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J Biol Chem, Vol. 273, Issue 45, 29607-29614, November 6, 1998
Mediates Peroxisome
Proliferation in the Absence of Extracellular Stimuli
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From the Mammalian cells typically contain hundreds of
peroxisomes but can increase peroxisome abundance further in response
to extracellular stimuli. We report here the identification and
characterization of two novel human peroxisomal membrane proteins,
PEX11 Department of Biology, The Johns Hopkins
University, Baltimore, Maryland 21218 and the Departments of
§ Biological Chemistry and Cell Biology and Anatomy, and
¶ Pediatrics and Molecular Biology and Genetics, and the
Howard Hughes Medical Institutes, The Johns Hopkins University
School of Medicine, Baltimore, Maryland 21205
and PEX11
. Overexpression of the human PEX11
gene alone was sufficient to induce peroxisome proliferation,
demonstrating that proliferation can occur in the absence of
extracellular stimuli and may be mediated by a single gene. Time course
studies indicated that PEX11 induces peroxisome proliferation
through a multistep process involving peroxisome elongation and
segregation of PEX11 from other peroxisomal membrane proteins,
followed by peroxisome division. Overexpression of PEX11
also induced peroxisome proliferation but at a much lower frequency
than PEX11 in our experimental system. The patterns of
PEX11 and PEX11 expression were examined
in the rat, the animal in which peroxisome proliferation has been
examined most extensively. Levels of PEX11 mRNA were
similar in all tissues examined and were unaffected by
peroxisome-proliferating agents. Conversely, PEX11
mRNA levels varied widely among different tissues, were highest in
tissues that are sensitive to peroxisome-proliferating agents, and were
induced more than 10-fold in response to the peroxisome proliferators
clofibrate and di(2-ethylhexyl) phthalate. Taken together, these data
implicate PEX11 in the constitutive control of peroxisome abundance
and suggest that PEX11 may regulate peroxisome abundance in response
to extracellular stimuli.
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