Research on the function of a single transmembrane metalloprotease of mouse ADAM33

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A disintegrin and metalloprotease (ADAM) family of the single transmembrane proteins has a unique domain structure, containing metalloprotease, disintegrin and EGF-like domains. 34 ADAMs have been identified to date. 17 ADAMs contain the unique amino acid sequence (HE-X-H-XX-G-XX-HD) in their metalloprotease domain required for enzymatic activity. We isolated novel mouse ADAM33 gene from the cDNA library in mouse brain, which is highly resembled the Xenopus ADAM13, suggesting play a role of the formation of early neural crest and neural tube. We investigated their nucleotide and amino acid sequence. The mouse ADAM33 amino acid sequence showed 42%. homology with Xenopus ADAM13, but both proteins were conserved their functional domains in protein structures. We also isolated the human ADAM33 gene, and this amino acid sequence showed the highest homology with mouse ADAM33 (70%).To clarify the function of mouse ADAM33, we generated transgenic mice using the DNA fragment containing chloramphenicol acetyltransferase (CAT) gene inserted between exogenous promoter and mouse ADAM33 gene. And then constructed DNA was microinjected into fertilized eggs. The transcriptional effects of this introduction in generated transgenic mice were analyzed with ELISA method, no obvious highly transcriptional mice were obtained. We resume generating the transgenic mice with alterative gene-structure, mouse ADAM33 gene was directly connected with their promoter.