Comparison of particle-associated progesterone and oxytocin in the ovine corpus luteum
G. E. Rice, G. Jenkin, G. D. Thorburn
The subcellular distribution of progesterone and oxytocin within the ovine corpus luteum was investigated using differential and density gradient centrifugation. Progesterone and oxytocin were associated with particles which sedimented to a density of 1.049-1.054 g/ml and 1.054-1.061 g/ml respectively. Particle-associated progesterone did not, however, display physical or biochemical characteristics consistent with its storage within secretory granules. When particle-associated progesterone was incubated in HEPES buffer at 37°C, 70% of the total progesterone was recovered in the incubation medium. The remaining stable particle-associated progesterone was not affected by treatments which stimulated oxytocin release and which have been shown to cause the release of peptides and biogenic amines from secretory granules. These results suggest that particle-associated progesterone represents the intercalation of progesterone into cell membranes and they do not support the hypothesis that progesterone is stored, in a protein-bound form, in luteal secretory granules.
Journal of Endocrinology
https://doi.org/10.1677/joe.0.1080109
10.1677/joe.0.1080109
Rice, G. E., Jenkin, G., & Thorburn, G. D. (1986). Comparison of particle-associated progesterone and oxytocin in the ovine corpus luteum. Journal of Endocrinology, 108(1), 109-116. https://doi.org/10.1677/joe.0.1080109
Rice, G. E. ; Jenkin, G. ; Thorburn, G. D. / Comparison of particle-associated progesterone and oxytocin in the ovine corpus luteum. In: Journal of Endocrinology. 1986 ; Vol. 108, No. 1. pp. 109-116.
@article{323f1ae7b52a42558e3eb9824fa903cc,
title = "Comparison of particle-associated progesterone and oxytocin in the ovine corpus luteum",
abstract = "The subcellular distribution of progesterone and oxytocin within the ovine corpus luteum was investigated using differential and density gradient centrifugation. Progesterone and oxytocin were associated with particles which sedimented to a density of 1.049-1.054 g/ml and 1.054-1.061 g/ml respectively. Particle-associated progesterone did not, however, display physical or biochemical characteristics consistent with its storage within secretory granules. When particle-associated progesterone was incubated in HEPES buffer at 37°C, 70% of the total progesterone was recovered in the incubation medium. The remaining stable particle-associated progesterone was not affected by treatments which stimulated oxytocin release and which have been shown to cause the release of peptides and biogenic amines from secretory granules. These results suggest that particle-associated progesterone represents the intercalation of progesterone into cell membranes and they do not support the hypothesis that progesterone is stored, in a protein-bound form, in luteal secretory granules.",
author = "Rice, {G. E.} and G. Jenkin and Thorburn, {G. D.}",
doi = "10.1677/joe.0.1080109",
journal = "Journal of Endocrinology",
publisher = "Bioscientifica",
Rice, GE, Jenkin, G & Thorburn, GD 1986, 'Comparison of particle-associated progesterone and oxytocin in the ovine corpus luteum', Journal of Endocrinology, vol. 108, no. 1, pp. 109-116. https://doi.org/10.1677/joe.0.1080109
Comparison of particle-associated progesterone and oxytocin in the ovine corpus luteum. / Rice, G. E.; Jenkin, G.; Thorburn, G. D.
In: Journal of Endocrinology, Vol. 108, No. 1, 01.01.1986, p. 109-116.
T1 - Comparison of particle-associated progesterone and oxytocin in the ovine corpus luteum
AU - Rice, G. E.
AU - Jenkin, G.
AU - Thorburn, G. D.
N2 - The subcellular distribution of progesterone and oxytocin within the ovine corpus luteum was investigated using differential and density gradient centrifugation. Progesterone and oxytocin were associated with particles which sedimented to a density of 1.049-1.054 g/ml and 1.054-1.061 g/ml respectively. Particle-associated progesterone did not, however, display physical or biochemical characteristics consistent with its storage within secretory granules. When particle-associated progesterone was incubated in HEPES buffer at 37°C, 70% of the total progesterone was recovered in the incubation medium. The remaining stable particle-associated progesterone was not affected by treatments which stimulated oxytocin release and which have been shown to cause the release of peptides and biogenic amines from secretory granules. These results suggest that particle-associated progesterone represents the intercalation of progesterone into cell membranes and they do not support the hypothesis that progesterone is stored, in a protein-bound form, in luteal secretory granules.
AB - The subcellular distribution of progesterone and oxytocin within the ovine corpus luteum was investigated using differential and density gradient centrifugation. Progesterone and oxytocin were associated with particles which sedimented to a density of 1.049-1.054 g/ml and 1.054-1.061 g/ml respectively. Particle-associated progesterone did not, however, display physical or biochemical characteristics consistent with its storage within secretory granules. When particle-associated progesterone was incubated in HEPES buffer at 37°C, 70% of the total progesterone was recovered in the incubation medium. The remaining stable particle-associated progesterone was not affected by treatments which stimulated oxytocin release and which have been shown to cause the release of peptides and biogenic amines from secretory granules. These results suggest that particle-associated progesterone represents the intercalation of progesterone into cell membranes and they do not support the hypothesis that progesterone is stored, in a protein-bound form, in luteal secretory granules.
U2 - 10.1677/joe.0.1080109
DO - 10.1677/joe.0.1080109
JO - Journal of Endocrinology
JF - Journal of Endocrinology
Rice GE, Jenkin G, Thorburn GD. Comparison of particle-associated progesterone and oxytocin in the ovine corpus luteum. Journal of Endocrinology. 1986 Jan 1;108(1):109-116. https://doi.org/10.1677/joe.0.1080109