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| 1 | Visceral hypersensitivity in inflammatory bowel diseases and irritable bowel syndrome: The role of proteases显示文摘Proteases, enzymes catalyzing the hydrolysis of peptide bonds, are present at high concentrations in the gastrointestinal tract. Besides their well-known role in the digestive process, they also function as signaling molecules through the activation of protease-activated receptors(PARs). Based on their chemical mechanism for catalysis, proteases can be classified into several classes: serine, cysteine, aspartic, metallo- and threonine proteases represent the mammalian protease families. In particular, the class of serine proteases will play a significant role in this review. In the last decades, proteases have been suggested to play a key role in the pathogenesis of visceral hypersensitivity, which is a major factor contributing to abdominal pain in patients with inflammatory bowel diseases and/or irritable bowel syndrome. So far, only a few preclinical animal studies have investigated the effect of protease inhibitors specifically on visceral sensitivity while their effect on inflammation is described in more detail. In our accompanying review we describe their effect on gastrointestinal permeability. On account of their promising results in the field of visceral hypersensitivity, further research is warranted. The aim of this review is to give an overview on the concept of visceral hypersensitivity as well as on the physiological and pathophysiological functions of proteases herein. | Hannah Ceuleers Hanne Van Spaendonk Nikita Hanning Jelena Heirbaut Anne-Marie Lambeir Jurgen Joossens Koen Augustyns Joris G De Man Ingrid De Meester Benedicte Y De Winter | 2016 | World Journal of Gastroenterology2016，22，47： | 7 |
| 2 | Regulation of intestinal permeability: The role of proteases显示文摘The gastrointestinal barrier is-with approximately 400 m^2-the human body's largest surface separating the external environment from the internal milieu. This barrier serves a dual function: permitting the absorption of nutrients, water and electrolytes on the one hand, while limiting host contact with noxious luminal antigens on the other hand. To maintain this selective barrier, junction protein complexes seal the intercellular space between adjacent epithelial cells and regulate the paracellular transport. Increased intestinal permeability is associated with and suggested as a player in the pathophysiology of various gastrointestinal and extraintestinal diseases such as inflammatory bowel disease, celiac disease and type 1 diabetes. The gastrointestinal tract is exposed to high levels of endogenous and exogenous proteases, both in the lumen and in the mucosa. There is increasing evidence to suggest that a dysregulation of the protease/antiprotease balance in the gut contributes to epithelial damage and increased permeability. Excessive proteolysis leads to direct cleavage of intercellular junction proteins, or to opening of the junction proteins via activation of protease activated receptors. In addition, proteases regulate the activity and availability of cytokines and growth factors, which are also known modulators of intestinal permeability. This review aims at outlining the mechanisms by which proteases alter the intestinal permeability. More knowledge on the role of proteases in mucosal homeostasis and gastrointestinal barrier function will definitely contribute to the identification of new therapeutic targets for permeability-related diseases. | Hanne Van Spaendonk Hannah Ceuleers Leonie Witters Eveline Patteet Jurgen Joossens Koen Augustyns Anne-Marie Lambeir Ingrid De Meester Joris G De Man Benedicte Y De Winter | 2017 | World Journal of Gastroenterology2017，23，12： | 6 |
| 3 | Dipeptidyl- peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV显示文摘 | Lambeir A M Durinx C Scharpe' S | 2003 | Crit Rev Clin Lab Sci2003，40，3： | 1 |
| 4 | Dipeptidyl-peptidase ivfrom bench to bedside:An update on structural properties,func-tions,and clinical aspects of the enzyme dpp iv显示文摘 | Lambeir A M Durinx C Scharpe S | 2003 | Crit Rev ClinLab Sci2003，40，3： | 1 |
| 5 | Suggested functions for prolyl oligopeptidase:a puzzling paradox 显示文摘 | Brandt I Scharpe S Lambeir AM | 2007 | Clin Chim Acta2007，377，12： | 1 |
| 6 | Dipeptidyl- peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV 显示文摘 | LAMBEIR A DURINX C DE MEESTER I | 2003 | Crit Rev Clin Lab Sci2003，40，3： | 1 |
| 7 | Dipeptidyl-peptidase IVconverts intact B-type natriuretic peptide into its des-SerPro form显示文摘 | Brandt I Lambeir AM Ketelslegers JM | 2006 | Clin Chem2006，52，1： | 1 |
| 8 | Dipeptidyl-peptidase IV from bench to bedside:an update on structural properties,functions,and clinical aspects of the enzyme DPP IV显示文摘 | Lambeir AM Durinx C Scharpe S | 2003 | Crit Rev Clin Lab Sci2003，40，3： | 1 |
| 9 | ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain显示文摘 | Sercu S Lambeir A M Steenackers E | 2009 | Matrix Biol2009，28，： | 1 |
| 10 | Pyrrolidides :synthesis and sa'ucture-activity relationship as inhibitors of dipeptidyl peptidase 1V 显示文摘 | AUGUSTYNS K J L LAMBEIR A M BORLOO M | 1997 | Eur J Med Chem1997，32，4： | 1 |
| 11 | The catalytic cycle of biosynthetic thiolase , a conformational journey of an acetyl group through four binding modes and two oxyanion holes显示文摘 | Kursula P Ojala J Lambeir AM | 2002 | Biochemistry2002，41，15： | 1 |
| 12 | Dipeptidyl-peptidase IV converts intact B-type natriuretic peptide into its des-SerPro form显示文摘 | Brandt I Lambeir AM Ketelslegers JM | 2006 | Clin Chem2006，82，： | 1 |
| 13 | Dipeptidyl-peptidase IV converts intact B-type natriuretic peptide into its des-SerPro form显示文摘 | Brandt I Lambeir A M Ketelslegers J M | 2006 | Clin Chem2006，52，： | 1 |
| 14 | Dipeptidyl?peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV 显示文摘 | Lambeir AM Durinx C Scharpe S | 2003 | CritRev Clin lab Sci2003，40，3： | 1 |
| 15 | Dipeptidyl-peptidase Ⅳ converts intact B-type natriuretic peptide into its des-SerPro form显示文摘 | Brandt I Lambeir AM Ketelslegers JM | | 0，，： | 1 |
| 16 | Dipcptidyl-pcptidase,functions,and clinical aspects of the enzyme DPP-Ⅳ显示文摘 | Lambeir A M Durinx C Scharpe S | 2003 | Crit Rev Clin Lab Sci2003，40，3： | 1 |
| 17 | Dipeptidyl peptidase Ⅳ from bench to bedside: An update on structural properties, functions, and clinical aspects of the enzyme DPP Ⅳ 显示文摘 | LAMBEIR AM DURINXC C SCHARPE S | 2003 | Crit Rev Clin Lab Sci2003，40，3： | 1 |
| 18 | Dipeptidylpeptidase IV from bench to bedside:an update on structural properties,functions,and clinical aspects of the enzyme DPP IV显示文摘 | Lambeir A M Durinx C Scharpe S | 2003 | Critical Reviews in Clinical Laboratory Sciences2003，40，3： | 1 |
| 19 | Wild- type and mutant D-xylose isomerase from Actinoplanes missouriensis : metal-ion dissociation constants, kinetic parameters of deuterated and non-deuterated substrates and solvent-isotope effects 显示文摘 | van Bastelaere PB Kersters-Hilderson HL Lambeir AM | 1995 | Biochem J1995，307，1： | 1 |
| 20 | Dipeptidyl-peptidase IV from bench to bedside:an update on structuarl properties,functions,and clinical aspects of the enzyme DPP IV显示文摘 | Lambeir AM Durinx C Scharpe S | 2003 | Cirt Rev Clin Lab Sci2003，40，3： | 1 |
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