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J Biol Chem, Vol. 275, Issue 4, 2554-2559, January 28, 2000

Identification of an Alternatively Spliced Seprase mRNA That Encodes a Novel Intracellular Isoform^*

Leslie A. Goldstein and Wen-Tien Chen

From the Department of Medicine, Division of Medical Oncology, State University of New York, Stony Brook, New York 11794-8160

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 proximal-central regions of the extracellular domain (Val⁵ through Ser⁴¹²) 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 Met⁵²² of seprase-l. The seprase-s open reading frame encodes a 239-amino acid polypeptide with an M_r ~ 27,000 that precisely overlaps the carboxyl-terminal catalytic region of seprase-l.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF007822.

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