[Studies on saponins of rhizomes of Panax zingiberensis Wu et Feng].
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Ginsenosides↗
Biomedical subjects
C R Yang
Publications and source records attributed to C R Yang.
The biosynthesis of p-tyramine, m-tyramine, and beta-phenylethylamine by rat striatal slices.
Slices of striatal tissue obtained from saline-injected rats were incubated with 3H-phenylalanine in the presence of pargyline. This resulted in the formation of 3H-m-tyramine, 3H-p-tyramine, and 3H-phenylethylamine. Pretreatment of the rats with alpha-methyl-p-tyrosine reduced the formation of 3H-m-tyramine and 3H-p-tyramine, but enhanced the formation of 3H-phenylethylamine. After incubation of striatal tissue obtained from saline-injected rats with 3H-ptyrosine, only 3H-p-tyramine was produced. In this case, alpha-methyl-p-tyrosine pretreatment enhanced 3H-p-tyramine formation. Striatal slices incubated with 3H-m-tyramine or 3H-p-tyramine did not yield any significant quantity of 3H-phenylethylamine; nor was 14C-phenylethylamine converted to 14C-m-tyramine or 14C-p-tyramine. Pretreatment of the rats with the monoamine oxidase inhibitor pargyline did not appreciably affect these findings. After incubation with 3H-dopamine very small quantities of 3H-m-tyramine and 3H-p-tyramine were formed, the ratio between them being 7:1. It is concluded that the major biosynthetic route for m-tyramine formation in the rat striatum is by hydroxylation of phenylalanine, probably by tyrosine hydroxylase to m-tyrosine, followed by decarboxylation, probably by L-aromatic amino acid decarboxylase, to m-tyramine. para-Tyramine is formed by decarboxylation of p-tyrosine, and phenylethylamine similarly by decarboxylation of phenylalanine.
Animals↗
Activation of the chick oviduct progesterone receptor by heparin in the presence or absence of hormone.
Activation (transformation) of the chick oviduct progesterone receptor was found to be induced at 0 degrees C by heparin free in solution as well as by chromatography on a column of heparin linked to acrylamide/agarose. The transformed molecule displayed properties of the activated form of [3H]progesterone-receptor complex obtained by heat treatment or by high ionic strength: smaller size (s20,w = 3.9 S, Stokes radius = 5.2 nm), lower rate of dissociation (t 1/2 approx. 50 h at 0 degrees C compared with approx. 20 h for the 'native' form) and increased binding to phosphocellulose. In all cases, molybdate was an effective inhibitor of transformation and stabilized a large 'native' form (s20,w = 7.9 S, Stokes radius = 7.6 nm). Transformation by neither KCl nor heparin depended on the presence of ligand bound to the receptor, and the properties of the receptor molecule produced by treatment of ligand-free receptor with high ionic strength or with heparin were identical with those of the activated progesterone-receptor complex, demonstrating that receptor activation can be obtained experimentally in the absence of hormone. Our data are compatible with a model in which activation implies separation of the 4 S units, which compose the approx. 8 S 'native' form.
Animals↗
Progesterone receptor from chick oviduct: purification of molybdate-stabilized form and preliminary characterization.
A molydate-stabilized, 'non-activated' form of the progesterone receptor from the cytosol of oestrogen-stimulated chick oviduct has been purified to homogeneity by a three-step procedure. The first step, affinity chromatography using a N-(12-amino-dodecyl)-3-oxo-4-androsten-17 beta-carboxamide-substituted Sepharose gel, purified the receptor 1500-2700-fold with approximately equal to 50% recovery. In the second step, ion-exchange chromatography through a DEAE-cellulose column, progesterone receptor was eluted as a single peak at 0.1 M KCl. Purification after this step was greater than 6700-fold. The third step was filtration through Ultrogel AcA 34, resulting in overall purification approximately equal to 7400-fold with overall recovery approximately equal to 25% of pure receptor on the basis of 1 binding site/molecule of Mr 85000. The purified molybdate-stabilized receptor had a sedimentation coefficient approximately equal to 7.9S +/- 0.1 (n = 4) in 0.15 M or 0.4 M KCl containing sucrose 5-20% gradient and approximately equal to 8.9S +/- 0.2 (n = 6) in 0.15 M KCl containing glycerol 10-35% gradient, and its Stokes radius was 7.05 +/- 0.10 nm (n = 3) (calculated Mr between 240000 and 280000). Binding specificity of the purified receptor was the same as that found in crude cytosol. SDS-PAGE revealed a single band migrating as a polypeptide of Mr approximately equal to 85000 +/- 2300 (n = 9). PAGE under non-denaturing conditions at total acrylamide concentrations 5%, 7% and 9% showed a single [3H]ORG 2058-protein band (ORG 2058 is a high-affinity analogue more suitable than progesterone for electrophoretic studies). The data suggest that the high molecular weight molybdate-stabilized progesterone receptor purified from oestrogen-primed chick oviduct is composed of only approximately equal to 85000-Mr polypeptide chains.
Animals↗
Antibodies against progesterone receptor from chick oviduct. Cross-reactivity with mammalian progesterone receptors.
The highly purified, molybdate-stabilized '8-9-S' form of the chick oviduct progesterone receptor complexed with [3H]progesterone (Specific activity approximately equal to 10-12 nmol bound steroid/mg protein) was prepared according to the three-step method [Renoir et al. (1982) Eur. J. Biochem. 127,71-79] and 50-90 micrograms samples were injected into a goat and a rabbit. Specific antibodies were observed as early as 2 weeks following the first booster injection and increased considerably 12 weeks later after further booster injections. Results were similar in the two animals, with higher titers observed in the goat. Antibodies cross-reacted with the 'transformed' 4-S form of the chick oviduct progesterone receptor. They also cross-reacted with molybdate-stabilized 8-9-S progesterone receptors of mammalian species (obtained from MCF-7 human breast cancer cells and from rabbit and mouse uteri), suggesting some evolutionary conservation of steroid hormone receptors. No cross-reaction was observed with chick oviduct oestradiol receptor and with chick plasma transcortin (a non-receptor progesterone-binding protein).
Animals↗