Gastric lipase: an extremophilic interfacial enzyme with medical applications

Aloulou, Ahmed; Carrière, Frédéric

doi:10.1007/s00018-008-7546-z

Cited by 47 publications

(30 citation statements)

References 22 publications

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“…It has been demonstrated that gastric lipase is activated in the acid medium of the stomach, and it remains active at pH 2 until pancreatic bicarbonate is secreted [29]. Optimal functioning of gastric lipase is an essential step for lipolysis and the resulting products from gastric lipase (such as monoglycerides, diglycerides and fatty acids) [20] stimulate CCK release and pancreatic lipase-colipase activation [30].…”

Section: Discussionmentioning

confidence: 99%

A sodium-bicarbonated mineral water reduces gallbladder emptying and postprandial lipaemia: A randomised four-way crossover study

et al. 2011

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Section: Discussionmentioning

confidence: 99%

A sodium-bicarbonated mineral water reduces gallbladder emptying and postprandial lipaemia: A randomised four-way crossover study

et al. 2011

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“…In addition to the gel-forming mucins MUC5AC and MUC6 as well as a variety of ions (e.g., H (73), cathelicidin LL-37/hCAP18 (74), lysozyme (19), and the extremophilic gastric lipase (75), which binds optimally to lipid-water interphases at low pH. On top, the luminal surface of the gastric mucus seems to be coated with a hydrophobic film of surfactant phospholipids (1,76,77).…”

Section: Tff2 a Muc6-binding Lectin Stabilizing The Gastric Mucus Bamentioning

confidence: 99%

TFF2, a MUC6-binding lectin stabilizing the gastric mucus barrier and more (Review)

Hoffmann

2015

International Journal of Oncology

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Abstract. The peptide TFF2 (formerly 'spasmolytic polypeptide'), a member of the trefoil factor family (TFF) containing two TFF domains, is mainly expressed together with the mucin MUC6 in the gastric epithelium and duodenal Brunner's glands. Pathologically, TFF2 expression is observed ectopically during stone diseases, chronic inflammatory conditions and in several metaplastic and neoplastic epithelia; most prominent being the 'spasmolytic polypeptide-expressing metaplasia' (SPEM), which is an established gastric precancerous lesion. TFF2 plays a critical role in maintaining gastric mucosal integrity and appears to restrain tumorigenesis in the stomach. Recently, porcine TFF2 has been shown to interact with the gastric mucin MUC6 and thus stabilize the gastric mucus barrier. On the one hand, TFF2 binds to MUC6 via non-covalent lectin interactions with the glycotope GlcNAcα1→4Galβ1→R. On the other hand, TFF2 is probably also covalently bound to MUC6 via disulfide bridges. Thus, implications for the complex multimeric assembly, cross-linking, and packaging of MUC6 as well as the rheology of gastric mucus are discussed in detail in this review. Furthermore, TFF2 is also expressed in minor amounts in the immune and nervous systems. Thus, similar to galectins, its lectin activity would perfectly enable TFF2 to form multivalent complexes and cross-linked lattices with a plethora of transmembrane glycoproteins and thus modulate different signal transduction processes. This could explain the multiple and diverse biological effects of TFF2 [e.g., motogenic, (anti)apoptotic, and angiogenic effects]. Finally, a function during fertilization is also possible for TFF domains because they occur as shuffled modules in certain zona pellucida proteins.

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“…To catalyze such interfacial reaction, lipases undergoe a conformational change consisting in the opening of an amphiphilic lid that gives access to the active site while it generates a large hydrophobic surface surrounding the catalytic cleft and part of the interfacial recognition site (IRS) [3][4][5][6]. HGL has been called "extremophilic" as it is stable and active in the acid environment of the stomach, it is resistant to pepsin hydrolysis and it is not inhibited by the bile salts present in the gastro-intestinal tract [7]. Its optimum activity at acidic pH (4-5.4) on natural long chain TG emulsions [8] is unique among lipases and is explained by a better adsorption at the lipid/water interface at low pH [9,10] while, above neutral pH, [11] the enzyme remains in the water phase and is poorly stable [12].…”

Section: Introductionmentioning

confidence: 99%

Adsorption of gastric lipase onto multicomponent model lipid monolayers with phase separation

Bourlieu-Lacanal

Pabœuf

Chever

et al. 2016

Colloids and Surfaces B: Biointerfaces

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. (ellipsometry, tensiometry and atomic force microscopy), it was evidenced that rDGL partitions toward liquid expanded phase and at phase boundaries. rDGL gets adsorbed at several levels of insertion suggesting molecular cooperation that may favor insertion and strongly impacts on the lipid phase lateral organization. The addition of phosphatidylserine, negatively charged, reinforced adsorption; hence besides hydrophobic interactions and as further investigated through surface potential modeling, rDGL adsorption is favored by electrostatic interactions.

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Gastric lipase: an extremophilic interfacial enzyme with medical applications

Cited by 47 publications

References 22 publications

A sodium-bicarbonated mineral water reduces gallbladder emptying and postprandial lipaemia: A randomised four-way crossover study

A sodium-bicarbonated mineral water reduces gallbladder emptying and postprandial lipaemia: A randomised four-way crossover study

TFF2, a MUC6-binding lectin stabilizing the gastric mucus barrier and more (Review)

Adsorption of gastric lipase onto multicomponent model lipid monolayers with phase separation

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