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Molecular Cloning and Characterization of a Novel Mammalian Endo-apyrase (LALP1)

  • Jing Da Shi
  • , Thomas Kukar
  • , Cong Yi Wang
  • , Quan Zhen Li
  • , Pedro E. Cruz
  • , Abdoreza Davoodi-Semiromi
  • , Ping Yang
  • , Yunrong Gu
  • , Wei Lian
  • , Donghai H. Wu
  • , Jin Xiong She*
  • *Corresponding author for this work
  • University of Florida
  • Dept. of Pathol., Immunol./Lab. Med.

Research output: Contribution to journalArticlepeer-review

Abstract

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 ∼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.

Original languageEnglish
Pages (from-to)17474-17478
Number of pages5
JournalJournal of Biological Chemistry
Volume276
Issue number20
DOIs
Publication statusPublished - 18 May 2001
Externally publishedYes

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