, constituents, colonic motility, and lactose tolerance in the irritable bowel syndrome.

Lactose intolerance and faecal characteristics were compared in 16 patients with symptomatic irritable bowel syndrome and in age- and sex-matched controls. Faecal stool weight was increased in the irritable bowel syndrome patients, whereas faecal bile acids, fat, volatile fatty acids, and neutral sterols were not significantly different. No lactose intolerance was found in irritable bowel syndrome subjects. Measurements of colonic motility showed only modest activity for both basal and food-stimulated activity. There was a weak correlation between the concentration of total bile acids, deoxycholic acid, lithocholic acid and the motility index.

Adolescent↗
PubMed1995

Lactose malabsorption in Khants in western Siberia.

BACKGROUND: We wanted to estimate the prevalence of selective lactose malabsorption (SLM) in Khants, a small Finno-Ugric population living in Western Siberia who have traditionally consumed no milk in adulthood. METHODS: A total of 80 Khants, aged 8-57 years and living on the middle reaches of the River Ob, were studied. The diagnosis was based on a lactose tolerance test; general malabsorption was excluded by a glucose-galactose tolerance test whenever possible. In six subjects electronmicroscopic examination of the duodenal mucosa was performed. RESULTS: The prevalence of SLM in the Khants was 94%. CONCLUSION: This is the highest prevalence found in the previous Soviet Union.

Adult↗
PubMed1976

Influence of viable yogurt microflora on digestion of lactose by the rat.

Laboratory rats were fed experimental diets including yogurt, pasteurized yogurt, and simulated yogurt with sucrose or lactose for 7 days followed by a single experimental meal of yogurt, pasteurized yogurt, or simulated yogurt. Assays of blood galactose demonstrated that animals fed natural yogurt containing the viable culture microflora were able to absorb galactose more efficiently. Intestinal lactase activity of yogurt-fed animals was greater than in animals fed other experimental diets including pasteurized yogurt. Gastrointestinal survival of culture organisms was demonstrated in vivo up to 3 h after feeding, and thus, the viable cells resulted in more efficient hydrolysis which favored lactose digestion in natural yogurt.

Animals↗
PubMed2006

Hypolactasia as a molecular basis of lactose intolerance.

Lactase-phlorizin hydrolase (LPH), a membrane-bound glycoprotein present in the luminal surface of enterocytes in the intestine is responsible for lactose intolerance, a phenomenon prevalent in humans worldwide. In the rodent intestine, the post-natal development of the LPH follows a specific pattern, such that the enzyme levels are high in the peri-natal period, but declines considerably upon maturation. The observed maturational decline in the LPH activity is very similar to adult-type hypolactasia observed in humans. Majority of the studies have been carried out using animal models or cell lines and a number of hypotheses have been put forward to explain the maturational decline of lactase activity such as: (a) decreased amount of lactase protein, (b) defect in post-translational modification of precursor lactase to the mature enzyme, and (c) synthesis of an inactive, high molecular weight lactase with altered glycosylation, however, the precise underlying mechanism of adult-type hypolactasia remains undefined. The present review describes the recent developments in understanding the regulation of lactase expression and the possible mechanism of adult-type hypolactasia, as a cause of lactose intolerance.

Animals↗
PubMed1991

Studies on small intestinal mucosal morphology lactase activity and lactose hydrolysis rate in childhood with diarrhea.

Small intestinal mucosal morphology, lactase activity and lactose hydrolysis were examined by peroral intestinal biopsy and intraluminal perfusion of the small intestine in 28 patients with acute and chronic diarrhea. This study shows that lactase deficiency and mucosal damage are more common in childhood diarrhea, and there are positive correlations among intestinal morphology, lactase activity and lactose hydrolysis. A small bowel biopsy is useful both in establishing the diagnosis and guiding dietary treatment for infants with chronic diarrhea. The pathophysiologic mechanism of diarrhea is also discussed.

Child, Preschool↗