The phorbol ester 12-O-tetradecanoyl-phorbol-13-acetate stimulates the dephosphorylation of mitochondrial ferredoxin in cultured chick kidney cells.

Endocrinology ◽  
1993 ◽  
Vol 133 (4) ◽  
pp. 1823-1829 ◽  
Author(s):  
C Tang ◽  
S R Kain ◽  
H L Henry
Keyword(s):  
Phorbol Ester ◽  
Kidney Cells ◽  
Chick Kidney

The development of chick-embryo-lethal-orphan (CELO) virus T and V antigens in lytically infected chick kidney cells

1971 ◽  
Vol 7 (1) ◽  
pp. 59-64 ◽  
Author(s):  
Jeffrey Anderson ◽  
Kenneth J. McCormick ◽  
Wayne A. Stenback ◽  
John J. Trentin
Keyword(s):  
Chick Embryo ◽  
Kidney Cells ◽  
Celo Virus ◽  
Chick Kidney

Studies on the growth, chemotherapy and enzyme variation of Eimeria acerulina var. diminuta and E. acervulina var. mivati

Parasitology ◽  
1977 ◽  
Vol 75 (2) ◽  
pp. 165-176 ◽  
Author(s):  
M. W. Shirley ◽  
B. J. Millard ◽  
P. L. Long
Keyword(s):  
Kidney Cells ◽  
Chicken Embryos ◽  
Eimeria Acervulina ◽  
Enzyme Variation ◽  
Similarities And Differences ◽  
Chick Kidney

Eimeria acervulina var. diminuta was serially passaged 12 times in chicken embryos, but growth in cultured chick kidney cells was linmited to 2 generations of schizonts. After 7 embryo passages the sensitivities of E. acervulina var. diminuta and an embryo-adapted strain of E. acervulina var. mivati to the anticoccidial drugs amprolium, methyl parasites were sensitive to all the anticoccidials but E. acervulina var. diminuta was more sensitive to sulphaquinoxaline and amprolium. The chicken-maintained strain of E. acervulina var. diminuta was extremely sensitive to clopidol, sulphaquinoxaline and decoquinate. Electrphoretic analyses of several enzymes from E. acervulina var. diminuta revealed enzyme profiles with similarities and differences to the embryo-adapted strain of E. acervulina var. mivati.

scholarly journals Effect of oestrogen and 1,25-dihydroxycholecalciferol on 25-hydroxycholecalciferol metabolism in primary chick kidney-cell cultures

1978 ◽  
Vol 174 (1) ◽  
pp. 231-236 ◽  
Author(s):  
E Spanos ◽  
D I Barrett ◽  
K T Chong ◽  
I MacIntyre
Keyword(s):  
Vitamin D ◽  
Cell Cultures ◽  
Kidney Cell ◽  
Primary Cultures ◽  
Kidney Cells ◽  
Hydroxylase Activity ◽  
Experimental Conditions ◽  
Polar Metabolites ◽  
Chick Kidney ◽  
25 Hydroxycholecalciferol

Primary cultures of chick kidney cells convert 25-hydroxycholecalciferol into more-polar metabolites. Cells from vitamin D-deficient chicks have high 25-hydroxycholecalciferol 1 alpha-hydroxylase (1 alpha-hydroxylase) activity, but no 25-hydroxycholecalciferol 24-hydroxylase (24-hydroxylase) activity. Physiological concentrations of 1,25-dihydroxycholeclaciferol suppress 1 alpha-hydroxylase and induce 24-hydroxylase activity. The inhibition of 1 alpha-hydroxylase preceded the induction of 24-hydroxylase. In contrast, oestradiol-17 beta had no effect on the activity of either hydroxylase under a variety of experimental conditions. These results clearly demonstrate that 1,25-dihydroxycholecalciferol, but not oestrogen, acts directly on the kidney cells to regulate the metabolism of 25-hydroxycholecalciferol.

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