Mueller M S, Harnasch M, Kolb C, Kusch J, Sadowski T, Sedlacek R
University of Konstanz, Department of Immunology, Postfach M662, Konstanz, Germany.
Gene. 2000 Oct 3;256(1-2):101-11. doi: 10.1016/s0378-1119(00)00369-3.
We have isolated a murine cDNA orthologous to the human matrix metalloproteinase 19 (hMMP-19). The murine MMP-19 cDNA was amplified by RT-PCR using specific primers whose DNA sequences were derived from both murine MMP-19 genomic DNA and partial cDNA sequences. The murine MMP-19 (mMMP-19) is 79% identical to the human ortholog and encodes a protein of 527 amino acids with a deduced molecular mass of 59.1kDa. Analyzing the exon/intron junctions we revealed that the murine MMP-19 gene consists of nine exons and eight introns, and thus differs from the gene organization of other matrix metalloproteinases. Furthermore, a 587bp fragment of the mMMP-19 promoter containing a TATA box and an AP-1 binding motif was cloned, and 3.3kb transcripts of the MMP-19 gene were identified in liver, kidney, spleen, and colon. Finally, immunostaining of murine heart cryosections showed that mMMP-19, like its human counterpart, is expressed in the arterial tunica media of large blood vessels. By cloning mMMP-19 and unraveling its genomic structure, we have obtained valuable information for further study of the function of this MMP in vivo.
