HORMONAL REGULATION OF RNA AND PROTEIN SYNTHESIS IN THE MOUSE MAMMARY GLAND BEFORE AND DURING LACTATION

1971 ◽  
Vol 50 (2) ◽  
pp. 281-291 ◽  
Author(s):  
M. R. BANERJEE ◽  
FERNE M. ROGERS ◽  
D. N. BANERJEE

SUMMARY As measured by [3H]uridine incorporation in vivo, the low rate of RNA synthesis in the mammary gland of virgin C3H and BALB/c mice increased sixfold in the mammary tissue of 15-day pregnant mice. In the 5-day lactating gland, RNA synthesis was ten times higher than that in virgin mammary tissue. On the 10th day of lactation this increased RNA synthetic activity in the mammary gland was considerably reduced but was still twice that of the mammary tissue of virgin mice. Twenty-four hours after adrenalectomy, RNA synthesis in lactating glands was reduced by over 80%, whereas in the mammary gland before lactation, it was reduced by 20–30% only. A single i.p. injection of 250 μg of cortisol led to a threefold increase of RNA synthesis within 1 to 2 h in lactating glands of adrenalectomized mice; this was followed by a decline. Incorporation of [3H]leucine into trichloroacetic acid-insoluble material from lactating mammary tissue was used as a measure of'total protein' synthesis, and [3H]leucine radioactivity determined in Ca2+−rennin precipitate of 105000 g supernatant of lactating mammary tissue homogenate was used as a measure of casein synthesis. Adrenalectomy caused a 50% reduction of 'total protein' synthesis, whereas synthesis of 'casein-like' phosphoprotein virtually stopped after the operation. The injection of cortisol into adrenalectomized mice induced a selective increase of [3H]leucine incorporation into the casein of lactating glands. The results indicate that RNA synthesis in the mammary tissue is more dependent on adrenal hormones during the functional than the structural state of differentiation. The hormonal regulation of RNA synthesis and its role in milk protein synthesis in the mammary gland in vivo is discussed.


1971 ◽  
Vol 50 (2) ◽  
pp. 241-249 ◽  
Author(s):  
D. Y. WANG ◽  
VICKY AMOR

SUMMARY The rates of synthesis of DNA, RNA and protein of mouse mammary gland explants in organ culture have been determined. Stimulation with insulin resulted in maximal rates of synthesis of these components, all occurring between 18 and 22 h of culture. The use of metabolic inhibitors of DNA, RNA or protein synthesis showed that after insulin stimulation, inhibition of any one of these processes was associated with a reduction in the synthesis of the other two components. Also the maximal rate of protein synthesis is governed by the net amount of RNA formed throughout the period of culture. Evidence is presented that the stimulation of DNA, RNA or protein synthesis by insulin is not due to increased transport of amino acids and that insulin appears to act rapidly on processes which subsequently lead to enhanced synthetic activity.



Endocrinology ◽  
2007 ◽  
Vol 148 (5) ◽  
pp. 2290-2300 ◽  
Author(s):  
Mark D. Aupperlee ◽  
Sandra Z. Haslam

In normal mouse mammary gland, the mitogenic action of progesterone (P) is mediated by two P receptor (PR) isoforms, PRA and PRB. PRA is predominantly expressed in the adult virgin, and PRB is predominantly expressed during pregnancy. To investigate hormonal regulation of PR isoform expression and isoform-specific functions in vivo, adult ovariectomized BALB/c mice were treated for 3, 5, or 10 d with estrogen (E), P, or estrogen plus progesterone (E+P). Using an immunohistochemical approach with isoform-specific antibodies, we investigated hormonal regulation of PRA and PRB and their functional roles in proliferation and morphogenesis. Significant E-induced proliferation was only observed after 5 d at the distal tips of ducts; there was no sidebranching or alveologenesis. P induced proliferation that resulted in sidebranching and alveologenesis, but E+P treatment produced more proliferation sooner and more extensive sidebranching and alveologenesis. PRA levels were increased by E and decreased by P. Increased PRB levels were induced by treatment with P or E+P and coincided with the formation of alveoli. PRA was the predominant PR isoform expressed during sidebranching, and colocalization of PRA with 5-bromo-2′-deoxyuridine revealed that proliferation of PRA-positive and -negative cells was responsible for P-induced sidebranching. PRB was the predominant PR isoform expressed during alveologenesis, and colocalization of PRB with 5-bromo-2′-deoxyuridine showed that both PRB-positive and -negative cells proliferated during alveolar expansion. These results demonstrate different hormonal regulation of PRA and PRB levels in vivo and suggest that P can induce proliferation through either PRA or PRB via direct and paracrine mechanisms.





1971 ◽  
Vol 49 (1) ◽  
pp. 39-49 ◽  
Author(s):  
M. R. BANERJEE ◽  
FERNE M. ROGERS

SUMMARY The influence of oestradiol and progesterone on nucleic acids and protein synthesis during early development of 3- to 4-week-old C3H mouse mammary gland in vivo was studied. The hormones were administered daily by subcutaneous injections for 6–9 days. Uptake of tritium-labelled appropriate nucleoside and amino acid precursors, as determined by radio-chemical and autoradiographic methods, was used as a measure of cellular biosynthesis. Administration of the steroid hormones induces a pronounced increase of RNA, protein, and DNA synthesis in the mammary parenchyma of both intact and ovariectomized mice. Increased RNA and protein synthesis were detectable after two injections of the hormones, the maximal level was reached after the 6th injection. Hormone-induced DNA synthesis rose sharply reaching a peak after four treatments. The stimulatory effect of the steroids on DNA synthesis was more pronounced on the end-bud cells up to the 4th injection but in the duct cells [3H]thymidine uptake continued to rise progressively even after the 6th injection. Autoradiographs showed that the hormones also cause a twofold increase in the silver grain count per nucleus indicating an accelerated uptake rate of the DNA precursor. In end-bud cells mitotic activity, used as a measure of cellular proliferative activity, rose to a sharp peak after four injections of the hormones but in duct cells it continued to rise even after the 6th injection. The significance of these results with respect to further lobulo-alveolar development of the mammary parenchyma is discussed.



1990 ◽  
Vol 125 (1) ◽  
pp. R1-R3 ◽  
Author(s):  
M. Peaker ◽  
E. Taylor

ABSTRACT Mammary tissue from goats had significantly higher aromatase activity at 148-149 days of pregnancy than earlier in pregnancy or during lactation. Aromatase activity was determined by production of 3H2O from [1 β–3H]androstenedione that was inhibited by 4–hydroxyandrostenedione. The time of maximum aromatization was during peak mammary output of oestradiol–17β described previously in vivo in the same species. Aromatase activity in the mouse mammary gland was low and no peak was observed in late pregnancy. It is concluded that the oestrogens produced by the mammary gland in the late–pregnant goat are formed by aromatization of androgens.



2011 ◽  
Vol 24 (7) ◽  
pp. 880-887 ◽  
Author(s):  
Sanaz A. Jansen ◽  
Suzanne D. Conzen ◽  
Xiaobing Fan ◽  
Erica Markiewicz ◽  
Thomas Krausz ◽  
...  


Weed Science ◽  
1980 ◽  
Vol 28 (3) ◽  
pp. 334-340 ◽  
Author(s):  
Luanne M. Deal ◽  
J. T. Reeves ◽  
B. A. Larkins ◽  
F. D. Hess

The effects of chloracetamides on protein synthesis were studied both in vivo and in vitro. Four chloracetamide herbicides, alachlor [2-chloro-2′,6′-diethyl-N-(methoxymethyl)acetanilide], metolachlor [2-chloro-N-(2-ethyl-6-methylphenyl)-N-(2-methoxy-1-methylethyl)acetamide], CDAA (N–N-diallyl-2-chloroacetamide), and propachlor (2-chloro-N-isopropylacetanilide) were tested for inhibition of [3H]-leucine incorporation into protein. Incorporation of3H-leucine into trichloroacetic acid (TCA)-insoluble protein was inhibited in oat (Avena sativaL. ‘Victory’) seedlings grown in sand culture and treated 12 h at 1 × 10−4M with these chloracetamides. The herbicides were also tested in a cell-free protein synthesizing system containing polyribosomes purified from oat root cytoplasm. These herbicides had no effect on the rates of polypeptide elongation nor on the synthesis of specific polypeptides when herbicides (1 × 10−4M) were added directly to the system. Polypeptide formation was inhibited 89% when 1 × 10−4M cycloheximide was added during translation. Cytoplasmic polyribosomes were isolated from oat roots treated 12 h with 1 × 10−4M herbicide. Translation rates and products were not altered when these polyribosomes were added to the in vitro system. Protein synthesis is inhibited when tested in an in vivo system; however, the inhibition does not occur during the translation of mRNA into protein.



Author(s):  
Stephen Weber-Hall ◽  
Deborah Phippard ◽  
Christina Niemeyer ◽  
Trevor Dale


1970 ◽  
Vol 116 (3) ◽  
pp. 349-355 ◽  
Author(s):  
R. F. Peters ◽  
M. C. Richardson ◽  
Margaret Small ◽  
A. M. White

1. The powerful anti-inflammatory glucocorticoid triamcinolone acetonide, administered to rats at 20 and 2.5mg/kg, leads to a decrease in the incorporation in vivo of [3H]uridine and [32P]orthophosphate into hind-limb skeletal muscle. 2. At the higher dose, this decrease in the rate of incorporation of precursors into RNA precedes a decrease in the incorporating ability of muscle ribosomes, which commences about 4–5h after drug administration, but is unaccompanied by any changes in the concentration of tissue ATP or free amino acids. 3. The ribosomal dysfunction extends to polyribosomes, which can only be successfully isolated from the muscle of triamcinolone-treated animals after the addition of α-amylase to the tissue homogenate to remove glycogen. 4. The specific radioactivity of muscle protein labelled in vivo with 14C-labelled amino acids does not decrease progressively after triamcinolone administration. After 2h there is an apparent stimulation of incorporation which leads to an overall discrepancy between measurements of protein-synthetic activity made in vivo and in vitro. 5. There is a significant increase in muscle-glycogen concentration between 8 and 12h after the administration of triamcinolone acetonide (20mg/kg), although a significant decrease occurs after 4h. The fall in glycogen concentration may be due to a decrease in the rate of synthesis of protein essential for glucose uptake into the tissues. 6. As judged by (a) incorporation of 14C-labelled amino acids into protein, (b) [3H]uridine and [32P]-orthophosphate incorporation into RNA, (c) the rate of induction of tryptophan pyrrolase and (d) changes in the pool sizes of taurine and tryptophan, the responses in liver followed the same time-course as those in muscle after administration of the drug.



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