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J. Biol. Chem., Vol. 258, Issue 17, 10312-10324, Sep, 1983
A Sobel and AH Tashjian Jr
The actions of thyrotropin-releasing hormone (TRH) on protein
phosphorylation in the GH4C1 clonal strain of rat pituitary cells were
examined by two-dimensional polyacrylamide gel electrophoresis and related
to the ability of this tripeptide to stimulate prolactin (PRL) synthesis
and release, respectively. Between 2 and 10 min after addition of the
hormone, TRH increased the rate of phosphorylation of a small number of
specific cytoplasmic proteins. The dose-response characteristics for
TRH-induced protein phosphorylation were closely similar to those for its
biological actions (ED50 congruent to 2 nM). TRH did not stimulate protein
phosphorylation in the related GH12C1 cell strain which lacks TRH
receptors. The proteins modified by TRH treatment were present in low
amounts in the cell; they were not detectable by silver staining of the
gels, except for protein 1 (Mr = 80,000) whose TRH-induced conversion from
its unphosphorylated to its more acidic phosphorylated form was observed
directly on silver-stained gels. Two distinct sets of phosphoproteins were
identified among the seven affected by TRH: set I, five proteins whose
phosphorylation was increased only by agents which stimulated PRL
synthesis; and set II, two proteins whose phosphorylation was also
increased by vasoactive intestinal peptide, which stimulates PRL release
but not its synthesis in GH4C1 cells. This distinction between
phosphoproteins related either to the release or synthesis of PRL was
substantiated further by the use of an analog of TRH, A42658, which
stimulated PRL synthesis and phosphorylation of proteins of set I at a
lower concentration (0.2-0.5 microM) than was required to stimulate PRL
release and phosphorylation of proteins of set II (greater than 0.5
microM). Finally, pretreatment of the cells with 1 mM ethylene glycol
bis(beta-aminoethyl ether)- N,N,N',N'-tetraacetic acid, which prevents
TRH-induced PRL release but not synthesis, also suppressed TRH-stimulated
phosphorylation of proteins of set II, but not of set I. These results
relate stimulation by TRH of the phosphorylation of two distinct sets of
proteins to the two major biological action of TRH in GH4C1 cells; proteins
of set I appear to be related to the regulation of PRL synthesis, whereas
those of set II appear related to modulation of PRL release.
Distinct patterns of cytoplasmic protein phosphorylation related to regulation of synthesis and release of prolactin by GH cells
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