Milk lipid digestion in the neonatal dog: the combined actions of gastric and bile salt stimulated lipases

Iverson, Sara J.; Kirk, Charlotte L.; Hamosh, Margit; Newsome, Joseph T.

doi:10.1016/0005-2760(91)90131-z

Cited by 60 publications

(28 citation statements)

References 61 publications

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“…Puppies have lingual lipase that, together with gastric lipase, aids in the breakdown of milk lipids, making these available for use. During suckling (about four weeks after birth), milk is usually the sole nutrition source for puppies (Iverson et al, 1991). This may explain the higher ether extract digestibility detected in puppies as compared to adults in the present study.…”

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confidence: 63%

“…As animal's age, the intestinal microbiota and morphology, as well as the production of digestive enzymes and hormones are modified, influencing digestibility (Fahey et al, 2008). According to Meyer et al (1940), amylase, trypsin, and lipase activities in the duodenal juice are reduced with age. However, Gilham et al (1993), in a study with Labrador Retriever puppies with twelve or twenty weeks of age, did not find any statistically significant influence of age on nutrient digestibility.…”

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confidence: 99%

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Digestibility of dry extruded food in adult dogs and puppies

Zanatta

Félix

Brito

et al. 2011

Arq. Bras. Med. Vet. Zootec.

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confidence: 63%

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confidence: 99%

Digestibility of dry extruded food in adult dogs and puppies

Zanatta

Félix

Brito

et al. 2011

Arq. Bras. Med. Vet. Zootec.

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“…However, the actual absorption and utilization of these fatty acids by the neonate depends upon initial hydrolysis. The importance of initial gastric digestion of dietary lipid by lingual and/or gastric lipases, especially in the ned hate, has become increasingly evident (47). However, most information on hydrolysis has been limited to artificial homogeneous TG containing fatty acids of chain-length and degree of unsaturation of 18:1 or lower.…”

Section: Discussionmentioning

confidence: 99%

Positional specificity of gastric hydrolysis of long‐chain n−3 polyunsaturated fatty acids of seal milk triglycerides

Iverson

Sampugna

Oftedal

1992

Lipids

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Long-chain n-3 polyunsaturated fatty acids (n-3 PUFA) of marine oils are important dietary components for both infants and adults, and are incorporated into mlUo~ following maternal dietary intake. However, little is known about the hydrolysis of these PUFA from milk triglycerides (TG) by lipases in suckling young. Seals, like human~, possess gastric lipase; however, the milk lipids of seals and sea lions are almost devoid of the readily hydrolyzable medium,chain fatty acids, and are characterized by a large percentage (10-30%) of n-3 PUFA. Gastric hydrolysis of milk lipids was studied in vivo in suckling pups of three species (the California sea lion, the harp seal and the hooded seal) in order to elucidate the actions and specifit~ ity of gastric lipases on milk TG in relation to fatty acid composition and TG structure. Regardless of milk fat content (31-61% fat) or extent of gastric hydrolysis (10-56%), the same fatty acids were preferentially released in all three species, as determined by their relative enrichment in the free fatty acid (FFA) fraction. In addition to 16:1 and 18:0, these were the PUFA of 18 carbons and longer, except for 22:6n-3. Levels of 20:5n-3 were most notably enriched in FFA, at up to five times that found in the TG. Although 22:6n-3 was apparently also released from the TG (reduced in the diglyceride), it was also notably re~ duced in FFA. Positional analysis of milk TG based on the products of Grignard hydrolysis revealed that these PUFA, including 22:6n-3, were preferentially esterified at the a-position of the TG, and that the fatty acids not released during gastric hydrolysis were located at the sn-2 position. The extreme reduction of 22:6n~ and enrichment of 20:5n-3 in FFA is discussed. Results from this study are consistent with reports that gastric lipase acts stere~ specifically to release fatty acids at the a-positions (sn-3, sn-1). We conclude that the n-3 PUFA in milk are efficiently hydrolyzed by gastric lipase and that this has important implications for digestion of milks enriched in PUFA by neonates in general. Lipids 27, 870-878 (1992).Long-chain n-3 polyunsaturated fatty acids (n-3 PUFA), characteristic of marine otis, have become a major focus of research due to their potent

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“…Lipid digestion begins in the stomach where the action of preduodenal lipase hydrolyzes up to 30% of ingested triglycerides into diglycerides and free fatty acids before delivery to the duodenum (51,52). In the duodenum, partially digested lipid mixes with pancreatic and biliary secretions, which are essential to its further digestion and absorption.…”

Section: Overviewmentioning

confidence: 99%

Carboxyl ester lipase

Hui

Howles

2002

Journal of Lipid Research

193

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Carboxyl ester lipase (CEL), previously named cholesterol esterase or bile salt-stimulated (or dependent) lipase, is a lipolytic enzyme capable of hydrolyzing cholesteryl esters, tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide. The active site catalytic triad of serine-histidine-aspartate is centrally located within the enzyme structure and is partially covered by a surface loop. The carboxyl terminus of the protein regulates enzymatic activity by forming hydrogen bonds with the surface loop to partially shield the active site. Bile salt binding to the loop domain frees the active site for accessibility by water-insoluble substrates. CEL is synthesized primarily in the pancreas and lactating mammary gland, but the enzyme is also expressed in liver, macrophages, and in the vessel wall. In the gastrointestinal tract, CEL serves as a compensatory protein to other lipolytic enzymes for complete digestion and absorption of lipid nutrients. Importantly, CEL also participates in chylomicron assembly and secretion, in a mechanism mediated through its ceramide hydrolytic activity. Cell culture studies suggest a role for CEL in lipoprotein metabolism and oxidized LDL-induced atherosclerosis. Thus, this enzyme, which has a wide substrate reactivity and diffuse anatomic distribution, may have multiple functions in lipid and lipoprotein metabolism, and atherosclerosis. Carboxyl ester lipase (CEL), previously named pancreatic cholesterol esterase and also known as bile salt-stimulated (or -dependent) lipase, is a nonspecific lipolytic enzyme capable of hydrolyzing cholesteryl esters, tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide (1-3). The hydrolysis of water-insoluble carboxyl esters with long chain fatty acyl groups by CEL requires its activation by bile salt. However, CEL hydrolysis of water-soluble substrates such as carboxyl esters with short chain fatty acids or lysophospholipids does not have an absolute dependence on bile salt activation. The CEL protein is synthesized primarily in the pancreatic acinar cells and lactating mammary glands of higher mammals. Small amounts of CEL are found in other tissues, particularly the liver, macrophages, endothelial cells, and eosinophils (4-10). Extensive research has been performed in recent years on the structure-function relationship of this protein as well as its physiological role in lipid metabolism. A significant body of work has also been devoted to studying CEL processing and transport in pancreatic acinar cells. The latter topic was reviewed recently (11) and will be discussed only briefly in this article when appropriate. This article will present an updated review on the structure-function studies of CEL as well as an in-depth discussion on the current understanding of its role in lipid metabolism. PROTEIN STRUCTURE-FUNCTION RELATIONSHIP Active siteThe nucleotide sequence of CEL from various species shows that it is a highly conserved protein belonging to the ␣ / ␤ hydrolase family. The carb...

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Milk lipid digestion in the neonatal dog: the combined actions of gastric and bile salt stimulated lipases

Cited by 60 publications

References 61 publications

Digestibility of dry extruded food in adult dogs and puppies

Digestibility of dry extruded food in adult dogs and puppies

Positional specificity of gastric hydrolysis of long‐chain n−3 polyunsaturated fatty acids of seal milk triglycerides

Carboxyl ester lipase

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