Discussion Paper: Mero‐Receptor Formation From a Larger Subcomponent of the Oviduct Progesterone Receptor<sup>*</sup>

Sherman, Merry R.; Diaz, Soledad C.

doi:10.1111/j.1749-6632.1977.tb29406.x

Cited by 16 publications

(13 citation statements)

References 9 publications

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“…Both crude protease extracts and partially purified enzyme (Vedeckis et al, 1980) were used. Contrary to other studies (Sherman & Diaz, 1977), we report that both receptor proteins are digested to form IV and ultimately to 1 Abbreviations used: RTF, receptor transforming factor; DES, diethylstilbestrol; Na2EDTA, disodium ethylenediaminetetraacetate; DEAE, diethylaminoethyl; [3H] progesterone, [ 1,2-3H2] progesterone; [3H]A, [3H]progesterone-progestophilin A complex; [3H]B, [3H]progesterone-progestophilin B complex. the meroreceptor.…”

contrasting

confidence: 74%

“…This enzyme is a calcium-activated protease very similar to the estrogen "receptor transforming factor" (RTF)1 in calf uterine cytosol characterized by co-workers (Puca et al, 1972, 1977;Sica et al, 1976). In the oviduct cytosol, the protease was shown (Sherman et al, 1974(Sherman et al, , 1976Sherman & Diaz, 1977) to digest the B receptor protein to a hormone-binding fragment termed the meroreceptor (Afr 23000; Stokes radius = 2.1 nm; sedimentation coefficient = 2.6 S) while the hormone-binding cleavage product of the A protein appeared to be a larger fragment, form IV (MT 43 000; Stokes radius = 2.7 nm; sedimentation coefficient = 3.6 S). Since the proteolytic fragments appeared to be different for the two proteins, it was not clear whether the A and B subunits shared identical, or merely kinetically similar, hormone-binding regions.…”

mentioning

confidence: 90%

“…& Diaz, 1977;Vedeckis et al, 1979Vedeckis et al, , 1980. This enzyme is a calcium-activated protease very similar to the estrogen "receptor transforming factor" (RTF)1 in calf uterine cytosol characterized by co-workers (Puca et al, 1972, 1977;Sica et al, 1976).…”

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confidence: 99%

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Progesterone-binding components of chick oviduct: analysis of receptor structure by limited proteolysis

Vedeckis¹,

Schrader²,

O’Malley³

1980

Biochemistry

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An endogenous calcium-activated sulfhydryl protease in chick oviduct cytosol has been utilized to study the structure of the chick oviduct progesterone receptor subunits, progestophilins A (79 000 g/mol) and B (117 000 g/mol). The protease is not a normal component of the native progesterone receptor aggregate (6 and 8 S) complexes. Both receptor protein subunits (A and B) can be cleaved to two hormone-binding fragments, form IV (43 000 g/mol) and meroreceptor (23 000 g/mol). The meroreceptors obtained from the A and B proteins are indistinguishable from each other on the basis of both size (gel filtration chromatography) and charge (isoelectric focusing, pI 8.3). These findings suggest a structural similarity between the A and B proteins. The discovery of a weak deoxyribonucleic acid (DNA) binding activity for the B protein suggests an even greater similarity between B and A subunits, since the A subunit has previously b:en shown to bind to DNA. The proteolytic fragments do not bind to DNA-cellulose, implying that the hormone- and DNA-binding regions of the A and B proteins exist in separate domains.

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Progesterone-binding components of chick oviduct: analysis of receptor structure by limited proteolysis

Vedeckis¹,

Schrader²,

O’Malley³

1980

Biochemistry

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“…Chick cytosol contains a Ca*+-activated protease which cleaves both native receptor subunits into smaller hormonebinding fragments (meroreceptors) and an unknown number of other peptides (Vedeckis et al, 1980;Sherman & Diaz, 1977). 3H-Labeled meroreceptor was prepared as described by Vedeckis et al (1980) and assayed by sucrose-gradient analysis (data not shown) and by protein A-Sepharose (Figure The indicated amounts of receptor were incubated with 150 pL of crude IgG in a final volume of 350 pL for 2 h at 4 O C and assayed by the protein A-Sepharose assay.…”

Section: Resultsmentioning

confidence: 99%

Analysis of chicken progesterone receptor structure using a spontaneous sheep antibody

Weigel¹,

Pousette²,

Schrader³

et al. 1981

Biochemistry

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A spontaneous sheep antibody to chick progesterone receptor was characterized and used as a tool to study the receptor structure. The antibody, which is present to some extent in sera from about one-third of the sheep tested, binds to Staphylococcus aureus protein A--Sepharose and therefore appears to be an Igg. It is specific for the chick progesterone receptor and does not react with free progesterone or with any of the other proteins tested, including other receptors and corticosteroid binding globulin. The antibody os nonprecipitating and has a vary low titer (equivalence point = 2.5 pmol of receptor/mL of serum). The interaction of the receptor with the antibody was measured, and an apparent dissociation constant of 2 x 10(-9) M was determined from these studies. The antibody reacts equally well with the two receptor subunits A and B but does not appear to react with the native aggregate form found in the cytosol. Thus, the immunologic site is occluded in the aggregate, and therefore the antibody will be a useful probe for this important region of the proteins. The antibody recognition sites on the receptors were further characterized by analysis of a proteolytic digest of receptors by using an endogenous Ca2+-activated neutral protease. Competition studies using native receptor and receptor digests demonstrated that the antigenic site was not destroyed in the digest and was separated from the hormone binding fragment. We conclude that receptor subunits A and B have a cross-reactive immunologic site on a portion of the molecule other than the hormone binding domain.

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“…Sherman and co-workers [8-101 have shown that, in the presence of 20 to 100 mM calcium, the progesterone receptor in chick oviduct cytosol is cleaved by protease(s) to form a 20,000 molecular weight mero-receptor [8] that can bind progesterone with the same affinity as the high molecular weight progesterone receptors. We incubated chick oviduct cytosol overnight in 20 mM calcium chloride at 4", conditions known to result in complete conversion of the progesterone receptor to the 20,000 molecular weight form [8][9][10][11]. Complete formation to the mero-receptor was varified by filtration on agarose, as described by Sherman et a1 [8].…”

Section: Baker Vaughn and Fanestilmentioning

confidence: 99%

Inhibition by protease inhibitors of binding of adrenal and sex steroid hormones

1978

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Binding of steroid hormones is inhibited by protease inhibitors and substrates. The protease inhibitors phenylmethyl sulphonylfluoride, tosyl-lysine chloromethyl ketone, and tosylamide-phenylethyl-chloromethyl ketone and the protease substrates tosyl arginine methyl ester and tryptophan methyl ester eliminate specific binding of aldosterone, dexamethasone, dihydrotestosterone, estrogen, and progesterone to their respective receptors. These protease inhibitors and substrates also inhibit binding of progesterone to the 20,000 molecular weight mero-receptor formed from the progesterone receptor in chick oviduct. The binding of estradiol to rat alpha-fetoprotein is inhibited by the protease inhibitors and substrates but not by tryptophan or tryptophan amide, indicating the importance of an ester structure in the inhibition of steroid binding. Our results suggest that all steroid hormone receptors have a site with both common structural features and a role in the regulation of steroid hormone binding.

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Discussion Paper: Mero‐Receptor Formation From a Larger Subcomponent of the Oviduct Progesterone Receptor^*

Cited by 16 publications

References 9 publications

Progesterone-binding components of chick oviduct: analysis of receptor structure by limited proteolysis

Progesterone-binding components of chick oviduct: analysis of receptor structure by limited proteolysis

Analysis of chicken progesterone receptor structure using a spontaneous sheep antibody

Inhibition by protease inhibitors of binding of adrenal and sex steroid hormones

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Discussion Paper: Mero‐Receptor Formation From a Larger Subcomponent of the Oviduct Progesterone Receptor*

Cited by 16 publications

References 9 publications

Progesterone-binding components of chick oviduct: analysis of receptor structure by limited proteolysis

Progesterone-binding components of chick oviduct: analysis of receptor structure by limited proteolysis

Analysis of chicken progesterone receptor structure using a spontaneous sheep antibody

Inhibition by protease inhibitors of binding of adrenal and sex steroid hormones

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Discussion Paper: Mero‐Receptor Formation From a Larger Subcomponent of the Oviduct Progesterone Receptor^*