Identification of an alternatively spliced seprase mRNA that encodes a novel intracellular isoform
Identification of an alternatively spliced seprase mRNA that encodes a novel intracellular isoform
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DOI：
10.1074/jbc.275.4.2554
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发表时间：
2000-01-28
影响因子：
4.8
通讯作者：
Chen, WT
中科院分区：
文献类型：
--
作者：
Goldstein, LA;Chen, WT
Seprase is a homodimeric 170-kDa integral membrane gelatinase that is related to the ectoenzyme dipeptidyl peptidase IV. We have identified an alternatively spliced seprase messenger from the human melanoma cell line LOX that encodes a novel truncated isoform, seprase-s. The splice variant mRNA is generated by an out-of-frame deletion of a 1223-base pair exonic region that encodes part of the cytoplasmic tail, transmembrane, and the membrane progimal-central regions of the extracellular domain (Val(5) through Ser(412)) of the seprase 97-kDa subunit (seprase-l). The seprase-s mRNA has an elongated 5' leader (548 nucleotides) that harbors at least two upstream open reading frames that inhibit seprase-s expression from a downstream major open reading frame. Deletion mutagenesis of the wild type splice variant cDNA confirms that initiation of the seprase-s coding sequence begins with an ATG codon that corresponds to Met(522) Of seprase-l, The seprase-s open reading frame encodes a 239-amino acid polypeptide with an M-r similar to 27,000 that precisely overlaps the carboxyl-terminal catalytic region of seprase-l.
