A unique secretory behavior for GP2 in the exocrine pancreas

GP2 is the major glycoprotein component of the zymogen granule membrane of pancreas acinar cell. It was recently found that this protein is secreted and forms a network of fibrils in pancreatic juice. In the present work, with an ELISA, we have examined the fluctuations of GP2 levels in the juice collected in resting and stimulated conditions. In anaesthetized fasting rats, GP2 represented about 6-8% of total protein output. Stimulation by caerulein, carbachol, or their combination caused an immediate and significant burst in both protein and GP2 outputs. However, the GP2 increase did not parallel protein release. Its relative proportions decreased with the intensity of the stimulus. The secretory behavior of GP2 cannot be explained with the current concepts of constitutive and regulated pathways of secretion and suggests the existence of a yet undefined mode of secretion for this protein.