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Lipase

An enzyme that assists in the breakdown and digestion of fat in the body and arteries.

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Published Clinical Studies
Lipase

  • Plant sources of acid stable lipases: potential therapy for cystic fibrosis.
  • Lipoprotein lipase: structure, function, regulation, and role in disease.
  • Pancreatic enzyme replacement therapy.

Plant sources of acid stable lipases: potential therapy for cystic fibrosis.

Tursi JM, Phair PG, Barnes GL.

Department of Gastroenterology, Royal Children's Hospital, Parkville, Victoria, Australia.

Exogenous lipase used in the treatment of pancreatic insufficiency may be destroyed by stomach acid. This study was undertaken to search for a readily availa  ble source of acid stable lipase. Eleven plant sources (avocado, walnut, pinenut, coconut, lupin, lentils, chickpea, mungbean, oats, castor beans and eggplant) were screened for lipolytic activity using a newly developed radio-isotopic labelled substrate method. The results obtained by this method were confirmed by thin layer chromatography. Two of the sources (castor bean and dehulled oats) showed significant lipolytic activity at pH 5.6, castor beans containing 1.5 U/mg of extracted solid and oats 400-1200 U/mg of extracted solid. Castor beans are difficult to obtain and so may be an impractical commercial source of lipase; however, oats are abundant. If simple methods of enzyme purification and concentration can be developed, oats may prove to be a practical source of acid stable lipase for use in the treatment of patients with pancreatic insufficiency, especially those who have cystic fibrosis.

PMID: 7865271 [PubMed - indexed for MEDLINE] Clinical Studies - References 

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Lipoprotein lipase: structure, function, regulation, androle in disease.

Mead JR, Irvine SA, Ramji DP.

Cardiff School of Biosciences, Cardiff University, Museum Avenue, P.O. Box 911, Cardiff CF10 3US, Wales, UK.

Lipoprotein lipase (LPL) catalyses the hydrolysis of the triacylglycerol component of circulating chylomicrons and very low density lipoproteins, thereby providing non-esterified fatty acids and 2-monoacylglycerol for tissue utilisation. Research carried out over the past two decades have not only established a central role for LPL in the overall lipid metabolism and transport but have also identified additional, non-catalytic functions of the enzyme. Furthermore, abnormalities in LPL function have been found to be associated with a number of pathophysiological conditions, including atherosclerosis, chylomicronaemia, obesity, Alzheimer's disease, and dyslipidaemia associated with diabetes, insulin resistance, and infection. Advances have also been made in relating the various domains in the protein to different functions, and in understanding the mechanisms that are responsible for the changes in LPL expression seen in response to nutritional and other physiological changes, and during disease. This review summarises recent findings in relation to the structure, function, and regulation of LPL along with its important role in disease.

Publication Types:

  • Review
  • Review, Academic

PMID: 12483461 [PubMed - indexed for MEDLINE]

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Pancreatic enzyme replacement therapy.

Layer P, Keller J, Lankisch PG.

Department of Medicine, Israelitic Hospital, Orchideenstieg 14, D-22297 Hamburg, Germany. layer@ik-h.de

Malabsorption due to severe pancreatic exocrine insufficiency is one of the most important late features of chronic pancreatitis. Generally, steatorrhea is more severe and occurs several years prior to malabsorption of other nutrients because synthesis and secretion of lipase are impaired more rapidly, its intraluminal survival is shorter, and the lack of pancreatic lipase activity is not compensated for by nonpancreatic mechanisms. Patients suffer not only from nutritional deficiencies but also from increased nutrient delivery to distal intestinal sites, causing symptoms by profound alteration of upper gastrointestinal secretory and motor functions. Adequate nutrient absorption requires delivery of sufficient enzymatic activity into the duodenal lumen simultaneously with meal nutrients. The following recommendations are based on modern therapeutic concepts: 25,000 to 40,000 units of lipase per meal using pH-sensitive pancreatin microspheres, with dosage increases, compliance checks, and differential diagnosis in case of treatment failure. Still, in most patients, lipid digestion cannot be completely normalized by current standard therapy, and future developments are needed to optimize treatment. See: Betaine HCL

Kiwi Digestion Aid - Natural Supplement


















Publication Types:

  • Review
  • Review, Tutorial

PMID: 11276376 [PubMed - indexed for MEDLINE]

 


References

  1. Micromedex Healthcare Series. Englewood, CO: MICROMEDEX Inc.

  2. Malesci A. New enteric-coated high-lipase pancreatic extract in the treatment of pancreatic steatorrhea. J Clin Gastroenterol, 1994; 18(1):32-5.

  3. Tursi JM, Phair PG, Barnes GL. Plant sources of acid stable lipases: potential therapy for cystic fibrosis. J Paediatr Child Health, 1994; 30(6):539-43.

  4. Smyth RL, et al. Strictures of ascending colon in cystic fibrosis and high-strength pancreatic enzymes. Lancet 1994;343:85-6.

  5. Smyth RL, et al. Fibrosing colonopathy in cystic fibrosis: results of a case-control study. Lancet 1995;346:1247-51.

  6. Croft NM, Marshall TG, Ferguson A. Gut inflammation in children with cystic fibrosis on high-dose enzyme supplements. Lancet 1995;346:1265-267.

  7. Lloyd-Still JD. Cystic fibrosis and colonic strictures. A new "iatrogenic" disease. J Clin Gastroenterol, 1995; 21(1):2-5.

  8. Martindale W. Martindale the Extra Pharmacopoeia. Pharmaceutical Press, 1999.

  9. McKevoy GK, ed. AHFS Drug Information. Bethesda, MD: American Society of Health-System Pharmacists, 1998.