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Molecular cloning, chromosomal location, and tissue-specific expression of
the murine cathepsin G gene
JW Heusel, EM Scarpati, NA Jenkins, DJ Gilbert, NG Copeland, SD Shapiro and TJ Ley
Department of Medicine, Jewish Hospital at Washington University Medical
Center, St Louis, MO 63110.
We previously have characterized a cluster of genes encoding cathepsin G
(CG) and two other CG-like hematopoietic serine proteases, CGL-1 and CGL-2,
on human chromosome 14. In this report, we clone and characterize a novel,
related murine hematopoietic serine protease gene using human CG (hCG) cDNA
as the probe. This murine gene spans approximately 2.5 kb of genomic DNA,
is organized into five exons and four introns, and bears a high degree of
homology to hCG at both nucleic acid (73%) and deduced amino acid (66%)
levels. The predicted cDNA contains an open reading frame of 783
nucleotides that encodes a nascent protein of 261 amino acids. Processing
of a putative signal (pre) peptide of 18 residues and an activation (pro)
dipeptide would generate a mature enzyme of approximately 27 Kd that has an
estimated pI of 12.0. Conserved residues at His44, Asp88, and Ser181 form
the characteristic catalytic triad of the serine protease superfamily. The
gene is tightly linked to the CTLA-1 locus on murine chromosome 14, where
the serine protease genes mCCP1-4 are clustered. Expression of this gene is
detected only in the bone marrow and is restricted to a small population of
early myeloid cells. These findings are consistent with the identification
of the gene encoding murine CG.
Volume 81,
Issue 6,
pp. 1614-1623,
03/15/1993
Copyright © 1993 by The American Society of Hematology
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