Sex Specific Binding of Steroid Hormones to Microsomal Membranes of Rat Liver

Blyth, Carol A.; Freedman, Robert B.; Rabin, B. R.

doi:10.1038/newbio230137a0

Cited by 54 publications

(19 citation statements)

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“…There are three distinct and separate modes of binding. I n region A 30 nmol oestradiol per g membrane protein are bound to the high affinity sites already reported [4]. The control treatment of smooth membranes with EDTA leaves these sites entirely unaffected.…”

Section: Male Membranes and Oestradiolmentioning

confidence: 83%

“…Previous observations [4] showed that high affinity steroid binding sites of smooth membranes (5 mg proteinlml) are saturated when the free steroid concentration is above 400nM and this level is achieved when the total steroid concentration is above 700 nRI. The concentrations of steroids and of extracts used in pretreatment of smooth membranes were calculated to achieve saturation of these high affinity sites.…”

Section: Pretreatment Of Smooth Membranes With Steroids or Extracts mentioning

confidence: 99%

“…If degranulated rough membranes contain the same concentration of hormone binding sites as smooth membranes and these are all occupied by the appropriate steroid, the minimum concentration of the extracts can be calculated from previously published data [4]. The approximate minimum concentrations of the steroids or equivalent substances are expected to be 1 .…”

Section: Preparation Of Ethyl Acetate Extracts Of Degranulated Rough mentioning

confidence: 99%

“…J. Biochem., Vol.29 terone but not oestradiol, and male smooth membranes contain analogous sites for oestradiol but not testosterone [4,5].…”

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confidence: 99%

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The Binding of Steroid Hormones to Degranulated Microsomes from Rat‐Liver Endoplasmic Reticulum

Blyth

Cooper

Roobol

et al. 1972

European Journal of Biochemistry

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1.Smooth reticular membranes from male rat liver contain high affinity binding sites for 2. Rough membranes from which polysomes have been removed by EDTA (degranulated 3. Ethyl acetate extracts of degranulated membranes contain materials which block the high 4. These extracts promote the at,tachment of ribosomes to smooth membranes of the same but 5. The ethyl acetate extracts from male and female degranulated membranes contain suboestradiol. Similar membranes from females contain analogous sites for testosterone. membranes), contain no high affinity binding sites for either hormone. affinity binding sites on smooth membranes of the same but not the opposite sex.not the opposite sex.stances which behave like oestradiol and testosterone, respectively.Polysomes can be removed from rough reticular membranes by treatment with EDTA, and the resultant degranulated membranes will rebind polysomes from the same, but not the opposite, sex in presence of magnesium ions [l-31. Smooth membranes, in contrast, will not bind polysomes unless a steroid hormone is also added. The steroid hormone requirements are sex-specific : oestradiol promotes binding of male polysomes to male smooth membranes and testosterone has a similar interaction in the female, in vitro [l-31. Female polysomes will bind to male smooth or degranulated rough membranes in presence of testosterone, and male polysomes to female membranes in the presence of oestradiol [2]. Oestradiol or testosterone can be replaced in the binding experiments by ethyl acetate extracts of female or male polysomes, respectively, [2]. A similar extract of male rough reticulum can be substituted for both testosterone and oestradiol, acting as a mixture of these two hormones [2]. It is possible that the basic difference between smooth and degranulated rough membranes from male rat liver is that the latter membranes already contain oestradiol (or a related substance callcd "0-substance" in [2]). Similarly female degranulated rough membranes would contain testosterone or "T-substance". Consistently, it has been shown that female smooth membranes possess "high-affinity" sites for testosTrivial Names. Cholesterol, 5-cholesten-3@-01; testosterone, 17/3-hydroxy-4-androsten-3-one.20 Eur. J. Biochem., Vol.29 terone but not oestradiol, and male smooth membranes contain analogous sites for oestradiol but not testosterone [4,5].I n this paper, we present data on the binding of steroid hormones and polyribosomes to degranulated rough microsomes from male and female rat liver. We show that materials can be extracted from degranulated rough membranes which block the "high affinity" steroid binding sites on, and cause polyribosome binding to, the smooth membranes of the same, but not the opposite, sex. MATERIALS AND METHODS Smooth and Rough Microsomal FractionsThese were prepared from the livers of 200g albino rats by differential centrifugation on a sucrosedensity gradient as described previously [5]. Degranulated Rough MembranesRough microsomal membranes were resuspended in 0.25 M sucroae s...

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Section: Male Membranes and Oestradiolmentioning

confidence: 83%

Section: Pretreatment Of Smooth Membranes With Steroids or Extracts mentioning

confidence: 99%

Section: Preparation Of Ethyl Acetate Extracts Of Degranulated Rough mentioning

confidence: 99%

“…J. Biochem., Vol.29 terone but not oestradiol, and male smooth membranes contain analogous sites for oestradiol but not testosterone [4,5].…”

mentioning

confidence: 99%

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The Binding of Steroid Hormones to Degranulated Microsomes from Rat‐Liver Endoplasmic Reticulum

Blyth

Cooper

Roobol

et al. 1972

European Journal of Biochemistry

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“…The reactivity of this cell of ovarian origin to testosterone but not to estradiol is reminescent of the demonstration of sex specificity in binding sites for sex hormones on intracellular membranes of rat liver cells (18,19). Activation of isolated endoplasmic reticulum from such cells required estradiol in the male, and testosterone in the female.…”

Section: Discussionmentioning

confidence: 93%

Further Changes in Differentiation State Accompanying the Conversion of Chinese Hamster Cells to Fibroblastic Form by Dibutyryl Adenosine Cyclic 3′:5′-Monophosphate and Hormones

Hsie

Jones

Puck

1971

Proc. Natl. Acad. Sci. U.S.A.

206

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The morphological conversion in vitro of Chinese hamster ovary cells to a fibroblast form by a relatively large amount of dibutyryl adenosine cyclic 3':5'-monophosphate, or by a combination of small amounts of this compound and testosterone, is attended by appearance of the following additional properties: acquisition of strict contact inhibition of growth; reorientation of the random growth pattern into one in which cells grow parallel to their long dimension; disappearance of the randomly distributed, knob-like, pseudopodal structures around the cell periphery; induction of collagen synthesis; and decrease in the ability to be agglutinated and rounded up by plant agglutinins and specific cell antibodies. The changes in these characteristics are consistent with the conversion from a malignant to a normal fibroblastic state.,) This conversion is under genetic control, as demonstrated by the production of specific mutants with altered characteristics. The response to testosterone is specific since steroids like estradiol and hydrocortisone are inactive, and others have limited activity. Some prostaglandins are equal in activity to testosterone and 5a-dihydrotestosterone. This system appears useful in study of the regulation of phenotypic expression in mammalian cells.In previous communications (1, 2) it was shown that treatment of Chinese hamster ovary cells in vitro with dibutyryl adenosine cyclic 3': 5'-monophosphate (But2A>p) converts a compact, randomly oriented cell culture which grows in a multilayered form into a monolayer of elongated fibroblastlike cells which grow parallel to one another. Testosterone, which has a similar though smaller effect at high concentrations, potentiates the action of But2A>p so that maximal, morphological conversion can be obtained by the joint action of both agents in concentrations of each which are virtually inactive when used singly. The transformation affects cells throughout most of the life cycle, is completely reversible, need not materially change the rate of cell reproduction, and can be inhibited by agents, like colcemid and vinblastine, which prevent assembly of cellular microtubules. Similar findings concerning the action of But2A>p, but not the hormone effect, have been reported by other investigators (3).The change from contact-inhibited, monolayered growth to multiple-layered growth that does not exhibit contact inhibition, has been associated with the conversion of normal, differentiated cells to malignancy. Therefore, it was important to investigate aspects of the present reversible cell transformation that might illuminate the relevance of these observations to the problem of loss and gain of specific differentiation characteristics and their implication for cancer. The present paper describes further properties of this reversible system. METHODS AND MATERIALSThe Chinese hamster ovary clone CHO-Kl, previously described, was used in all of these experiments (4). The properties of this cell line and procedures used in its cultivation have been reported ...

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Vitamin D and the Skeleton

Kodíček

1973

Novartis Foundation Symposia

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Sex Specific Binding of Steroid Hormones to Microsomal Membranes of Rat Liver

Cited by 54 publications

References 3 publications

The Binding of Steroid Hormones to Degranulated Microsomes from Rat‐Liver Endoplasmic Reticulum

The Binding of Steroid Hormones to Degranulated Microsomes from Rat‐Liver Endoplasmic Reticulum

Further Changes in Differentiation State Accompanying the Conversion of Chinese Hamster Cells to Fibroblastic Form by Dibutyryl Adenosine Cyclic 3′:5′-Monophosphate and Hormones

Vitamin D and the Skeleton

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