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Molecular cloning and characterization of a novel mammalian endo-apyrase (LALP1).

The Journal of biological chemistry (2001-03-30)
J D Shi, T Kukar, C Y Wang, Q Z Li, P E Cruz, A Davoodi-Semiromi, P Yang, Y Gu, W Lian, D H Wu, J X She
RÉSUMÉ

Here we describe the cloning, localization, and characterization of a novel mammalian endo-apyrase (LALP1) in human and mouse. The predicted human LALP1 gene encodes a 604-amino acid protein, whereas the mouse Lalp1 gene encodes a 606-amino acid protein. The human and mouse genes have 88% amino acid sequence identity. These genes share considerable homologies with hLALP70, a recently discovered mammalian lysosomal endo-apyrase. The human LALP1 gene resides on chromosome 10q23-q24 and contains 12 exons and 11 introns covering a genomic region of approximately 46 kilobase pairs. The subcellular localization and enzymatic activity of LALP1 indicated that LALP1 is indeed an endo-apyrase with substrate preference for nucleoside triphosphates UTP, GTP, and CTP.