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PubMed1993

Post-prandial lipase, pepsin and acid secretion of a Heidenhain pouch in the rabbit.

The kinetics of the gastric secretion of lipase, pepsin and acid were studied after a meal in Heidenhain-pouch rabbits. After a 24-h fast, feeding immediately stimulated (< 15 min) lipase (x 4.1) and later on pepsin (x 1.8) output which reached respectively 16 and 47% of the output observed after pentagastrin stimulation (64 micrograms.kg-1.h-1 for 1 h), and which were significantly correlated. Lipase concentration was enhanced earlier and to a greater degree (x 7.3) than pepsin concentration (x 2.5). No stimulation of high basal acid secretion occurred. It was concluded that: 1) gastric lipase secretion is stimulated by feeding in the rabbit; 2) pepsin secretion is stimulated by feeding. The modalities of the secretion of lipase and pepsin are compatible with the existence of distinct secretory cells; 3) acid secretion is not stimulated by feeding. The decrease in acid secretion during the post-prandial phase favors a physiological role for lipase which is altered by low pH. The absence of acid stimulation by feeding in the rabbit, in contrast to other species, requires additional studies on the release of gastrointestinal hormones, namely gastrin, cholecystokinin and somatostatin.

Animals↗
PubMed2002

Asymptomatic elevation of serum lipase and amylase in conjunction with Crohn's disease and ulcerative colitis.

BACKGROUND AND OBJECTIVE: Elevated serum lipase and amylase are often observed in IBD patients (Crohn's disease and ulcerative colitis) without clinical symptoms of a pancreatitis. The intention of this prospective study is to evaluate the frequency of elevated serum lipase and amylase with these patients and to try to explain this phenomenon in consideration of the existing literature. PATIENTS AND METHODS: 136 IBD patients (MC: 66; CU: 70) participated in this prospective study which lasted 3 months. All patients with increased levels of serum lipase and amylase were prospectively followed-up for another 3 months. RESULTS: We found an asymptomatic elevation of serum lipase and amylase without symptoms of a pancreatitis in 14 % of the observed IBD patients. A significance between the elevation of lipase/amylase and the activity index (CDAI,CAI) or the CRP level could not be found. A significant increase of lipase/amylase (more than twice the normal standard) was shown more often in lipase (4.4 %) than in amylase levels (0.7 %). The possible reasons for an asymptomatic increase of lipase/amylase in IBD patients (e. g. latent extra-intestinal involvement of the pancreas in IBD with pancreatitis; extra-pancreatic release of lipase/amylase from the inflammatory bowel; intestinal reabsorption of released lipase/amylase in the inflammatory bowel) are discussed in this text. CONCLUSION: An asymptomatic elevation of lipase/amylase in IBD patients is not infrequent (14 %). The increase of lipase or amylase, without typical symptoms, makes a pancreatitis with a required therapy unlikely. A specific pancreatitis therapy is not necessary in these cases. The therapy should be guided by the requirements of the IBD therapy.

Adolescent↗
PubMed1979

Increase in lipoprotein lipase during clofibrate treatment of hypertriglyceridemia in patients on hemodialysis.

In 11 hypertriglyceridemic patients on hemodialysis, clofibrate (1 to 1.50 g per week) reduced plasma triglyceride (-40 +/- 20%, P less than 0.001), very-low-density-lipoprotein triglyceride (-44 +/- 20%, P less than 0.001) and very-low-density lipoprotein cholesterol (-39 +/- 25%, P less than 0.01), and it increased high-density-lipoprotein cholesterol (82 +/- 106%, P less than 0.005). Low pretreatment lipoprotein-lipase activity in adipose-tissue specimens and postheparin plasma increased to normal with clofibrate, whereas low hepatic triglyceride lipase activity did not change. The reduced very-low-density-lipoprotein triglyceride correlated with the increased lipoprotein-lipase activity in adipose tissue (rs = 0.792, P less than 0.02, n = 8) and postheparin plasma (rs = 0.851, P less than 0.02, n = 8), whereas increased high-density-lipoprotein cholesterol correlated with changes in this activity in adipose tissue (rs = 0.696, P less than 0.06) and post-heparin plasma (rs = 0.679, P less than 0.10). There was no correlation between changes in hepatic triglyceride lipase activity and plasma lipids during treatment. Reduced lipoprotein-lipase activity may cause hypertriglyceridemia and decreased high-density-lipoprotein cholesterol in patients on hemodialysis; clofibrate may correct these abnormalities by increasing lipoprotein-lipase activity to normal.

Adipose Tissue↗
PubMed1996

Premature atherosclerosis in patients with familial chylomicronemia caused by mutations in the lipoprotein lipase gene.

BACKGROUND: Patients with lipoprotein lipase deficiency usually present with chylomicronemia in childhood. The syndrome has been considered nonatherogenic primarily because of the low levels of low-density lipoprotein (LDL) cholesterol. We prospectively evaluated patients with lipoprotein lipase deficiency for atherosclerosis. METHODS: Evidence of carotid, peripheral, and coronary atherosclerosis was sought in four patients (two men and two women) with the phenotype of familial chylomicronemia by clinical examination over a period of 14 to 30 years and by Doppler ultrasonography, B-mode ultrasonography [corrected], and exercise-tolerance testing after the age of 40. Angiography was performed when indicated. Lipoprotein lipase deficiency was assessed in vivo and in vitro by functional assays and DNA-sequence analysis. RESULTS: All four patients had a profound functional deficiency of lipoprotein lipase with a reduced enzymatic mass due to missense mutations on both alleles of the lipoprotein lipase gene. In all four patients, peripheral or coronary atherosclerosis (or both) was observed before the age of 55. Despite following a low-fat diet in which fat composed 10 to 15 percent of the daily caloric intake, the patients had hypertriglyceridemia (mean [+/- SD] triglyceride level, 2621 +/- 1112 mg per deciliter [29.59 +/- 12.55 mmol per liter]), low plasma levels of high-density lipoprotein cholesterol (17 +/- 7 mg per deciliter [0.43 +/- 0.18 mmol per liter]), and very low levels of LDL cholesterol (28 +/- 16 mg per deciliter [0.72 +/- 0.41 mmol per liter]). Three patients had one risk factor for atherosclerosis, whereas in one male patient, heavy smoking and diabetes were associated with an accelerated course of the disease. CONCLUSIONS: Premature atherosclerosis can occur in patients with familiar chylomicronemia as a result of mutations in the lipoprotein lipase gene. Defective lipolysis may increase susceptibility to atherosclerosis in humans.

Aged↗
PubMed2000

An ethylene-induced cDNA encoding a lipase expressed at the onset of senescence.

A cDNA clone encoding a lipase (lipolytic acyl hydrolase) expressed at the onset of petal senescence has been isolated by screening a cDNA expression library prepared from carnation flowers (Dianthus caryophyllus). The cDNA contains the lipase consensus sequence, ITFAGHSLGA, and encodes a 447-amino acid polypeptide with a calculated molecular mass of 50.2 kDa that appears to be a cytosolic protein. Over-expression of the clone in Escherichia coli yielded a protein of the expected molecular weight that proved capable of deesterifying fatty acids from p-nitrophenylpalmitate, tri-linolein, soybean phospholipid, and Tween in both in vitro and in situ assays of enzyme activity. The abundance of the lipase mRNA increases just as carnation flowers begin to senesce, and expression of the gene is also induced by treatment with ethylene. Southern blot analyses of carnation genomic DNA have indicated that the lipase is a single copy gene. The lipase gene is also expressed in carnation leaves and is up-regulated when the leaves are treated with ethylene. Deesterification of membrane lipids and ensuing loss of membrane structural integrity are well established early events of plant senescence, and the expression pattern of this lipase gene together with the lipolytic activity of its cognate protein indicate that it plays a fundamentally central role in mediating the onset of senescence.

Amino Acid Sequence↗
PubMed2001

Crystal structure of the open form of dog gastric lipase in complex with a phosphonate inhibitor.

Fat digestion in humans and some mammals such as dogs requires the successive intervention of two lipases: gastric lipase, which is stable and active despite the highly acidic stomach environment, followed by the classical pancreatic lipase secreted into the duodenum. We previously solved the structure of recombinant human gastric lipase (HGL) at 3.0-A resolution in its closed form; this was the first structure to be described within the mammalian acid lipase family. Here we report on the open structure of the recombinant dog gastric lipase (r-DGL) at 2.7-A resolution in complex with the undecyl-butyl (C11Y4) phosphonate inhibitor. HGL and r-DGL show 85.7% amino acid sequence identity, which makes it relevant to compare the forms from two different species. The open r-DGL structure confirms the previous description of the HGL catalytic triad (Ser(153), His(353), and Asp(324)) with the catalytic serine buried and an oxyanion hole (NH groups of Gln(154) and Leu(67)). In r-DGL, the binding of the C11Y4 phosphonate inhibitor induces part of the cap domain, the lid, to roll over the enzyme surface and to expose a catalytic crevice measuring approximately 20 x 20 x 7 A(3). The C11Y4 phosphonate fits into this crevice, and a molecule of beta-octyl glucoside fills up the crevice. The C11Y4 phosphonate inhibitor and the detergent molecule suggest a possible binding mode for the natural substrates, the triglyceride molecules.

Animals↗
PubMed2004

Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities.

Genetic knockout of hormone-sensitive lipase in mice has implicated the presence of other intracellular triacylglycerol (TAG) lipases mediating TAG hydrolysis in adipocytes. Despite intense interest in these TAG lipases, their molecular identities thus far are largely unknown. Sequence data base searches for proteins containing calcium-independent phospholipase A2 (iPLA2) dual signature nucleotide ((G/A)XGXXG) and lipase (GXSXG) consensus sequence motifs identified a novel subfamily of three putative iPLA2/lipase family members designated iPLA2epsilon, iPLA2zeta, and iPLA2eta (previously named adiponutrin, TTS-2.2, and GS2, respectively) of previously unknown catalytic function. Herein we describe the cloning, heterologous expression, and affinity purification of the three human isoforms of this iPLA2 subfamily in Sf9 cells, and we demonstrate that each possesses abundant TAG lipase activity. Moreover, iPLA2epsilon, iPLA2zeta, and iPLA2eta also possess acylglycerol transacylase activity utilizing mono-olein as an acyl donor which, in the presence of mono-olein or diolein acceptors, results in the synthesis of diolein and triolein, respectively. (E)-6-(Bromomethylene)-3-(1-naphthalenyl)-2H-tetrahydropyran-2-one, a mechanism-based suicide substrate inhibitor of all known iPLA2s, inhibits the triglyceride lipase activity of each of the three isoforms similarly (IC50=0.1-0.5 microm). Quantitative PCR revealed dramatically increased expression of iPLA2epsilon and iPLA2zeta transcripts during the hormone-induced differentiation of 3T3-L1 cells into adipocytes and identified the presence of all three iPLA2 isoforms in human SW872 liposarcoma cells. Collectively, these results identify three novel TAG lipases/acylglycerol transacylases that likely participate in TAG hydrolysis and the acyl-CoA independent transacylation of acylglycerols, thereby facilitating energy mobilization and storage in adipocytes.

3T3-L1 Cells↗
PubMed2005

Role of the lid hydrophobicity pattern in pancreatic lipase activity.

Pancreatic lipase is a soluble globular protein that must undergo structural modifications before it can hydrolyze oil droplets coated with bile salts. The binding of colipase and movement of the lipase lid open access to the active site. Mechanisms triggering lid mobility are unclear. The *KNILSQIVDIDGI* fragment of the lid of the human pancreatic lipase is predicted by molecular modeling to be a tilted peptide. Tilted peptides are hydrophobicity motifs involved in membrane fusion and more globally in perturbations of hydrophobic/hydrophilic interfaces. Analysis of this lid fragment predicts no clear consensus of secondary structure that suggests that its structure is not strongly sequence determined and could vary with environment. Point mutations were designed to modify the hydrophobicity profile of the [240-252] fragment and their consequences on the lipase-mediated catalysis were tested. Two mutants, in which the tilted peptide motif was lost, also have poor activity on bile salt-coated oil droplets and cannot be reactivated by colipase. Conversely, one mutant in which a different tilted peptide is created retains colipase dependence. These results suggest that the tilted hydrophobicity pattern of the [240-252] fragment is neither important for colipase binding to lipase, nor for interfacial binding but is important to trigger the maximal catalytic efficiency of lipase in the presence of bile salt.

Algorithms↗
PubMed2005

Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles.

Triacylglycerol (TAG) lipases are required for mobilization of TAG stored in lipid particles. Recently, Tgl3p was identified as a major TAG lipase of the yeast Saccharomyces cerevisiae (Athenstaedt, K., and Daum, G. (2003) J. Biol. Chem. 278, 23317-23323). Here, we report the identification of Tgl4p and Tgl5p as additional TAG lipases of the yeast. Both polypeptides, encoded by open reading frames YKR089c/TGL4 and YOR081c/TGL5, share 30 and 26% homology, respectively, to Tgl3p. Cell fractionation experiments and microscopic inspection of strains bearing Tgl4p-GFP and Tgl5p-GFP hybrids demonstrated that both proteins are localized to lipid particles similar to Tgl3p. A 1.7-fold increased amount of TAG enriched in myristic and palmitic acids and the reduced mobilization rate of TAG from tgl4Delta in the presence of the fatty acid synthesis inhibitor cerulenin demonstrated the lipolytic function of Tgl4p in vivo. In contrast, neither the total amount of TAG nor the TAG mobilization rate after addition of cerulenin was affected in tgl5Delta cells. However, the enrichment of C26:0 esterified to TAG of tgl5Delta, an additional increase of TAG in the tgl4Deltatgl5Delta double deletion mutant compared with tgl4Delta, and the impairment of TAG mobilization in the tgl4Deltatgl5Delta strain in the presence of cerulenin suggested that also Tgl5p functions as a TAG lipase in vivo. Most importantly, the purified His(6)-tagged Tgl4p and Tgl5p hybrids exhibited TAG lipase activity demonstrating their function in vitro. In summary, our data obtained by biochemical, molecular, and cell biological analyses unambiguously identified Tgl4p and Tgl5p as novel TAG lipases of yeast lipid particles with certain enzymatic specificities.

Amino Acid Sequence↗
PubMed2003

The combined use of whole Cuphea seeds containing medium chain fatty acids and an exogenous lipase in piglet nutrition.

In search for an alternative for nutritional antimicrobials in piglet feeding, the effects of adding whole Cuphea seeds, as a natural source of medium chain fatty acids (MCFA), with known antimicrobial effects, and an exogenous lipase to a weaner diet were studied. The foregut flora, the gut morphology, some digestive parameters and the zootechnical performance of weaned piglets were investigated. Thirty newly weaned piglets, initial weight 7.0 +/- 0.4 kg, were divided according to litter, sex and weight in two groups (control diet; Cuphea + lipase diet). The Cuphea seeds (lanceolata and ignea) (50 g kg(-1)) were substituted for soybean oil (15 g kg(-1)), Alphacell (25 g kg(-1)) and soy protein isolate (10 g kg(-1)) in the control diet. Also 500 mg kg(-1) microbial lipase was added to the Cuphea diet. The piglets were weighted individually on days 0, 3. 7, 14 and 16. Feed intake was recorded per pen during days 0 to 3, 3 to 7, 7 to 14 and 14 to 16. On day 7 five piglets of each experimental group were euthanized for counting the gastric and small intestinal gut flora and for gut morphology at two sites of the small intestine (proximal, distal). The results indicate a trend towards improved performances parameters by feeding Cuphea + lipase. The enzymic released MCFA (1.7 g kg(-1) fresh gastric contents) tended to decrease the number of Coliforms in the proximal small intestine, but increased the number in the stomach and distal small intestine. With Culphea, the number of Streptococci was significantly lower in small intestine, but not in the stomach, while the number of Lactobacilli was significantly lower in the distal small intestine and tended to be lower in the stomach and proximal small intestine. No differences between the diets were noted for the total anaerobic microbial load in the stomach or in the gut. Feeding Cuphea + lipase resulted in a significantly greater villus height (distal small intestine) and a lesser crypt depth (proximal and distal small intestine) and greater villus/crypt ratio depth (proximal and distal small intestine). The intra-epithelial lymphocyte (IEL) counts per 100 enterocytes were significantly decreased in the proximal small intestine and tended to decrease in the distal small intestine by feeding the Cuphea + lipase diet. Both phenomena are indicative for a more healthy and better functional state of the mucosa. Present results are in line with foregoing research, showing that manipulation of the gut ecosystem by the enzymic in situ released MCFA in the stomach and foregut can result in improved performances of the piglets, which makes the concept a potential alternative for in-feed nutritional antibiotics.

Animal Feed↗
PubMed1993

Lipase of Malassezia furfur: some properties and their relationship to cell growth.

Lipase activity of Malassezia furfur, detected with alpha-naphthyl palmitate as a substrate, appeared to be associated with the insoluble fraction of the organism. Profiles of M. furfur lipase were similar to those of Candida cylindracea lipase. The pH optimum of the lipase was acidic, pH 5.0, which is very similar to skin surface pH. The enzyme activity was strongly activated by a lipase activator, sodium taurocholate (STC). Addition of STC to the culture medium activated cell growth in a dose-dependent manner and induced hyphae production. These results suggest that M. furfur lipase plays an important role in cell growth.

Cell Division↗
PubMed2005

Adsorption of lipase on hollow fiber membrane chips.

The amount of lipase from Mucor miehei adsorption on ultrafiltration polysulfone hollow fiber membrane chips has been determined using different lipase concentrations at three different temperatures, namely 30, 35, and 40 degrees C. It was experimentally shown that adsorption of lipase increases with temperature. The results were used to evaluate the constants found in the Langmuir adsorption isotherm model coupled with the Van't Hoff's relationship. A temperature dependence correlation for the amount of adsorbed lipase activity, alip,ads, and that present in the supernatant solution, alip,free was determined. The effect of varying the concentration on a cross-linking agent, namely, glutaraldehyde, to the membrane chips was also tested. It was found that, under the same operating conditions, the amount of lipase adsorbed on polysulfone membranes was increased dramatically after pre-treating the membrane with 1% Glutaraldehyde. However, increasing the concentration of the cross-linking agent has a low effect on the amount of lipase adsorbed.

Adsorption↗
PubMed1999

Circulating human hepatic lipase mRNA in patients with hepatocellular carcinoma and healthy controls.

OBJECTIVE: To evaluate circulating human hepatic lipase mRNA as an indicator of circulating hepatoma cells by reverse transcriptase-polymerase chain reaction (RT-PCR) in patients with hepatocellular carcinoma (HCC). DESIGN: Prospective study SETTING: University hospital, Germany. SUBJECTS: 15 patients with hepatocellular carcinoma and 8 healthy volunteers. INTERVENTIONS: Peripheral venous blood was obtained and total RNA was extracted from the lymphocytic layer by caesium chloride gradient centrifugation. The mRNA was reverse transcripted, and hepatic lipase cDNA was amplified by hepatic lipase specific primers with PCR. The integrity of isolated RNA was confirmed by RT-PCR with beta-actin specific primers. Amplificates were visualised by agarose gel electrophoresis and ethidium bromide staining. MAIN OUTCOME MEASURES: Detection of hepatic-lipase-specific RT-PCR products in peripheral blood. RESULTS: Circulating hepatic lipase-specific PCR products were detected in all patients with HCC and in all healthy controls. CONCLUSION: Detection of circulating human hepatic lipase-mRNA by RT-PCR does not indicate metastasising HCC.

Biomarkers, Tumor↗
PubMed2003

Effect of lipid excipients on in vitro pancreatic lipase activity.

PURPOSE: To study the effects of two lipid excipients, Peceol and Gelucire 44/14 on the in vitro pancreatic lipase activity. METHODS: A 50 microL reaction mixture, consisting of 45 microL (3H) triolein as the radiolabeled substrate, 2.5 microL Peceol or Gelucire 44/14 (0.05-0.5%), either alone or in combination, 2.5 microL colipase (100 microg/mL), and 2.5 microL pancreatic lipase (1 mg/mL), was incubated for 10 min at room temperature. At the end of incubation, the reaction was stopped by the addition of an extraction solvent containing chloroform, methanol, and n-heptane (12.5:14:10), and the mixture vortexed briefly. Subsequently, 250 microL of 50 mM sodium carbonate was added and the aqueous and organic phase separated by centrifugation for 5 min at 1000 g. One hundred microliters of the supernatant was transferred to a scintillation counter and then radioactivity measured after the addition of 3.6 mL of scintillation fluid. Pancreatic lipase activity was determined by measuring the amount of free fatty acid released into the incubation medium and expressed as micromol free fatty acid released/min. RESULTS: When used alone, Peceol inhibited the pancreatic lipase activity significantly in a concentration-dependent manner, with a maximum inhibition of 57% at 0.4% of the excipient [p < 0.05, one-way analysis of variance (ANOVA)]. Similarly, Gelucire 44/14 alone caused inhibition of lipase activity in a concentration-dependent manner. However, the maximum inhibition (30%) was smaller in magnitude compared with the former agent. When the two excipients were used in combination, the inhibitory effects on the enzyme activity were similar to those observed with the individual agents (p < 0.05, one-way ANOVA). However, the maximum inhibition of 30% was lower than that observed with Peceol alone. CONCLUSIONS: The results from this study suggest that these lipid excipients inhibit in vitro pancreatic lipase activity and should be taken into consideration when developing oral formulations using these agents.

Excipients↗
PubMed2005

Modification of porcine pancreatic lipase with Z-proline.

Porcine pancreatic lipase was modified with Z-proline via the constitution of amide bonds between the free amino groups of lipase and the carboxyl groups of Z-proline, which were activated by 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC). Different amounts of Z-proline were bound to lipase. Modification degree was determined by 2,4,6-trinitrobenzene sulphonic acid (TNBS), by means of the decrease in free amino groups on lipase. The reason for choosing Z-proline was its unique structural characteristics, protected amino groups, and its effect on protein conformation by reducing the flexibility of the lipase molecule, thus achieving stabilization against changes in pH and temperature. After the modification, porcine pancreatic lipase was found to have new physicochemical characteristics, such as optimum alkaline pH stability and thermal stability at elevated temperatures.

Animals↗
PubMed1978

Rapid amylase and lipase determinations by nephelometry.

The Coleman 91 nephelometer provides rapid, simple amylase and lipase assays, which are particularly suited to emergency requests. Linearity of amylase compares favorably with that of the Phadebas assay, and comparable precision was obtainable with serum and urine. Normal ranges for serum amylase are slightly higher than those based on the amyloclastic end-point assay. The serum lipase assay shows improved linearity over titrimetric procedures, although kinetics remain variably non-linear. Occasional sera show discordantly elevated nephelometric lipase and normal titrimetric lipase. Precision of the nephelometric lipase assay is somewhat lower than that of amylase; normal ranges are considerably higher than those based on titrimetry. Extremely lactescent sera may yield falsely low nephelometric amylase and lipase activities: these sera must be serially diluted to achieve actual values.

Amylases↗
PubMed1978

Transiently elevated apparent lipase by nephelometry.

Occasional patient sera showing normal or minimally elevated lipase activity in the 6-hour titrimetric assay and discordantly high lipase activity in the 6-minute nephelometric assay were encountered. Most of these sera had normal amylase activity. They represented about 1% of outpatient sera subjected to amylase assay. A few sera with discordant lipase activities showed elevated amylase activities and were from patients with the diagnosis of pancreatic dysfunction. Nephelometric lipase assay in these sera showed pronounced nonlinear kinetics; in the most discordant cases a gradual decay of initially high activity to zero occurred. Elevated nephelometric lipase activity was lost inordinately in serial dilution of serum or on serial reduction of undiluted assay volume. In tracer experiments, two of these sera liberated no significant amount of free fatty acids after extensive "de-emulsification" of the nephelometric substrate mixture. This nonlipolytic "deemulsifying" activity was found to be relatively heat-stable in one serum. The nature of this activity remains obscure. A simple and effective protocol is suggested to detect and identify these aberrant nephelometric lipases in the routine laboratory.

Amylases↗
PubMed1987

Human serum pancreatic lipase and trypsin 1 in aging: enzymatic and immunoenzymatic assays.

Two major human pancreatic proteins, lipase and trypsin I, were measured in human sera from 35 elderly healthy adults and 51 young healthy adults. Lipase enzymatic activity was determined by a turbidimetric assay in the presence of colipase; lipase immunoreactive protein and trypsin immunoreactive protein were measured by using immunoenzymatic assays. Serum levels of the pancreatic enzymes were similar in young and elderly adults, with no significant differences between the groups for any of the assays. There was a close correlation between lipase enzyme activity and immunoreactivity in all participants, suggesting that the catalytic activity of lipase was not affected by aging. There were also significant correlations between the levels of immunoreactive lipase protein and immunoreactive trypsin protein, within and between the two groups, suggesting an age-independent relationship between these two pancreatic enzymes.

Adult↗