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Isolation and characterization of a TATA-less promoter for the human beta 3
integrin gene
M Villa-Garcia, L Li, G Riely and PF Bray
Department of Medicine, Johns Hopkins School of Medicine, Baltimore, MD
21205.
Proper expression of the human platelet fibrinogen receptor is necessary
for the maintenance of normal hemostasis. This receptor is formed by the
heterodimer alpha IIb beta 3, a prototypic member of the integrin family of
adhesive molecules. beta 3 is also expressed in other tissues with alpha v
as the vitronectin receptor. It was not possible to study the basis for
tissue-specific expression of this gene, because the beta 3 gene promoter
had not been isolated previously. We have now isolated a 6.0-kb human
genomic DNA fragment containing 2.0 kb of sequence 5' to the beta 3 ATG
start codon. This clone also contains sequence encoding the signal peptide
of the immature beta 3 protein and 3.0 kb of 3' intronic sequence. Primer
extension and RNase protection studies of poly A+ RNA from a human
erythroleukemia (HEL) cell line indicated a major transcription start site
30 bp upstream of the ATG start codon. In an orientation-dependent manner,
a 584-bp fragment 5' to the start codon promotes expression of the
chloramphenicol acetyl transferase (CAT) reporter gene in K562 cells. CAT
expression from this beta 3 promoter is fivefold above expression from a
"promoter-less" control CAT construct. This beta 3 promoter lacks TATA and
CAAT cis-acting elements, but there are two Sp1 sites flanking the
transcription start site. Other potential transcription factor binding
sites are also identified. Phorbol esters (TPA), which increase beta 3
transcription in K562 cells, stimulated transcription from the 584-bp 5'
beta 3 region. The isolation of this beta 3 promoter region should permit a
more detailed analysis of its transcriptional regulation.
Volume 83,
Issue 3,
pp. 668-676,
02/01/1994
Copyright © 1994 by The American Society of Hematology
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