Expression, production, and characterization of full-length vitronectin in Escherichia coli.

Vitronectin (VN) is one of the primary adhesive proteins in serum and serves to promote the attachment and spreading of a wide variety of cell types to tissue culture plastic. In this study, the pGEX2t expression vector was used to express full-length human VN as a GST-tagged fusion protein in Escherichia coli. GST/VN production was induced with IPTG and the protein was found to localize to inclusion bodies.

Fibronectin matrix polymerization regulates small airway epithelial cell migration.

The continuous conversion of soluble fibronectin into extracellular matrix fibrils occurs through a dynamic, cell-dependent process. As the extracellular matrix is assembled, changes in the conformation of matrix proteins may expose biologically active, matricryptic sites that alter cell behavior. In this study, an in vitro model of wound healing was used to determine the role of matrix fibronectin in airway epithelial cell motility.

Evidence on the presence of secretin cells in the gastric antral and oxyntic mucosa.

Secretin is released from upper small intestinal mucosa to drive pancreatic secretion of fluid and bicarbonate and inhibit gastric acid secretion. Recently, we found that, in isolated, vascularly perfused rat stomach model, the inhibition of acid secretion by pituitary adenylate cyclase activating polypeptide (PACAP) was mediated in part via local release of secretin. However, the presence of secretin-producing cells and mRNA in gastric mucosa, particularly in oxyntic mucosa, has not been established.