TAILIEUCHUNG - Báo cáo Y học: Proteolytic action of duodenase is required to induce DNA synthesis in pulmonary artery fibroblasts A role for phosphoinositide 3-kinase

Duodenase is a 29-kDa serine endopeptidase that displays selective trypsin- and chymotrypsin-like substrate specificity. This enzyme has been localized to epitheliocytes of Brunner’s glands, and as described here, to mast cells within the intestinal mucosa and lungworm-infected lung, implying an important additional role in inflammation and tissue remodelling. In primary cultures of pulmonary artery fibroblasts, duodenase induced a concentration-dependent increase in [3H]thymidine incorporation with a maximal effect observed at 30 nM. Pretreating duodenase with soybean trypsin inhibitor abolished DNA synthesis, confirming that proteolytic activity was an essential requirement for this response. . | Eur. J. Biochem. 269 1171-1180 2002 FEBS 2002 Proteolytic action of duodenase is required to induce DNA synthesis in pulmonary artery fibroblasts A role for phosphoinositide 3-kinase Alan D. Pemberton1 Tatyana S. Zamolodchikova2 Cheryl L. Scudamore3 Edwin R. Chilvers4 Hugh R. P. Miller1 and Trevor R. Walker5 1 Department of Veterinary Studies University of Edinburgh Easter Bush Veterinary Centre Roslin Edinburgh UK Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences Moscow Russia 3 Department of Veterinary Pathology University of Edinburgh Easter Bush Veterinary Centre Roslin Edinburgh UK 4Respiratory Medicine Unit Department of Medicine University of Cambridge School of Clinical Medicine Addenbrooke s and Papworth Hospitals Cambridge UK 5Rayne Laboratory Respiratory Medicine Unit University of Edinburgh Medical School Edinburgh UK Duodenase is a 29-kDa serine endopeptidase that displays selective trypsin- and chymotrypsin-like substrate specificity. This enzyme has been localized to epitheliocytes of Brunner s glands and as described here to mast cells within the intestinal mucosa and lungworm-infected lung implying an important additional role in inflammation and tissue remodelling. In primary cultures of pulmonary artery fibroblasts duodenase induced a concentration-dependent increase in 3H thymidine incorporation with a maximal effect observed at 30 nM. Pretreating duodenase with soybean trypsin inhibitor abolished DNA synthesis confirming that proteolytic activity was an essential requirement for this response. PAR1 PAR2 and PAR4 activating peptides were unable to induce 3H thymidine incorporation in pulmonary artery fibroblasts. Likewise pretreatment of fibroblasts with TNFa known to up-regulate PAR2 expression in other systems and IL-1P did not enhance the potential of duodenase to induce DNA synthesis. Furthermore duo-denase increased GTPyS binding to fibroblast membranes indicating that a G-protein-coupled receptor may .

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