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J. Biol. Chem., Vol. 261, Issue 26, 11962-11967, 09, 1986
SH Kaufmann, S Okret, AC Wikstrom, JA Gustafsson and JH Shaper
The nuclear matrix is a putative skeletal structure which has been
implicated in many nuclear functions. To assess a possible role of the
nuclear matrix in glucocorticoid action, purified rat liver nuclei
containing glucocorticoid-receptor complexes were treated with DNase I +/-
RNase A followed by 1.6 M NaCl, thus yielding salt-extractable and
salt-resistant (nuclear matrix) fractions. The subnuclear distribution of
hormone-receptor complexes was determined by following the fate of
unmetabolized radiolabel after injection of labeled triamcinolone acetonide
into adrenalectomized animals and subjecting various subfractions to
immunoblotting using a monoclonal antibody which recognizes the
glucocorticoid receptor. Both techniques indicated that 50-70% of the total
nuclear hormone-receptor complexes were recovered in the nuclear matrix
fraction. Previous results (Kaufmann, S. H., and Shaper, J. H. (1984) Exp.
Cell Res. 155, 477-495) suggest that a variety of nuclear polypeptides
become nuclease- and salt-resistant as a result of the formation of
intermolecular disulfide bonds. The following evidence suggests that
disulfide bonds mediate the association between the glucocorticoid receptor
and the nuclear matrix. When nuclei were isolated in the absence of
sulfhydryl-blocking and - cross-linking reagents, sodium dodecyl
sulfate-polyacrylamide gel electrophoresis under nonreducing conditions
revealed that the receptor was present as a high molecular weight
disulfide-cross-linked complex. When nuclei were isolated in the presence
of the irreversible sulfhydryl-blocking reagent iodoacetamide, the
disulfide bonds which cross-linked the receptor into high molecular weight
complexes were absent; and 85-100% of the hormone-receptor complexes were
salt- extractable. When nuclei (isolated in the absence of iodoacetamide)
were treated with the sulfhydryl-cross-linking reagent sodium
tetrathionate, greater than 95% of the nuclear hormone-receptor complexes
became resistant to extraction with nucleases and 1.6 M NaCl. The
implications of these results for other matrix-associated nuclear functions
are discussed.
Binding of the glucocorticoid receptor to the rat liver nuclear matrix. The role of disulfide bond formation
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