Secretion of acetylcholinesterase by a mouse hepatocyte X rat liver cell hybrid culture

Summary A hybrid cell line (E-2) that secretes the enzyme acetylcholinesterase (AChE) has been prepared. The E-2 cell was the product of a fusion between primary mouse hepatocytes and a chemically transformed rat liver cell line (FRL), neither of which expresses AChE activity. The enzyme was determined to be AChE on the basis of its susceptibility to inhibition by BW284c51 but not by iso-OMPA, as well as its substrate specificity. Although the secreted enzyme was salt soluble and its activity not modified by the addition of the nonionic detergent, Triton X-100, the activity of the cellular enzyme (derived from homogenates of E-2 cells) was greatly enhanced in the presence of the detergent. This work was supported by funds from the Chemical Research and Development Center, Aberdeen Proving Ground, MD. The opinions and assertions are the private ones of the authors and are not to be construed as official. These experiments were conducted according to the principles set forth in the “Guide for the Care and Use of Experimental Animals,” DHEW Publ. No. (NIH) 78-23.