Acute pancreatitis is the most frequent disease of the pancreas. The spectrum of acute pancreatitis can range from mild edematous to severe necrotizing. One of the most interesting hypotheses for the pathogeny of the disease is that autodigestion of the gland occurs when hydrolytic enzymes (e.g.: trypsinogen, chymotrypsinogen, proelastase, and prophospholipase A) are unduly activated within the pancreas rather than into the intestinal lumen. The active enzymes then digest cellular membranes and lead to edema, interstitial hemorrhage, vascular damage, coagulation necrosis, fat necrosis, and parenchymal cell necrosis.

Living organisms respond at the cellular level to stress or pathological aggression by altering the normal pattern of protein synthesis. That change is characterized by a dramatic induction of stress proteins with concomitant inhibition of the normal array of cellular proteins. Stress proteins are not novel components of the stressed cells since most of them are expressed to some level in cells grown under normal conditions.

The aim of our research is to characterize at the molecular level the pancreatic emergency program set up in response to pancreatitis. We developed a strategy in which the phenotype of the pancreas with acute pancreatitis was established by characterization of a large number of its transcripts. Such a cDNA collection represents a reservoir from which transcripts involved in the emergency response can be identified on the basis of their expression patterns. In this report, we describe a novel membrane protein, named VMP1, that is strongly and rapidly induced in pancreas during acute pancreatitis.