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 Previous Article | Table of Contents | Next Article 
Lactoferrin gene promoter: structural integrity and nonexpression in HL60
cells
JJ Johnston, P Rintels, J Chung, J Sather, EJ Benz and N Berliner
Department of Internal Medicine, Yale University School of Medicine, New
Haven, CT 06510.
Lactoferrin is a member of the transferrin family of iron-binding proteins.
It is found in several glandular epithelial tissues and human neutrophils,
where it is localized to secondary granules. To examine the mechanisms
controlling lactoferrin gene expression in neutrophils and defects in its
expression in acute leukemia, we have cloned a lactoferrin cDNA from a
chronic myelogenous leukemia library, and used it to obtain genomic clones
representing the chromosomal lactoferrin gene. Using polymerase chain
reaction, primer extension, and S1 analysis, we have identified the 5' end
of the lactoferrin mRNA. We have defined a putative promoter region for the
gene, and characterized its first two exons. In addition, we have examined
the structure of these regions in DNA from HL60 cells. HL60 is a leukemic
cell line that undergoes phenotypic neutrophil maturation on exposure to
dimethyl sulfoxide (DMSO). However, the cells cannot be induced to express
any secondary granule protein genes. We have shown that the 5' end of the
lactoferrin gene, including the putative promoter region, is entirely
normal in HL60. By Northern analysis, nuclear run-on studies, and primer
extension assays we have shown that the gene is not transcribed in
DMSO-induced HL60 cells. This supports the hypothesis that the defect in
HL60 is an abnormality in the production or activity of a transacting
regulator of lactoferrin gene expression.
Volume 79,
Issue 11,
pp. 2998-3006,
06/01/1992
Copyright © 1992 by The American Society of Hematology
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