Substances & Homeopatic Remedies

Physalis alkekengi

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Comp Biochem Physiol B Biochem Mol Biol. 1996 Oct;115(2):267-71.   
Modulation of the pituitary and basomedial hypothalamic lysyl-aminopeptidase activities be beta-estradiol and/or an aqueous extract of Physalis alkekengi fruits.
Vessal M, Rasti M, Kooshesh F.
Department of Biochemistry, Shiraz University of Medical Sciences, Iran.

Injections of an aqueous extract of winter cherry fruits (Physalis alkekengi) to adult female cycling rats by an intraperitoneal route resulted in the diminution of the pituitary lysyl-aminopeptidase (Lys-AP) activity by 50% and that of the basomedial hypothalamus (BMH) by 45%. Administration of daily doses of 3.75, 7.5, and 15 micrograms beta-estradiol for a period of 5-8 days to such animals increased pituitary Lys-AP activity from 31% to 61.5% and that of BMH from 20% to 87%, respectively. Administration of the same doses of beta-estradiol along with a given dose of the aqueous extract for 7-8 days diminished Lys-AP inhibitory effect of the extract in both the pituitary and BMH and eventually, at the highest dose of beta-estradiol, increased the pituitary enzyme activity by 9% and that of BMH by 5%. It is concluded that Lys-AP enzymes of both tissues, being estrogen-induced proteins, are inhibited by the estrogen antagonistic principle of the winter cherry aqueous extract. It is further suggested that BMH Lys-AP activity may be used as an enzyme marker for the action of beta-estradiol in hypothalamus.

Comp Biochem Physiol C Pharmacol Toxicol Endocrinol. 1995 Oct;112(2):229-36.
Comparison of the effects of an aqueous extract of Physalis alkekengi fruits and/or various doses of 17-beta-estradiol on rat estrous cycle and uterine glucose 6-phosphate dehydrogenase activity.
Vessal M, Yazdanian M.
Department of Biochemistry, Shiraz University of Medical Sciences, Iran.

Intraperitoneal injections of an aqueous extract of winter cherry fruits (Physalis alkekengi) to adult normal cycling female rats produced 100% diestrus and diminished uterine glucose 6-P dehydrogenase activity (an estrogen-induced protein) by 52%. Daily doses of 1.88, 3.75 and 7.5 micrograms 17-beta-estradiol administered intraperitoneally to adult female rats for a period of 6-8 days prolonged proestrus or estrus and increased uterine glucose 6-P dehydrogenase activity by 11.5%, 26.9% and 82.1%, respectively. Combined intraperitoneal injections of a given dose of the aqueous extract together with the above doses of 17-beta-estradiol for 8 consecutive days shortened the time spent in diestrus proportional to the dose employed and proportionately reduced the uterine glucose 6-P dehydrogenase inhibitory power of the aqueous extract (1.88 micrograms estradiol, 33.9% inhibition; 3.75 micrograms estradiol, 27% inhibition; and 7.5 micrograms estradiol, 6.0% activation). The data obtained clearly demonstrate the presence of an estrogen antagonist in the aqueous extract of Physalis alkekengi fruits.

Pharmazie. 1986 Apr;41(4):265-8. Related Articles, Links  
[The potential antineoplastic acting constituents of Physalis alkekengi L. var franchetii Mast.]
Dornberger K.

In a continuing search for potent antineoplastic compounds in indigenous plants, a water extract of Physalis alkekengi L. var. franchetii Mast. fruits was shown to have reproducible antineoplastic activity against Ehrlich ascites carcinoma in mice. Systematic fractionation of the extract led to the isolation of citric acid as the major active principle.



Eur J Biochem. 1995 Apr 15;229(2):369-76. Related Articles, Links  
Calystegins of Physalis alkekengi var. francheti (Solanaceae). Structure determination and their glycosidase inhibitory activities.
Asano N, Kato A, Oseki K, Kizu H, Matsui K.
Faculty of Pharmaceutical Sciences, Hokuriku University, Japan.

Five calystegins were extracted from the roots of Physalis alkekengi var. francheti (Solanaceae) with hot water and purified to homogeneity by the combination of a variety of ion-exchange column chromatographies. Their structures have been determined from the 1H- and 13C-NMR spectral data, and two of the compounds were identified as calystegins A3 and B2, which have been isolated from the roots of Calystegia sepium (Convolvulaceae). Two of the remaining three were found to be 1 alpha, 3 alpha, 4 beta-trihydroxy-nor-tropane and 1 alpha, 2 alpha, 3 alpha, 4 beta-tetrahydroxy-nor-tropane and given the trivial name calystegins A5 and B3, respectively. The last calystegin was assigned as 1 alpha, 2 beta, 3 alpha, 6 alpha-tetrahydroxy-nor-tropane, which was the same as the relative configuration proposed in the literature for calystegin B1 isolated from C. sepium. However, the 13C-NMR spectral data for the compound from C. sepium differed substantially from our results. From a personal communication with the authors of the original paper on calystegins, it was clarified that the 13C-NMR chemical shifts of calystegin B1 in the original paper had been erroneous. Since their corrected 13C-NMR data of calystegin B1 and its 1H-NMR chemical shifts in the original paper are very close to our present data, we concluded that both compounds from C. sepium and P. alkekengi are identical. Calystegin B2 has been known to be a potent competitive inhibitor of almond beta-glucosidase (Ki = 1.2 microM) and coffee bean alpha-galactosidase (Ki = 0.86 microM). In this study calystegin B1 (1 alpha, 2 beta, 3 alpha, 6 alpha-tetrahydroxy-nor-tropane) proved to be a potent competitive inhibitor of almond beta-glucosidase (Ki = 1.9 microM) and bovine liver beta-galactosidase (Ki = 1.6 microM), but not an inhibitor of alpha-galactosidases. Calystegin A3 was found to be a weaker inhibitor compared to calystegin B2 but with the same inhibitory spectrum. Calystegin A5, a 2-deoxy derivative of calystegin B2, showed no activity against any glycosidases tested. Since calystegin B3, a 2-epimer of calystegin B2, also exhibited only a weak inhibitory activity, it was concluded that the equatorially oriented OH group at C2 is the essential feature for recognition and strong binding by the active site of glycosidases.(ABSTRACT TRUNCATED AT 400 WORDS)