Steatorrhea and azotorrhea and their relation to growth and nutrition in adolescents and young adults with cystic fibrosis

Lapey, Allen; Kattwinkel, John; Agnese, Paul A. di Sant'; Laster, Leonard

doi:10.1016/s0022-3476(74)80712-2

Cited by 102 publications

(29 citation statements)

References 24 publications

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“…Nevertheless, during fat balance studies without pancreatic enzyme preparations, two of the patients absorbed more than 40% of the dietary lipids. Similar results have been reported by others (18,23). We have previously found that gastric contents collected during fasting often contain little or no lipase activity, but this enzyme activity is always present in samples of gastric contents obtained after feeding (9), and in this study, identical observations were made in CF patients.…”

Section: Discussionsupporting

confidence: 92%

See 1 more Smart Citation

Lingual Lipase. an Important Lipase in the Digestion of Dietary Lipids in Cystic Fibrosis?

Fredrikzon

Bläckberg

1980

Pediatr Res

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Section: Discussionsupporting

confidence: 92%

“…is often low or absent (18,19 (20) that a patient with pancreatic lipase deficiency absorbed erties of the triglyceride-hydrolyzing activities of lingual lipase around 5~ of !he dietary triglycerides.…”

Section: Discussionmentioning

confidence: 99%

Lingual Lipase. an Important Lipase in the Digestion of Dietary Lipids in Cystic Fibrosis?

Fredrikzon

Bläckberg

1980

Pediatr Res

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“…In patients with pancreatic diabetes, digestion and absorption of proteins are also disturbed due to pancreatic exocrine insufficiency (Lapey et al 1974; Twesky T. Nakamura et al…”

Section: Discussionmentioning

confidence: 99%

Increased Plasma Gluconeogenic and System A Amino Acids in Patients with Pancreatic Diabetes due to Chronic Pancreatitis in Comparison with Primary Diabetes.

Nakamura

Takebe

Kudoh

et al. 1994

Tohoku J. Exp. Med.

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We examined the plasma amino acid profiles of 17 patients with pancreatic diabetes in comparison with those of 14 healthy subjects and 16 patients with primary diabetes of similarly poor glycemic control. We also measured fasting plasma glucagon and free insulin levels in patients with pancreatic diabetes and in those with primary diabetes. The fasting plasma amino acid level was highest in patients with pancreatic diabetes. Furthermore, the plasma glucagon level in patients with pancreatic diabetes was significantly low, and negative correlations were found between glucagon and glucagon-related System A and gluconeogenic amino acids. On the other hand, the levels of branched-chain amino acids (BCAA) and System L amino acids, which are subjected to change in the state of diabetes mellitus, increased in patients with pancreatic diabetes. From the above results, we determined that the amino acid profile in patients with pancreatic diabetes resembled that in patients with total pancreatectomy. It is our opinion that the increases of amino acid levels (gluconeogenic and System A amino acids) in patients with pancreatic diabetes is not dependent on maldigestion/malabsorption under treatment, but is mainly dependent on glucagon deficiency. gluconeogenic and system A amino acids; pancreatic diabetes; hypoglucagonemia With regard to the relationship between amino acid metabolism and chronic pancreatitis, the following three points can be considered; 1) Abnormalities of amino acids as a cause of hereditary familial pancreatitis among chronic pancreatitis sufferers (Gross et al. 1957), 2) possible change in plasma amino acid profile due to malnutrition caused by maldigestion resulting from chronic pancreatitis and 3) abnormal amino acid metabolism due to secondary diabetes

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“…Likewise, in cystic fibrosis, a genetic disease resulting in severe pancreatic insufficiency (50), as much as 50-80% of dietary fat is absorbed in the absence of pancreatic lipase (38). Recent studies show that lingual lipase is well developed at birth [as early as 26 wk gestation (27)] and that it remains fully active in persons with cystic fibrosis (1, 56).…”

Section: Discussionmentioning

confidence: 99%

Fat Digestion in the Stomach: Stability of Lingual Lipase in the Gastric Environment

Fink

Hamosh

1984

Pediatr Res

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SummaryDigestion of dietary fat starts in the stomach, where lingual lipase hydrolyzes triglycerides to free fatty acids and partial glycerides at pH 3.0-6.0. Lingual lipase is secreted continuously from lingual serous glands and accumulates in the stomach between meals, when gastric pH is ~3 . 0 . We have, therefore, examined the resistance of lingual lipase to low pH and its possible protection by dietary components present in the stomach contents. Partially purified rat lingual lipase (7-15 pg enzyme protein) was preincubated at 37OC for 10-60 min at pH 1.0-6.0 before incubation for assay of lipolytic activity, hydrolysis of tri-['Hlolein at pH 5.4. The data show that partially purified rat lingual lipase preparations are stable at 37°C in the pH range of 2.5-6.0. Enzyme activity, however, is rapidly and irreversibly lost during preincubation at pH 1.0-2.4 for 10-30 min. Protein (gelatin 1% or albumin 1% or 2.5%) cannot prevent the inactivation of lingual lipase at low pH. The large molecular species (molecular weight >500,000) of lingual lipase (thought to be an aggregate of enzyme with lipids) is slightly more resistant to inactivation than the 46,000 dalton preparation, suggesting that lipids might protect the enzyme from inactivation. Indeed, about 60% of the initial lipase activity is preserved during incubation at pH 2.0 in the presence of 50 mM lecithin or 10 mM triolein. The data indicate that triglycerides which are hydrolyzed by this enzyme as well as phospholipids that are not hydrolyzed can prevent the inactivation of the enzyme. Lingual lipase is resistant to peptic digestion, even at high pepsin concentrations. Because of the special importance of lingual lipase in neonatal fat digestion, we compared the stability of the lipase in gastric aspirates of newborn infants to that of rat lingual lipase. The lipase in human gastric aspirates is more resistant to inactivation than the rat enzyme. There are however individual variations in enzyme stability: from preservation of 100% of original activity to the loss of 80% of activity during incubation for 30 min at pH 1.6. The data suggest that substances within the newborn infant's stomach stabilize the enzyme at low pH. We suggest that the extensive intragastric hydrolysis of dietary fat (in formula or breast milk) is related to the stability of the lipase in the stomach of newborn infants. Abbreviations BSA, bovine serum albumin FFA, free fatty acids Digestion of dietary fat by lingual lipase is initiated in the stomach of the newborn (4,28,29,40,63) and the adult (10, 26, 28, 5 1). Intragastric lipolysis results in the hydrolysis of 10-30% of dietary fat to partial glycerides and FFA (4,26,28,29,40,57,63). The products of intragastric lipolysis are amphiphilic substances (62) that facilitate fat emulsification (26) and enhance the intestinal hydrolysis of fat by pancreatic lipase (6). Recent studies show that the site of action of lingual lipase, an enzyme with optimal activity at pH 3.0-6.0, is not limited to the stomach, but continues in the duoden...

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Steatorrhea and azotorrhea and their relation to growth and nutrition in adolescents and young adults with cystic fibrosis

Cited by 102 publications

References 24 publications

Lingual Lipase. an Important Lipase in the Digestion of Dietary Lipids in Cystic Fibrosis?

Lingual Lipase. an Important Lipase in the Digestion of Dietary Lipids in Cystic Fibrosis?

Increased Plasma Gluconeogenic and System A Amino Acids in Patients with Pancreatic Diabetes due to Chronic Pancreatitis in Comparison with Primary Diabetes.

Fat Digestion in the Stomach: Stability of Lingual Lipase in the Gastric Environment

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