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The very high rate of protein synthesis in acinar cells generates a constant low level of ER stress. Under normal conditions, this ER stress is readily compensated for by the UPR and EOR, which reduce the rate of protein synthesis while increasing production of molecules that facilitate cell recovery and repair.
The digestive processes are completed in the intestinal lumen, where large emulsions of fat globules are mixed with bile salts (BS) and pancreatic juice containing lipid digestive enzymes to form an aqueous suspension of small fatty droplets to maximize exposure to the pancreatic lipases for lipid hydrolysis.
Monoacylglycerol (MAG), diacylglycerol (DAG) and free FAs that are released by lipid hydrolysis join BS, CL, lysophosphatidic acid (LPA) and fat-soluble vitamins to form mixed micelles that provide a continuous source of digested dietary products for absorption at the brush-border membranes of the enterocytes.


Excessive acinar cell apoptosis can lead to necrosis, a severe systemic inflammatory response, acute respiratory distress, and life-threatening multiorgan failure. Altered Ca2+ release from the ER, and ROS, are thought to activate NF-κB, a key regulator of inflammatory gene expression.
They are then re-esterified sequentially inside the endoplasmic reticulum by MAG acyltransferase (MGAT) and diacylglycerol acyltransferase (DGAT) to form TAG. Dietary CL is acylated by acyl-CoA:cholesterol acyltransferase (ACAT) to cholesterol esters (CE).





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