A NOVEL POTENTIAL METALLOPEPTIDASE DERIVED FROM THE ENKEPHALINASE GENE BY ALTERNATIVE SPLICING

Abstract: Amplification of rat intestine mRNAs was performed by the reverse transcriptase‐polymerase chain reaction (RT‐PCR) using various oligonucleotide primers mainly corresponding to the translated region of the enkephalinase (EC 3.4.24.11, membrane metalloendopeptidase, MME 1) gene. In addition to the expected transcript, a shorter one was identified and its sequence indicated that it corresponds to an alternatively spliced mRNA from which exons 5–18 of MME I are deleted. It encodes a deduced 255 amino acid protein, MME II, instead of the 742 amino acid sequence of enkephalinase. The deduced structure of MME II is consistent with its being a membrane‐bound, zinc‐containing glycoprotein with a modified peptidase activity. MME II mRNA is also expressed, together with MME I mRNA, in brain and thyroid in a tissue‐specific manner. Copyright © 1990, Wiley Blackwell. All rights reserved