Premium
Molecular characterization and expression analysis of leucine‐rich α2‐glycoprotein, a novel marker of granulocytic differentiation
Author(s) -
O’Donnell Lynn C.,
Druhan Lawrence J.,
Avalos Belinda R.
Publication year - 2002
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.72.3.478
Subject(s) - biology , microbiology and biotechnology , cellular differentiation , lactoferrin , complementary dna , gene , progenitor cell , glycoprotein , stem cell , genetics
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 α2‐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.