Pgk-1 is an X-linked gene encoding 3-phosphoglycerate kinase, an enzym
e necessary in every cell for glycolysis. The regulatory sequences of
the Pgk-1 gene were used to drive the E. coli lacZ reporter gene and 2
strains of transgenic animals created with this Pgk-lacZ transgene ca
rried on autosomes. The levels of expression of Pgk-1 varied from one
adult tissue to another and the transgene was similarly regulated. How
ever, in situ staining of the beta-galactosidase encoded by the transg
ene indicated extensive cell-to-cell variability in its level of expre
ssion. A reproducible subset of cells stained darkly for the transgene
product. Some of these beta-galactosidase positive cells were rapidly
proliferating while others appeared to be metabolically very active,
suggesting that the Pgk-1 promoter is regulated so as to be more activ
e in cells requiring high levels of glycolysis. Although Pgk-l is X-li
nked and subject to X chromosome inactivation, the transgenes were not
inactivated in either female somatic or male germ cells. Thus, the Pg
k-1 promoter drives transgene expression in all tissues but the levels
of expression are not uniform in each cell. (C) 1994 Wiley-Liss, Inc.