IN VITRO EVIDENCE FOR A PROGESTERONE AND CORTICOSTEROID BINDING PROTEIN IN THE HUMAN UTERUS

1974 ◽  
Vol 75 (3) ◽  
pp. 579-583 ◽  
Author(s):  
J. L. McGuire ◽  
C. D. Bariso ◽  
B. S. Fuller
Keyword(s):  
Guinea Pig ◽  
Medroxyprogesterone Acetate ◽  
Binding Protein ◽  
Supernatant Fraction ◽  
Human Uterus ◽  
Macromolecular Component

ABSTRACT When 3H-progesterone was incubated with the 273 000 g supernatant fraction from human uteri, labelled steroid was bound to a macromolecular component. Concomitant incubation with unlabelled corticosteroids, progesterone, testosterone and oestradiol-17β depressed binding of 3H-progesterone, whereas cholesterol and the synthetic progestins chlormadinone and medroxyprogesterone acetate did not competitively inhibit 3H-progesterone binding. These findings are consistent with the existence of a transcortin-like progesterone binder in uteri of lower species such as the rat, guinea pig and rabbit.

MYOMETRIAL RESPONSES TO THE MENSTRUAL PLAIN-MUSCLE STIMULANT

1959 ◽  
Vol 19 (2) ◽  
pp. 150-157 ◽  
Author(s):  
V. R. PICKLES
Keyword(s):  
Guinea Pig ◽  
Active Material ◽  
Menstrual Period ◽  
Human Myometrium ◽  
Human Uterus ◽  
Normal Menstruation ◽  
Menstrual Fluid

SUMMARY The guinea-pig uterus and strips of human myometrium are stimulated in vitro by ether extracts of menstrual fluid; the guinea-pig uterus is also stimulated in vivo by intravenous or intracardiac injections of the same extracts. The amount of the active material recovered from menstrual fluid probably varies from subject to subject, and in one instance was shown to decrease steadily from the beginning to the end of the menstrual period. The uterine responses in vitro take several forms, all excitatory; they are compared with the contractions of the human uterus in vivo during normal menstruation and dysmenorrhoea.

scholarly journals The influence of environmental agents on prostaglandin biosynthesis and metabolism in the lung. Inhibition of lung 15-hydroxyprostaglandin dehydrogenase by exposure of guinea pigs to 100 per cent oxygen at atmospheric pressure

1975 ◽  
Vol 146 (3) ◽  
pp. 549-556 ◽  
Author(s):  
D G Parkes ◽  
T E Eling
Keyword(s):  
Guinea Pig ◽  
Atmospheric Pressure ◽  
Guinea Pigs ◽  
Supernatant Fraction ◽  
Strong Absorption Band ◽  
Prostaglandin Dehydrogenase ◽  
Environmental Agents ◽  
Contrast Exposure ◽  
Dehydrogenase System

Enzymes in the 100 000g supernatant fraction of guinea-pig lungs, in the presence of NAD-+, converted PGF-2 α (prostaglanding F-2 α) into a less-polar compound. The u.v. spectrum of this metabolite showed a strong absorption band at 230 nm, which is characteristic of a carbonyl group in conjugation with a double bond. Reduction of this metabolite with NaBH4 resulted in a compound that behaved like PGF2 α on t.l.c. and g.l.c. From this evidence we concluded that PGF2α is metabolized in vitro to 15-oxo-PGF2 α by the NAD-+-dependent prostaglandin dehydrogenase system of guinea-pig lung. The effect of exposure of the animal to SO-2 and O2 on the rate of prostaglanding biosynthesis and catabolism by lung fractions in vitro was studied. Exposure of guinea pigs to 500 p.m. of SO2 for 5h or to 50p.p.m for 9 days (6h/day) did not alter the production or degradation of prostaglandings by lung fractions in vitro. In contrast, exposure of guinea pigs to 100%O2 for 48 h inhibited the rate of prostaglanding metabolism in vitro by 60-70% without significantly altering the rate of biosynthesis by lung fractions. Inhibition of prostaglandin dehydrogenase activity in vitro by lung fractions after exposure of the animal to O2 was dependent on the duration of exposure. Gluthathione S-aryltransferase and catechol O-methyltransferase activites of guinea-pig lung 100 000g supernatant were unaltered by exposure of the animal to O2. Thus it appears that inhibition of pulmonary prostaglandin dehydrogenase by exposure of the animal to O2 is not the result of a general tox;ic response. It was postulated that the inhibition of prostaglanding dehydrogenase may occur after exposure of the animal to other oxidant gases.

scholarly journals Exchange of phospholipids between brain membranes in vitro

1972 ◽  
Vol 126 (4) ◽  
pp. 823-835 ◽  
Author(s):  
E. K. Miller ◽  
R. M. C. Dawson
Keyword(s):  
Mitochondrial Fraction ◽  
Supernatant Fraction ◽  
Exchange Processes ◽  
Brain Microsomes ◽  
Phospholipid Transfer ◽  
Myelin Fraction ◽  
Macromolecular Component ◽  
The Brain ◽  
Guinea Pig Brain

1. When unlabelled mitochondria from guinea-pig brain were incubated with a 32P-labelled microsomal fraction from brain there was a transfer of phospholipid to the mitochondria, which could not be accounted for by an aggregation of microsomes and mitochondria or an exchange with microsomes contaminating the mitochondria. Under similar circumstances there was a transfer of phospholipid from 32P-labelled mitochondria to microsomes, indicating that the process was one of exchange. 2. The transfer from microsomes was greatly stimulated by a non-dialysable heat-labile macromolecular component in the brain supernatant fraction but not by the concentration of the particulate fractions. 3. Phospholipid-exchange processes occurred most readily between pH7 and 7.5 and were inhibited by the presence of myelin and on the addition of lysophosphatidylcholine. 4. The rates of transfer of individual phospholipids from brain microsomes to mitochondria were similar. 5. 32P-labelled microsomes could slowly donate phospholipid to the isolated synaptosomal (nerve-ending) fraction but the phospholipids of the myelin fraction did not exchange. 6. Subfractionation of the synaptosomal fraction after [32P]phospholipid transfer showed that the mitochondria were most actively labelled during the incubation. All of the isolated individual synaptosomal membranes were capable of acquiring phospholipid on incubation with a 32P-labelled brain supernatant fraction although a greater percentage was again exchanged by the mitochondrial fraction.

Inhibition of Human and Animal Platelet Adhesiveness to Glass Bead Columns by Adenosine, Dipyridamole, Chlorpromazine and Acetylsalicylic Acid

1976 ◽  
Vol 36 (02) ◽  
pp. 401-410 ◽  
Author(s):  
Buichi Fujttani ◽  
Toshimichi Tsuboi ◽  
Kazuko Takeno ◽  
Kouichi Yoshida ◽  
Masanao Shimizu
Keyword(s):  
Guinea Pig ◽  
Acetylsalicylic Acid ◽  
Guinea Pigs ◽  
Glass Bead ◽  
Animal Species ◽  
Inhibitory Effect ◽  
Rabbit Platelet ◽  
Platelet Adhesiveness

SummaryThe differences among human, rabbit and guinea-pig platelet adhesiveness as for inhibitions by adenosine, dipyridamole, chlorpromazine and acetylsalicylic acid are described, and the influence of measurement conditions on platelet adhesiveness is also reported. Platelet adhesiveness of human and animal species decreased with an increase of heparin concentrations and an increase of flow rate of blood passing through a glass bead column. Human and rabbit platelet adhesiveness was inhibited in vitro by adenosine, dipyridamole and chlorpromazine, but not by acetylsalicylic acid. On the other hand, guinea-pig platelet adhesiveness was inhibited by the four drugs including acetylsalicylic acid. In in vivo study, adenosine, dipyridamole and chlorpromazine inhibited platelet adhesiveness in rabbits and guinea-pigs. Acetylsalicylic acid showed the inhibitory effect in guinea-pigs, but not in rabbits.

INCORPORATION OF IODIDE INTO ORGANIC COMPOUNDS IN THE GUINEA PIG THYROID

1963 ◽  
Vol 43 (1) ◽  
pp. 110-118 ◽  
Author(s):  
R. Ekholm ◽  
T. Zelander ◽  
P.-S. Agrell
Keyword(s):  
Guinea Pig ◽  
Protein Binding ◽  
Organic Compounds ◽  
Guinea Pigs ◽  
Microsomal Fraction ◽  
Thyroid Tissue ◽  
Particulate Fraction ◽  
Supernatant Fraction ◽  
Hydrolysis Of

ABSTRACT Guinea pigs, kept on a iodine-sufficient diet, were injected with Na131I and the thyroids excised from 45 seconds to 5 days later. The thyroid tissue was homogenized and separated into a combined nuclear-mitochondrial-microsomal fraction and a supernatant fraction by centrifugation at 140 000 g for one hour. Protein bound 131iodine (PB131I) and free 131iodide were determined in the fractions and the PB131I was analysed for monoiodotyrosine (MIT), diiodotyrosine (DIT) and thyroxine after hydrolysis of PB131I. As early as only 20 minutes after the Na131I-injection almost 100% of the particulate fraction 131I was protein bound. In the supernatant fraction the protein binding was somewhat less rapid and PB131I values above 90% of total supernatant 131I were not found until 3 hours after the injection. In all experiments the total amount of PB131I was higher in the supernatant than in the corresponding particulate fraction. The ratio between supernatant PB131I and pellet PB131I was lower in experiments up to 3 minutes and from 2 to 5 days than in experiments of 6 minutes to 20 hours. Hydrolysis of PB131I yielded, even in the shortest experiments, both MIT and DIT. The DIT/MIT ratio was lower in the experiments up to 2 hours than in those of 3 hours and over.

INHIBITION OF LIPOLYTIC ACTIVITY OF SYNTHETIC β1–24 AND β1–39 CORTICOTROPHIN BY ANTI-ACTH ANTISERUM

1966 ◽  
Vol 51 (1) ◽  
pp. 88-94 ◽  
Author(s):  
A. Villanueva ◽  
S. J. H. Ashcroft ◽  
J. P. Felber
Keyword(s):  
Guinea Pig ◽  
Lipolytic Activity ◽  
Peptide Hormones ◽  
Fat Pad ◽  
Double Antibody ◽  
Epididymal Fat ◽  
Antibody Complex ◽  
Radio Immunoassay ◽  
Antigen Antibody

ABSTRACT The synthetic ACTH peptides β1–39 and β1–24 stimulated lipolysis as determined by the rat epididymal fat pad in vitro. The stimulating effect of these peptides was diminished by prior incubation of the peptides with antibodies produced by the guinea-pig against ACTH. The stimulating effect of these hormones was also diminished by the double antibody system used in the radio-immunoassay of ACTH and other peptide hormones, in which incubation with antiserum is followed by precipitation of the antigen-antibody complex by rabbit anti-guinea-pig-γ-globulin.

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