Journal of Leukocyte Biology
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(Journal of Leukocyte Biology. 2002;72:478-485.)
© 2002 by Society for Leukocyte Biology

Molecular characterization and expression analysis of leucine-rich {alpha}2-glycoprotein, a novel marker of granulocytic differentiation

Lynn C. O’Donnell, Lawrence J. Druhan and Belinda R. Avalos

Bone Marrow Transplant Program, The Arthur G. James Cancer Hospital and Richard J. Solove Research Institute, The Ohio State University College of Medicine and Public Health, Columbus

Correspondence: Dr. Belinda R. Avalos, The Ohio State University, Bone Marrow Transplant Program, A437A Starling-Loving Hall, 320 West Tenth Avenue, Columbus, OH 43210. E-mail: avalos-1{at}medctr.osu.edu

Using data obtained from cDNA representational difference analysis to identify genes induced during neutrophilic differentiation of the 32D clone 3G (32Dcl3G) cells, we isolated cDNA clones for murine and human leucine-rich {alpha}2-glycoprotein (hLRG), a protein with unknown function purified 25 years ago. Expression of LRG during differentiation of 32Dcl3G cells preceded the expression of lactoferrin and gelatinase but followed myeloperoxidase. LRG transcripts were also detected in human neutrophils and progenitor cells but not in peripheral blood mononuclear cells. Notably, LRG expression was up-regulated during neutrophilic differentiation of human MPD and HL-60 cells but down-regulated during monocytic differentiation of HL-60 cells. The hLRG gene was localized to chromosome 19p13.3, a region to which the genes for several neutrophil granule enzymes also map. The putative promoter region of LRG was found to contain consensus-binding sites for PU.1, C/EBP, STAT, and MZF1. These results suggest that LRG is a novel marker for early neutrophilic granulocyte differentiation.

Key Words: RDA • 32Dcl3G • LRG • myelopoiesis




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