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J. Biol. Chem., Vol. 276, Issue 20, 17474-17478, May 18, 2001
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From the 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.
Molecular Cloning and Characterization of a Novel
Mammalian Endo-apyrase (LALP1)*
§,
,
§,
,
,
,
,
**
Department of Pathology, Immunology and
Laboratory Medicine, Center for Mammalian Genetics and Diabetes Center
of Excellence, College of Medicine, and ¶ Department of Medicinal
Chemistry, College of Pharmacy and The McKnight Brain Institute,
University of Florida, Gainesville, Florida 32610
*
This research was supported in part by National Institutes
of Health Grants 1R01DK53266-01 (to J.-X. S) and AG015688 (to
D. H. W).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a University of Florida Alumni Fellowship.
**
To whom correspondence should be addressed: Dept. of Pathology,
Immunology and Laboratory Medicine, Box 100275, University of Florida,
Gainesville, FL 32610. Tel.: 352-392-0677; Fax: 352-392-3053; E-mail:
she@ufl.edu.
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