Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Colipases”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 433 records · Page 24Linked to original sources
PubMed1990

Inhibition of lipolysis by hydrocarbons and fatty alcohols.

The hydrolysis of long-chain triglyceride by pancreatic lipase (EC 3.1.1.3) is inhibited by hydrophobic solutes that are dissolved in the fat. Solutes tested included n-alkanes (C10-C16), aromatic and chlorinated aromatic hydrocarbons (including a PCB and DDT), n-alcohols (C10-C16), and cholesterol. Except for cholesterol, which stimulated lipolysis at low concentrations, all compounds produced roughly similar inhibition curves that followed the pattern of a typical Langmuir adsorption isotherm (Mattson, F. H., R. A. Volpenhein, and L. Benjamin, 1970. J. Biol. Chem. 245: 5335-5340). According to this interpretation, hydrophobic solutes dissolved within fat droplets partition between the interior oil phase and the surface monolayer where lipolysis occurs. Although the aromatic and chlorinated aromatic hydrocarbons were approximately 25% more inhibitory than the long-chain aliphatic hydrocarbons, as a single class, hydrocarbons were 7-10 times weaker inhibitors of lipolysis than fatty alcohols. In contrast to the alcohols whose inhibitory action may involve several mechanisms, the hydrocarbons behaved like simple dilution inhibitors; i.e., at 50% inhibition the mass ratio of hexadecane to triglyceride was 0.42. The lack of a chain length effect indicates that the hydrocarbons are not adsorbed at the interface but interdigitate the triglyceride molecules and align parallel to the lipid acyl chains. Inhibition by hydrophobic solutes was not reversed by the presence of 4 mM taurodeoxycholate and pancreatic procolipase or colipase.

Animals↗
PubMed1989

Diagnostic value of measuring pancreatic lipase and the P3 isoform of the pancreatic amylase isoenzyme in serum of hospitalized hyperamylasemic patients.

We assayed amylase (AMY) isoenzymes by cellulose acetate electrophoresis and determined pancreatic lipase (LPS) activity by a turbidimetric colipase-supplemented method in 54 hospitalized hyperamylasemic patients (32 men and 22 women; mean age 61.5, SD 16, years). In AMY isoenzyme analysis, use of a value for P3 isoform greater than 14 U/L as a positive test for acute pancreatitis gave a diagnostic efficiency of 92.6%, a predictive value of a positive test result of 90.5%, and a predictive value of a negative test of 100%. Four of 12 patients with other, nonpancreatic abdominal diseases had false-positive test results. LPS activity (cutoff limit, 700 U/L) was as effective as P3 isoform in distinguishing patients with acute pancreatitis (sensitivity, 100%) from those without acute pancreatitis (specificity, 81.3%). Thus, P3 isoform and LPS appear to be interchangeable markers of pathological release of pancreatic enzymes into the bloodstream during acute pancreatitis. This finding decreases the need for the expensive radiological procedures currently required to confirm this diagnosis. In particular, negative results virtually exclude acute pancreatitis.

Acute Disease↗
PubMed1986

[Nutrition of premature infants below 1,500 g: enteral prerequisites].

The development of the human fetal gastrointestinal tract takes place early during gestation. The pancreas although developed by morphological means at the 16th week of gestation excretes its exocrine enzymes later at the 24th week of gestation except for amylase which reaches its full activity 6 months after birth. Trypsinogen secreted at the 24th week is activated into trypsin by enterokinase at the 26th week of gestation whereas lipase and colipase are secreted from the 24th week. The small intestine starts developing at the 10th week morphologically and functionally. At the same time when villi and crypts start to develop at the 11th to 12th week the first enzyme activities can be detected, i.e. sucrase-isomaltase, maltase-glucoamylase and lactase. Also peptidases and lysosomal hydrolases are measured at this age. With the exception of lactase, intestinal enzymes reach sufficient activities at the 25th week of gestation. Lactase activity remains low until the 32nd-34th week. For the digestion and absorption of lipids, protein and carbohydrates the gastrointestinal tract of premature infants under 1500 g in rather well equipped. Lipids are hydrolysed by the mutual action of breast milk lipase, lingual lipase, gastric lipase and pancreatic lipase. The carbohydrates lactose and oligosaccharides as supplements to breast milk are hydrolysed by lactase, sucrase-isomaltase and maltase-glucoamylase. Breast milk proteins and cows milk hydrolysates are digested by pancreatic proteases into oligopeptides which can be hydrolysed within the lumen by brush border peptidases and be absorbed. Peptides also can actively be transported through the microvillus membrane and be hydrolyzed by intracellular peptidases.(ABSTRACT TRUNCATED AT 250 WORDS)

Dietary Carbohydrates↗
PubMed1986

An enzymatic method for calibration of serum lipase assays.

An enzymatic method for the calibration of a turbidimetric lipase assay is described, based on measurement of free fatty acids liberated by the action of lipase. The substrate of the turbidimetric assay is a colipase-containing triolein emulsion. For determination of the free fatty acids a commercial test kit including acyl-CoA synthetase, acyl-CoA oxidase, and peroxidase is used. Intra- and interassay imprecision (CV) is about 5% at above-normal lipase activities, about 10% at normal values. Temperature coefficients are 1.24 and 1.45, respectively, for measurements at 30 and 37 degrees C vs 25 degrees C.

Animals↗
PubMed1979

Hydrolysis of mixed monomolecular films of triglyceride/lecithin by pancreatic lipase.

The main purpose of this study was to describe the influence of lecithin upon lipolysis of mixed monomolecular films of trioctanoylglycerol/didodecanoylphosphatidycholine by pancreatic lipase in order to mimic some physiological situations. The quantity of enzyme adsorbed to the interface was simultaneously determined using 5-thio-2-nitro[14C]benzoyl lipase. Lipolytic activity was enhanced 3- to 4-fold in the presence of colipase, an effect which is attributed to increased enzyme turnover number. When a pure triglyceride film was progressively diluted with lecithin, the minimum specific activity of lipase exhibited a bell-shaped curve: a mixed film containing only 20% trioctanoylglycerol was hydrolyzed at the same rate as a monolayer of pure triglyceride.

Animals↗
PubMed1984

Differentiating two forms of plasma lipase by use of media with different ionic strengths.

Three different techniques of lipase (EC 3.1.1.3) determination (titrimetry, nephelometry, and enzyme immunoassay) were used to investigate an interesting effect of ionic strength on enzyme activity. Both activation in the presence of NaCl (140 mmol/L) and strong immunoinhibition were observed for lipase from plasma of subjects with acute pancreatitis. Another type of lipase, not associated with pancreatitis and only weakly immunoinhibited, showed maximum activity in the presence of 80 mmol/L NaCl. The pancreatitis-type lipase was activated by 140 mmol/L NaCl solution only if colipase and sodium deoxycholate were also present, which suggests that these components are cofactors in the activating effect and confirms the specificity of this property. These findings can be exploited to improve the diagnosis of acute pancreatitis.

Acute Disease↗
PubMed1981

Characterization of human exocrine pancreatic proteins by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis.

Exocrine proteins contained in human pancreatic juice were separated in two dimensions using isoelectric focusing and sodium dodecyl sulfate gel electrophoresis. Nineteen discrete proteins were found. Fifteen of these were identified by actual or potential enzyme activity and include three forms of trypsinogen, two forms each of procarboxypeptidase A, procarboxypeptidase B, proelastase, and colipase, and one form each for amylase, lipase, chymotrypsinogen, and prophospholipase A2. Lipase and four unidentified proteins were found to contain carbohydrate by the periodic acid Schiff staining method. Each pancreatic protein was characterized by isoelectric point and molecular weight. Proteins were quantitated according to relative mass, as measured by the incorporation of a mixture of 15 3H-amino acids into secretory proteins contained in tissue slices, and according to the distribution of Coomassie blue R stain among proteins contained in pancreatic juice, as determined by two-dimensional gel scanning and computer analysis. The second form of pancreatic procarboxypeptidase B (IEPn6.7) was present in only 4 of 10 subjects tested. Trypsinogens 1 and 3 were covalently labeled with 35SO4. Trypsin derived from trypsinogen 2 showed no inhibition with soybean trypsin inhibitor or Trasylol.

Carboxypeptidase B↗
PubMed1982

Steatorrhea and pancreatic insufficiency in Shwachman syndrome.

Fat absorption was assessed on two or more occasions in 12 of 14 patients with Shwachman syndrome. Of 11 children who initially had steatorrhea, 6 were subsequently found to have normal fat excretion. In 10 of these 11 patients the last estimate was smaller than the initial estimate after an interval of 0.3-12.7 yr. The most dramatic improvement occurred under 4 yr of age but improvement appeared to continue over a more extended period where sufficient follow-up was available. All patients had pronounced pancreatic insufficiency as tested by duodenal drainage corrected by nonabsorbable marker under stimulation with cholecystokinin and secretin. Pancreatic lipase secretion was assessed in 3 patients with steatorrhea and 5 without steatorrhea (73% of the surviving patients) using a sensitive assay which used maximum stimulation with colipase. Pancreatic lipase secretion was less than 2% of normal mean secretion in the steatorrheic patients and ranged from 3.7% to 13.6% in the patients without steatorrhea. These results indicate that fat absorption improves in the majority of patients with Shwachman syndrome and appears to be associated with marginal improvement in pancreatic lipase secretion. Due to the occult nature of bowel complaints in older patients, the diagnosis may be overlooked unless careful screening for pancreatic function takes place.

Adolescent↗
PubMed1982

[Determination of the catalytic activity of lipase by the continuous titration method].

Development of a standardized procedure for the titrimetric assay of lipase has been suggested. Comparative studies with triolein und olive oil were therefore undertaken. Optimal conditions, such as pH, substrate and glycocholate concentrations, etc. were determined for the assay with triolein. The results agree with those obtained earlier with olive oil as substrate. Experience with the quality of various reagents used since 1966 is reported. Problems of methodology are then discussed, especially the incomplete characterization and purity of the bile acid preparations, and their effects on the test conditions. A critical analysis shows that two point tests with modifications of the continuous titration cannot give reliable results. Haemolysis and its effect on catalytic activity of lipase are used to illustrate the consequences of the uncritical acceptance of data from the literature. Furthermore, the required sensitivity of the analytical equipment, operational errors, and the uncritical evaluation and interpretation of analytical data are discussed. The first experiments to be performed with the addition of colipase are described, and the question of whether this cofactor should be used routinely for test purposes is considered. The problem of whether lipoproteinlipase can be quantitatively inhibited is discussed. In view of the outlay on apparatus and the time required for the assay, continuous titration is definitely not suitable for routine screening purposes. On the other hand, simpler methods that give reproducible quantitative results have not yet been developed.

Catalysis↗
PubMed1993

Lipase in serum--the elusive enzyme: an overview.

Lipase is a glycoprotein with 420-449 amino acid residues and a M(r) of 46,000-56,000 for pancreatic lipase and 32,000-39,000 for serum lipase. Lipase is present in the pancreas, intestines, and a variety of other tissues. The concentration gradient between pancreatic tissue and serum lipase is approximately 20,000-fold. Serine, as part of an Asp-His-Ser triad, is the nucleophilic residue essential for catalysis. Lipase differs from other esterases by the presence of a hydrophobic recognition site. The optimal pH is between 7.5 and 10.0, depending on the reaction condition; the pI for the various forms of the enzyme has been reported as 5.80 and 5.85; 6.4, 6.8, and 7.0; and 7.4 for a purified fraction. Several authors report the presence of two molecular forms in the pancreas and three electrophoretic bands with lipolytic activity. In normal serum two bands have been observed; in pancreatitis as many as four bands have been seen. Lipolytic activity may not always be due to lipase. Assays specific for lipase require a triglyceride as substrate as well as the presence of colipase (a water-soluble and heat-stable protein, essential for lipase action), a secondary bile salt, and Ca2+. The clinical sensitivity of all modern assays is high because of selection of a low decision limit; the clinical specificity varies greatly but can be improved by increasing the cutoff point. Lipase determinations in pancreatitis are superior to amylase determinations. The reasons for the great variability of reports regarding the clinical utility of lipase are discussed, and the clinical utility of lipase determinations is summarized.

Chemical Phenomena↗
PubMed1997

Collection of pancreatic juice from growing pigs. A comparative study of the pouch method and the catheter method.

CONCLUSION: The results of this study demonstrate that there are large differences in the amount of pancreatic juice secreted and in the chemical and enzymatic composition of pancreatic juice when the pouch and the catheter methods were used, and these differences must be taken into consideration in future studies with either method. METHODS: A study was performed to compare the two most commonly used methods to collect pancreatic juice from growing pigs; namely, the pouch method (PM) and the catheter method (CM). In the first part of the study, three barrows (initial weight 37 kg) were fitted with a pancreatic pouch re-entrant cannula. An isolated pouch was prepared in which the pancreatic duct enters the duodenum. In the second part of the study, also with three barrows (initial weight 32 kg), a catheter was inserted into the pancreatic duct. RESULTS: At several points during the 24-h collection, the hourly rate of pancreatic juice secretion in CM pigs was larger (p < 0.05) than for PM pigs. CM pigs also had a higher (p < 0.05) daily volume of secretion, 4.09 vs 2.63 L/24 h for PM pigs. The pH of pancreatic juice collected from CM pigs was consistently higher (p < 0.01) throughout the 24-h collection. In contrast, the concentration and daily output of bicarbonate did not differ between CM and PM pigs. The concentration of protein in pancreatic juice from PM pigs (7.21 g/L) was higher (p < 0.001) than for CM pigs (4.08 g/L). Specific amylase and lipase and total amylase activities were greater (p < 0.01) in pancreatic juice collected from PM pigs. Specific and total carboxyl ester hydrolase and colipase activities were substantially (p < 0.01) larger in pancreatic juice collected from CM pigs. A major difference between the methods was that trypsin and chymotrypsin were fully active in pancreatic juice from PM pigs, whereas virtually no trypsin or chymotrypsin activity was detected in pancreatic juice from CM pigs. Specific and total chymotrypsin activities did not differ between PM and CM pigs. Both specific and total trypsin activities were substantially higher in pancreatic juice from CM pigs: 3682 U/L and 12,752 U/24 h, respectively, vs 1031 U/L and 2639 U/24 h, respectively, in pancreatic juice from PM pigs.

Animals↗
PubMed1993

Effect of enterostatin on the feeding responses to galanin and NPY.

We have investigated the possibility that enterostatin may inhibit the intake of dietary fat by inhibiting either galanin or NPY-induced feeding pathways. Rats, adapted to either high fat (HF) or low fat-high carbohydrate (HC) diets and fitted with third ventricular cannulas were used to study the effects of intracerebroventricular (i.c.v.) enterostatin on i.c.v. NPY and galanin induced feeding responses in satiated rats. An equimolar dose of enterostatin (0.1 nmoles) inhibited, while a tenfold excess of enterostatin abolished the feeding response to galanin in rats adapted to a HF diet. The galanin stimulation of food intake was reduced in rats adapted to the HC diet and this response was less sensitive to inhibition by enterostatin. Enterostatin had no inhibitory effects on NPY-induced feeding in rats adapted to the HC diet and only a small inhibitory effect, at tenfold molar excess, in rats adapted to the HF diet. The ability of enterostatin to bind to galanin or NPY Y-1 receptors was investigated in ligand binding studies. Enterostatin failed to displace 125I-galanin or 125I-PYY from specific binding sites in rat forebrain homogenates or SK-N-MC cells respectively. The data provide support for the hypothesis that enterostatin specifically inhibits a galanin-responsive fat intake system, but indicate that this effect is not modulated by direct interaction with either galanin or NPY-Y1 receptors.

Analysis of Variance↗
PubMed1994

Vagal-central nervous system interactions modulate the feeding response to peripheral enterostatin.

Enterostatin selectively inhibits the intake of dietary fat after both peripheral and central administration. We have investigated the role of the hepatic vagus nerve in modulating the peripheral response to enterostatin in Sprague-Dawley rats adapted to a high fat (HF) diet. Intraperitoneal (ip) enterostatin reduced intake of HF diet after overnight starvation. This response was abolished by selective vagal hepatic branch transection. Immunohistochemical techniques were used to identify the location of Fos protein in brain nuclei after ip enterostatin. Fos protein was evident in the nucleus tractus solitarius (NTS), parabrachial, paraventricular and supraoptic nuclei. The pattern of expression of Fos-like immunoreactivity differed from that induced by the lipoprivic agent beta-mercaptoacetate. Transection of the hepatic vagus blocked the central Fos responses to ip enterostatin. We conclude that afferent hepatic vagal nerve activity is required for the feeding response to peripheral enterostatin.

Animals↗
PubMed1996

Plasma insulin in response to enterostatin and effect of adrenalectomy in rats.

Enterostatin has previously been reported to alter serum insulin and corticosterone levels after central administration of the peptide. The purpose of the present study was to investigate the effect of peripheral administration of enterostatin on insulin and corticosterone levels as well as the response of plasma insulin to enterostatin administration in adrenalectomized rats. Female Sprague-Dawley rats were given a bolus injection intravenously with enterostatin alone or together with glucose. Enterostatin increased basal plasma levels of insulin, but significantly inhibited the increase in plasma insulin stimulated by glucose. Plasma corticosterone levels were not altered after a single intravenous injection of enterostatin. In rats infused chronically with enterostatin, plasma insulin levels were significantly reduced and plasma corticosterone levels were increased. The daily food intake was lower in these rats, but there was no effect on body weight. After adrenalectomy, the responsiveness of plasma insulin to enterostatin infusion was completely abolished. Furthermore, adrenalectomy itself reduced basal plasma levels of insulin and increased plasma levels of endogenous enterostatin. These results suggest that peripheral enterostatin administration produces a similar effect as central infusion of the peptide, and that the glucocorticoid hormones are involved in the regulation of plasma insulin by enterostatin.

Adrenalectomy↗
PubMed1996

Role of intraduodenally administered enterostatin in rats: inhibition of food.

Central and peripheral administration of enterostatin have been reported to reduce fat or high-fat food intake in rats. Enterostatin is formed in the intestinal lumen by tryptic cleavage of pancreatic procolipase during intraluminal fat digestion. The present experiments were designed to test if enterostatin following intraintestinal infusion would affect food intake in a similar way as intracerebraventricularly or intravenously administered enterostatin. Female Sprague-Dawley rats were fitted with a duodenal catheter and adapted to feeding schedule for 6 hours each day. After 10 days enterostatin (5.65 and 11.3 nmol/kg/min) or saline were infused into the duodenum and food intake measured. Enterostatin significantly reduced high-fat food intake during the 6 hours of feeding, but had no inhibitory effect on low-fat food intake. Addition of tetracaine to the enterostatin infusates blocked the satiating potency of intestinal enterostatin. These results support the hypothesis of a preabsorptive site of action for enterostatin.

Anesthetics, Local↗
PubMed1998

Effects of enterostatin on consumption of optional foods in non-food-deprived rats.

Enterostatin, the activation peptide of procolipase, has been reported to reduce high-fat food consumption in rats. This reduction has been reliably demonstrated using procedures in which the test diet was also the maintenance diet of the animals. Other reports, though, have shown that peripherally administered enterostatin had no effect on the consumption of oil provided as an option to the diet, and that centrally administered enterostatin had no effect on the consumption of an optional high-fat mixed food. However, the effects of peripherally administered enterostatin on the consumption of an optional high-fat mixed food have not been examined. This experiment, then, examined the effects of peripherally administered enterostatin on the consumption of optional, mixed foods (no-fat and high-fat cookies) provided in addition to a standard diet under choice and nonchoice conditions. Four experiments were conducted. In experiment I, the effect of enterostatin in a two-choice feeding paradigm was assessed. In experiment II, the effect of enterostatin in a nonchoice feeding paradigm was assessed. In experiment III, the effect of enterostatin administered at five different pretreatment times in a non-choice feeding paradigm was assessed. Enterostatin had no effect on cookie intake in any of these experiments. Finally, experiment IV was undertaken to verify the activity of the peptide. Enterostatin significantly reduced the consumption of a standard diet in overnight food-deprived rats, thus confirming the activity of the peptide used in experiments I to III. Enterostatin may not play a major role in the regulation of food intake that is stimulated by optional foods that are periodically provided in addition to a standard well-balanced diet.

Animals↗
PubMed1983

Killing of Giardia lamblia trophozoites by normal human milk.

The clinical course of giardiasis is variable, and serum antibodies do not appear to be protective. We propose that natural factors either produced by intestinal tissue, transported into the intestine, or ingested (ie, by breast-fed babies) might promote resistance to this disease. Human milk is very rich in secretory IgA (S-IgA) antibodies, as well as nonspecific antibacterial factors (eg, lactoferrin, lysozyme). Previous studies showed that Giardia lamblia trophozoites were killed by nonimmune human milk (NHM) in a time- and concentration-dependent manner. Removal of greater than 99% of the S-IgA from NHM did not decrease its Giardia-cidal activity. Thus, the killing was not antibody dependent. This is the first demonstration of nonimmune antiparasitic defenses in human milk. The present studies show that in the presence of NHM, trophozoites lost motility, swelled, and lysed. The Giardia-cidal activity (GCA) may be specific to human milk, since unheated cow's and goat's milk were virtually devoid of activity. Much, but not all, of the GCA was lost when NHM was heated or reacted with diisopropylfluorophosphate (DIFP), a specific esterase inhibitor. Activity of the major human milk lipase (BSL, bile salt-stimulated lipase, a fatty acid esterase) was lost after heat or DIFP treatment and was absent from cow's or goat's milk. The parasites were also killed by pure BSL. These studies suggest that BSL may be a heat-labile Giardia-cidal component of NHM.

Animals↗