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J. Biol. Chem., Vol. 276, Issue 1, 715-721, January 5, 2001
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From the Department of Pharmacology, Yale University School of
Medicine, New Haven, Connecticut 06520
Rat prolactin in the dense cores of secretory
granules of the pituitary gland is a Lubrol-insoluble aggregate. In
GH4C1 cells, newly synthesized rat
prolactin and growth hormone were soluble, but after 30 min about 40%
converted to a Lubrol-insoluble form. Transport from the endoplasmic
reticulum is necessary for conversion to Lubrol insolubility, since
incubating cells with brefeldin A or at 15 °C reduced formation of
insoluble rat 35S-prolactin. Formation of Lubrol-insoluble
aggregates has protein and cell specificity; newly synthesized human
growth hormone expressed in AtT20 cells underwent a 40% conversion to
Lubrol insolubility with time, but albumin did not, and human growth
hormone expressed in COS cells underwent less than 10% conversion to
Lubrol insolubility. del32-46 growth hormone, a naturally occurring
form of growth hormone, and P89L growth hormone underwent conversion,
although they were secreted more slowly, indicating that there is some tolerance in structural requirements for aggregation. An intracellular compartment with an acidic pH is not necessary for conversion to Lubrol
insolubility, because incubation with chloroquine or bafilomycin
slowed, but did not prevent, the conversion.
GH4C1 cells treated with estradiol, insulin,
and epidermal growth factor accumulate more secretory granules and
store more prolactin, but not more growth hormone, than untreated
cells; Lubrol-insoluble aggregates of prolactin and growth hormone
formed to the same extent in hormone-treated or untreated
GH4C1 cells, but prolactin was retained longer
in hormone-treated cells. These findings indicate that aggregation
alone is not sufficient to cause retention of secretory granule
proteins, and there is an additional selective process.
Acquisition of Lubrol Insolubility, a Common Step for Growth
Hormone and Prolactin in the Secretory Pathway of Neuroendocrine
Cells*
*
This work was supported by National Institutes of Health
Grant DK 46807 and a grant from the American Diabetes Association.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Pharmacology,
Yale University School of Medicine, 333 Cedar St., New Haven, CT
06520-8066. Tel.: 203-785-4539; Fax: 203-737-2027; E-mail: priscilla.dannies@yale.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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