A novel potential metallopeptidase derived from the enkephalinase gene by alternative splicing.
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 I) 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.
Llorens-Cortes
C
C
Unité de Neurobiologie et Pharmacologie, Centre Paul Broca de l'INSERM, Paris, France.
Giros
B
B
Schwartz
J C
JC
D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004274:DNA, Recombinant; D005796:Genes; D008297:Male; D008666:Metalloendopeptidases / Q000235:genetics*; D008969:Molecular Sequence Data; D015260:Neprilysin / Q000235:genetics*; D016133:Polymerase Chain Reaction; D012326:RNA Splicing; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D004274:DNA, Recombinant; D012333:RNA, Messenger; D008666:Metalloendopeptidases; D015260:Neprilysin