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Vol. 8, Issue 10, 1911-1931, October 1997
Department of Cellular and Structural Biology, University of
Colorado School of Medicine, Denver, Colorado 80262
To characterize endogenous molecules and activities of the Golgi
complex, proteins in transit were >99% cleared from rat hepatocytes by using cycloheximide (CHX) treatment. The loss of proteins in transit
resulted in condensation of the Golgi cisternae and stacks. Isolation
of a stacked Golgi fraction is equally efficient with or without
proteins in transit [control (CTL SGF1) and cycloheximide (CHX
SGF1)]. Electron microscopy and morphometric analysis showed that
>90% of the elements could be positively identified as Golgi stacks
or cisternae. Biochemical analysis showed that the cis-, medial-, trans-, and TGN Golgi markers were enriched
over the postnuclear supernatant 200- to 400-fold with and 400- to
700-fold without proteins in transit. To provide information on a
mechanism for import of calcium required at the later stages of the
secretory pathway, calcium uptake into CTL SGF1 and CHX SGF1 was
examined. All calcium uptake into CTL SGF1 was dependent on a
thapsigargin-resistant pump not resident to the Golgi complex and a
thapsigargin-sensitive pump resident to the Golgi. Experiments using
CHX SGF1 showed that the thapsigargin-resistant activity was a plasma
membrane calcium ATPase isoform in transit to the plasma membrane and
the thapsigargin-sensitive pump was a sarcoplasmic/endoplasmic
reticulum calcium ATPase isoform. In vivo both of these calcium ATPases function to maintain millimolar levels of calcium within the Golgi lumen.
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