Background. The pancreatic regenerating (reg) gene is an acinar cell product involved in islet formation and maintenance. Human reg protein is mitogenic to pancreatic beta and ductular cells, and its amino acid sequence predicts it to be a calcium-dependent lectin. Methods. We studied the biologic activity and cellular localization of rat reg I isolated from the acinar cell line AR42J and the lectin properties of reg from AR42J and pancreatic juice. Bioactivity was assayed by milogenesis on the ductular cell line ARIP. Cellular localization was determined by differential centrifugation. Lectin properties were assessed by affinity chromatography. Results. Reg protein from crude AR42J cellular lysate and purified reg protein from AR42J induced thymidine incorporation to ARIP Conditioned medium from AR42J and co-culture of AR42J with morphologically distinguishable ARIP, however, failed to induce mitogenesis. Reg protein was localized within the vesicle fraction of the cell and was not membrane bound. Affinity chromotography revealed that reg protein did not bind to mannose or galactose in the presence or absence of calcium. In pancreatic juice a previously undescribed mannose-binding protein was discovered at 25,000 to 30,000 daltons. Conclusions. We conclude that reg produced in the acinar cell line AR42J is biologically active but not efficiently secreted, even though it localized within the cellular vesicles. Despite predictions based on its amino acid sequence, it does not appear to be a calcium-dependent lectin.
ASJC Scopus subject areas