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Biomedical subjects

S J Kennedy

Publications and source records attributed to S J Kennedy.

25 records · Page 2Linked to original sources
PubMed1981

Effect of bromocriptine, somatostatin, and oestradiol-17 beta on hormone secretion and ultrastructure of human pituitary tumours in vitro.

The effect of bromocriptine and somatostatin on hormone secretion and the ultrastructure of human pituitary adenomas was studied in vitro. Prolactin secretion was inhibited by bromocriptine in 3 out of 10 prolactin-secreting tumours and in explants from 2 normal pituitaries. GH secretion was reduced by bromocriptine in 4 out of 6 GH-secreting adenomas but was not affected by the drug in the incubations of normal pituitaries. Somatostatin inhibited GH secretion in 2 out of 5 pituitary adenomas and the effect was comparable with that of bromocriptine. Incubation of prolactin-secreting adenomas with oestradiol for as long as 24 days produced no change in hormone secretion. Examination of tumour explants by electron microscopy showed that somatostatin and bromocriptine produced accumulation of secretion granules but no changes in the secretory organelles. Long term bromocriptine treatment of "nude" athymic mice bearing xenografts of human pituitary adenomas suppressed hormone secretion and produced some increase in secretion granules but there were no morphological changes in the secretory organelles or other vital structures of the adenoma cells.

Adenoma↗
PubMed1979

Ultrastructure of normal monkey liver.

The normal ultrastructure of the liver of rhesus and cynomolgus monkeys is described. A classification of type A and B periportal hepatocytes is introduced together with a discussion of the high incidence of mitochondrial abnormalities. It is suggested that the rhesus monkey is more suitable as an experimental model than the cynomolgus since its liver ultrastructure is less variable.

Animals↗
PubMed1978

Structures of membrane proteins.

The possible conformations of integral membrane proteins are restricted by the nature of their environment. In order to satisfy the requirement of maximum hydrogen bonding, those portions of the polypeptide chain which are in contact with lipid hydrocarbon must be organized into regions of regular secondary structure. As possible models of the intramembranous regions of integral membrane proteins, three types of regular structures are discussed. Two, the alpha helix and the beta-pleated sheet, are regularly occurring structural features of soluble proteins. The third is a newly proposed class of conformations called beta helices. These helices have unique features which make them particularly well-suited to the lipid bilayer environment. The central segment of the membrane-spanning protein glycophorin can be arranged into a beta helix with a hydrophobic exterior and a polar interior containing charged amino-acid side chains. Such structures could function as transmembrane ion channels. A model of the activation process based on a hypothetical equilibrium between alpha and beta helical forms of a transmembrane protein is presented. The model can accurately reproduce the kinetics and voltage dependence of the channels in nerve.

Glycophorins↗
PubMed1977

Synthetic peptides form ion channels in artificial lipid bilayer membranes.

Ion permeability of cell membranes is considered to be mediated by ion channels. The synthesis and testing of four peptides having the sequence (Leu-Ser-Leu-Gly)n and expected to form beta126,6-helical ion channels in lipid bilayer membranes is reported. The two peptides capable of forming helices four turns in length have been demonstrated to form ion channels in an artificial lipid bilayer membrane system. The ion selectivity of the channels is consistent with the predicted beta12-helical model in which ions traversing the channel are coordinated by serine hydroxyl groups arrayed in the interior of the channel.

Amino Acid Sequence↗