Autoradiographic Localization of Albumin-<sup>131</sup>I Accumulation in the Estrogen-Stimulated Rat Uterus

Peterson, Roy P.; Spaziani, Eugene

doi:10.1210/endo-89-5-1280

Cited by 25 publications

(8 citation statements)

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“…Analyses of uterine fluids show the existence of prealbumin, albumin, and globulins similar to those present in the blood plasma (Beier, 1968;Peterson and Spaziani, 1971). Our studies, using an exogenous protein tracer ~horseradish peroxidase), show that the movement of plasma-derived proteins into the uterine lumen is blocked by tight junctions between endometrial cells.…”

Section: The Transendometrial Transport Of Enzymesmentioning

confidence: 99%

Endogenous peroxidase: specific marker enzyme for tissues displaying growth dependency on estrogen.

Anderson¹,

Kang²,

DeSombre³

1975

The Journal of Cell Biology

106

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Data derived from a correlated morphological and biochemical study suggest the following: (a) estradiol-17~, diethylstilbestrol, the estrogen antagonists nafoxidine (Upjohn 11,100), and Parke Davis CI628 induce synthesis of an endogenous peroxidase in the epithelium of target tissues like the vagina, the cervix, the uterus, and in the acinar cells of the estrogen-dependent rat mammary tumor; (b) peroxidase is a "specific" secretory protein of the estrogen-sensitized uterine endometrium; (c) peroxidase synthesis is not a nonspecific response to steroid hormone action, since progesterone and testosterone do not induce its synthesis; (d) endogenous peroxidase is a possible diagnostic protein for the detection of estrogen-dependent growing tissues, including breast cancer; (e) movement of exogenous horseradish peroxidase from the interstitium to the uterine lumina is restricted by tight junctions located at the apices of epithelial cells. Estrogen and antagonists do not appear to influence the transepithelial movement of exogenous peroxidase into the lumen.The uterus, cervix, vagina, and mammary gland of mammals require estrogen for their postpubertal trophic development and for the maintenance of their differentiated state. Indeed, the presence of estrogen-binding proteins (estrogen receptors or estrophiles, Jensen et al., 1966 a) in these tissues and of estrogen dependency of rat and human mammary carcinoma are well documented (Huggins et al., 1959; Jensen et al., 1966 b;Heuson et al., 1972).In the course of our investigation it was discovered that tissues displaying growth dependency on estrogen synthesize and secrete "specific marker proteins" into their lumina. These results show (a) that synthesis of peroxidase ~ (or a hemoprotein with peroxidatic activity) is a consistent marker for estrogen-dependent tissues (carcinogen-induced rat mammary carcinoma, cervix, vagina, and uterus), (b) estrogen antagonists (Upjohn 11,100; ~Throughout this paper, the DAB-positive reaction product will be referred to as peroxidase, since uterine peroxidase is a well-documented enzyme (see text) and since the histochemical medium employed is designed to demonstrate peroxidase activity. It is of course possible that what is being visualized in either a hemeprotein, which may possess peroxidase activity, or several substances with peroxidasic activity. The biochemical characterization of this enzyme as a peroxidase is still very limited.

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Section: The Transendometrial Transport Of Enzymesmentioning

confidence: 99%

Endogenous peroxidase: specific marker enzyme for tissues displaying growth dependency on estrogen.

Anderson¹,

Kang²,

DeSombre³

1975

The Journal of Cell Biology

106

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“…According to Milgrom & Baulieu (1970&), CBG in rat uterus is an intracellular component. However, according to Peterson & Spaziani (1971), plasma proteins tend to penetrate specific tissue sites, particularly those with a high collagen foundation as, for instance, in the uterus during oestrogen stimulation ; in general, the connective tissue component of the uterus appears to function as a temporary pool for extracellular plasma protein. The latter observation has a bearing on an interesting hypothesis proposed by Keller, Richardson & Yates (1969) regarding protein binding and the biological activity of corticosteroids in certain peripheral tissues, i.e.…”

Section: Discussionmentioning

confidence: 99%

A Comparative Study of Progesterone- And Cortisol-Binding Activity in the Uterus and Serum of Pregnant and Non-Pregnant Women

Gueriguian¹,

Sawyer²,

Pearlman³

1974

Journal of Endocrinology

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The 105000 g supernatant fraction (soluble proteins) of homogenates of human uterine tissue, essentially myometrium, and peripheral blood serum, were assayed for progesterone-and cortisol-binding activity by batchwise use of Sephadex G-25 in test tubes (not gel filtration) under equilibrium conditions; the results were expressed empirically as the reciprocal of the protein concentration, 1/P, at 50% steroid binding. The steroid-binding activity of the uterine soluble proteins was due apparently to a single component closely resembling corticosteroid-binding globulin (CBG) with respect to equilibrium association constants, steroid ligand specificity, and elution behaviour on hydroxylapatite chromatography and Sephadex G-100 filtration. Therefore, the mean 1/P values for steroid-binding activity were converted to the apparent CBG content (nmol/g total soluble protein). Comparison of the mean ratio (about 0\m=.\2) of the respective total binding activity, uterus (g): serum (ml), with the mean ratio (0\m=.\03) of the total iron content, uterus:serum, indicated that the high CBG content of the uterus could not be attributed to retention of blood; the apparent CBG levels in skeletal muscle (pectoral) were very low. The mean values for the apparent CBG content of uterine soluble protein were almost as high as those for the CBG content of serum protein; the mean value for the apparent CBG content of uterine soluble protein was slightly higher for pregnant women (mostly in early pregnancy) than that for non-pregnant women with various gynaecological complications. On polyacrylamide gel electrophoresis, soluble protein from the uterus resembled that of serum in the areas corresponding to serum albumin and transferrin; the electrophoretic patterns were distinctly different, however, in the area between the origin and the transferrin band.It is suggested that CBG may accumulate in interstitial fluid of the myometrium, thereby regulating the local concentration of bound and unbound progesterone and cortisol, and influencing hormone action on the respective target cells, muscle and fibroblast. A more extensive study of levels of progesterone-and cortisol-binding activity in serum was carried out also. It was concluded that the progesterone-binding activity of human serum, as in the case of human myometrium, is due largely to CBG.

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“…The uptake of pro teins, including prothrombin, 2 serum albumin, soybean trypsin inhibitor, fibrinogen, and α 2 -macroglobulin 3 has been described. Serum albumin, 4 plasminogen, 5 and α 1protease inhibitor 3 move through the uterus and are found in the uterine lumen within 6 hours of E 2 stimulation; endogenous and plasma plasminogen activators also migrate into the lumen. 6 Early uterine genomic responses to E 2 follow a welldefined path.…”

Section: The Uterus and Estradiolmentioning

confidence: 99%

Thrombin as a Hormonally Regulated Growth Factor in Estrogen-Responsive Tissue

Henrikson¹

1992

Semin Thromb Hemost

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The possibility that thrombin has a physiologic role in addition to its central place in coagulation is indicated by observations that thrombin is a mitogen or potentiator of other peptide growth factors in various cell types. In this article I explore the possibility that thrombin might act as a mediator of steroid hormone-directed growth and development. The steroid estradiol (E 2 ) induces increases in tissue factor (TF) and prothrombin by different mech anisms. Increases in both allow a generation of thrombin that is appropriate for its subsequent involvement in ste roid-induced growth and development. THE UTERUS AND ESTRADIOLThe immature rat uterus is a model system in which the molecular mechanism of action of steroid hormones has been studied. Puberty in the rat begins at about 7 weeks of age. At that time, the ovaries begin to make significant quantities of E 2 ; the uterus responds to the E 2 stimulation with a burst of growth and development that is in part mediated by the estrogen receptor found within the uterine cells.A 19-to 21-day-old female rat has a full comple ment of estrogen receptors within the uterus and a very low plasma E 2 concentration. A single injection of E 2 has dramatic effects, which are generally categorized as early (within 3 to 6 hours of injection) and late (after 12 to 24 hours). 1 Late effects include a general increase in net protein, RNA, and DNA synthesis, followed by cell divi sion. Early responses include a dramatic increase in wet weight (50% within 3 hours) and an increase in selected mRNAs and proteins. The early increases in mRNA are consequences of specific actions of E 2 , which result in increases in a limited number of proteins that are believed to be central to the development of the uterus.Early uterine effects of E 2 can be divided into ge nomic and nongenomic responses. The nongenomic re sponses generally result from the altered vascular perme ability that occurs after E 2 stimulation, an inflammatory type of response to the steroid. The increase in perme ability allows a massive amount of plasma protein and water to move into the interstitial space of the organ. A wide variety of proteins has been shown to move into the uterus within a defined time period. The uptake of pro teins, including prothrombin, 2 serum albumin, soybean trypsin inhibitor, fibrinogen, and α 2 -macroglobulin 3 has been described. Serum albumin, 4 plasminogen, 5 and α 1 -protease inhibitor 3 move through the uterus and are found in the uterine lumen within 6 hours of E 2 stimulation; endogenous and plasma plasminogen activators also migrate into the lumen. 6 Early uterine genomic responses to E 2 follow a welldefined path. 7-10 E 2 enters the cell by free diffusion, binds to a specific receptor in the nucleus, and as an E 2 -receptor complex promotes gene activity by binding to specific areas of the genome called estrogen response elements (EREs). The activation of the genes results in the specific transcription and translation of genes that are presumed to be involved in the generalize...

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Autoradiographic Localization of Albumin-¹³¹I Accumulation in the Estrogen-Stimulated Rat Uterus

Cited by 25 publications

References 0 publications

Endogenous peroxidase: specific marker enzyme for tissues displaying growth dependency on estrogen.

Endogenous peroxidase: specific marker enzyme for tissues displaying growth dependency on estrogen.

A Comparative Study of Progesterone- And Cortisol-Binding Activity in the Uterus and Serum of Pregnant and Non-Pregnant Women

Thrombin as a Hormonally Regulated Growth Factor in Estrogen-Responsive Tissue

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Autoradiographic Localization of Albumin-131I Accumulation in the Estrogen-Stimulated Rat Uterus

Cited by 25 publications

References 0 publications

Endogenous peroxidase: specific marker enzyme for tissues displaying growth dependency on estrogen.

Endogenous peroxidase: specific marker enzyme for tissues displaying growth dependency on estrogen.

A Comparative Study of Progesterone- And Cortisol-Binding Activity in the Uterus and Serum of Pregnant and Non-Pregnant Women

Thrombin as a Hormonally Regulated Growth Factor in Estrogen-Responsive Tissue

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Autoradiographic Localization of Albumin-¹³¹I Accumulation in the Estrogen-Stimulated Rat Uterus