scholarly journals Adenylate Cyclase Activity in Adrenocorticotropic Hormone-sensitive and Mutant Adrenocortical Tumor Cell Lines

1972 ◽  
Vol 247 (10) ◽  
pp. 3134-3138 ◽  
Author(s):  
Bernard P. Schimmer
Keyword(s):  
Adenylate Cyclase ◽  
Tumor Cell ◽  
Cell Lines ◽  
Adrenocorticotropic Hormone ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Adrenocortical Tumor ◽  
Tumor Cell Lines ◽  
Hormone Sensitive

Effects of benzyl alcohol on PTH receptor-adenylate cyclase system of canine kidney

1985 ◽  
Vol 248 (1) ◽  
pp. E31-E35
Author(s):  
K. J. Martin ◽  
C. L. McConkey ◽  
T. J. Stokes
Keyword(s):  
Enzyme Activity ◽  
Adenylate Cyclase ◽  
Benzyl Alcohol ◽  
Membrane Fluidity ◽  
Phospholipid Composition ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Adenylate Cyclase System ◽  
Hormone Sensitive ◽  
Canine Kidney

In many systems, perturbations of membrane architecture by changes of lipid and phospholipid composition have been shown to alter the activity of membrane-bound enzymes. The present studies examined the effect of benzyl alcohol, an agent that has been shown to increase membrane fluidity, on the parathyroid hormone (PTH)-sensitive adenylate cyclase system of canine kidney. Benzyl alcohol progressively increased basal adenylate cyclase activity up to fourfold and maximal enzyme activity in the presence of PTH, GTP, guanylimidodiphosphate, and sodium fluoride by four- to sixfold. In the presence of 20 mM Mn2+ (no Mg2+), conditions under which enzyme activity is devoid of influence of guanine nucleotides or hormones, benzyl alcohol was without effect. PTH binding was increased by 25% in the presence of benzyl alcohol without a change in binding affinity. Fluorescent polarization studies using diphenylhexatriene showed a decrease in fluorescence anisotropy in the presence of benzyl alcohol. The results suggest that benzyl alcohol facilitates the interaction of the components of the adenylate cyclase system, presumably by increasing membrane fluidity. Alterations of membrane fluidity may be a potent means of regulating hormone sensitive adenylate cyclase activity.

Adenylate cyclase activity in Y1 mouse adrenocortical tumor cells: some properties of the enzyme associated with purified plasma membrane fractions

1983 ◽  
Vol 61 (7) ◽  
pp. 547-552 ◽  
Author(s):  
Bernard P. Schimmer
Keyword(s):  
Plasma Membrane ◽  
Adenylate Cyclase ◽  
Plasma Membranes ◽  
Tumor Cell Line ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Adenylate Cyclase System ◽  
Adrenocortical Tumor ◽  
Intact Cells ◽  
Order Of Magnitude

Fractions enriched in plasma membranes were prepared from the Y1 mouse adrenocortical tumor cell line and were characterized with respect to adenylate cyclase activity. Optimal requirements of the adenylate cyclase system for guanyl nucleotides, Mg2+, ATP, and corticotropin (ACTH) were determined. The sensitivity of the adenylate cyclase system to ACTH1–24 in plasma membrane fractions was comparable with that observed in isolated intact cells. Polycations such as poly-L-arginine and histone competitively inhibited the action of ACTH1–24, supporting the view that the affinity of ACTH for the adenylate cyclase system is determined by the basic core of amino acids at residues 15–18. ACTH1–24 was at least one order of magnitude more potent than ACTH1–39 in stimulating adenylate cyclase activity in plasma membrane fractions.

scholarly journals Autocrine proliferative effect of ghrelin on leukemic HL-60 and THP-1 cells

2007 ◽  
Vol 192 (1) ◽  
pp. 199-205 ◽  
Author(s):  
Carine De Vriese ◽  
Christine Delporte
Keyword(s):  
Cell Proliferation ◽  
Adenylate Cyclase ◽  
Vasoactive Intestinal Peptide ◽  
Cell Lines ◽  
Leukemic Cell ◽  
Peptide Hormone ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Supt1 Cell ◽  
Ghrelin Receptor

Ghrelin is a 28 amino acid peptide hormone that is mainly produced by the stomach, but also by several tissues and tumors. Ghrelin is octanoylated on the Ser3, but is also detected as a des-acylated form. Only the acylated ghrelin activates the GH secretagogue receptor (GHS-R) type 1a to stimulate GH release, and regulate food intake and energy metabolism. For the first time, we report that ghrelin and des-acyl ghrelin are present in human promyelocytic HL-60, monocytic THP-1 and lymphoblastic SupT1 cell lines. The human leukemic cell lines did not express the functional GHS-R 1a, whereas they expressed GHS-R 1b, a truncated variant of the receptor. Leukemic cell proliferation was not modified by the addition of octanoylated or des-acyl ghrelins. However, THP-1 and HL-60 cell proliferations were inhibited by SB801, an antibody directed against the N-terminal octanoylated portion of ghrelin, suggesting that octanoylated ghrelin stimulates cell proliferation via an autocrine pathway involving an as yet unidentified ghrelin receptor. Both octanoylated and des-acyl ghrelins did not alter the basal adenylate cyclase activity. Treatments of THP-1 and SupT1 cells by both octanoylated and des-acyl ghrelins did not modify the adenylate cyclase activity in response to vasoactive intestinal peptide, suggesting that ghrelin is unlikely to modulate the anti-inflammatory and differentiating properties of vasoactive intestinal peptide.

scholarly journals Biological Effects of EF24, a Curcumin Derivative, Alone or Combined with Mitotane in Adrenocortical Tumor Cell Lines

Molecules ◽  
2019 ◽  
Vol 24 (12) ◽  
pp. 2202 ◽  
Author(s):  
Loris Bertazza ◽  
Susi Barollo ◽  
Maria Elena Mari ◽  
Irene Faccio ◽  
Maira Zorzan ◽  
...  
Keyword(s):  
Tumor Cell ◽  
Cell Lines ◽  
Biological Effects ◽  
Adrenocortical Tumor ◽  
Tumor Cell Lines ◽  
Adrenocortical Cancer ◽  
Reference Drug ◽  
Enhanced Solubility ◽  
H295r Cells ◽  
First Time

Background: Curcumin has numerous properties and is used in many preclinical conditions, including cancer. It has low bioavailability, while its derivative EF24 shows enhanced solubility. However, its effects have never been explored in adrenocortical tumor cell models. The efficacy of EF24 alone or combined with mitotane (reference drug for adrenocortical cancer) was evaluated in two adrenocortical tumor cell lines, SW13 and H295R. Method and Results: EF24 reduced cell viability with an IC50 (half maximal inhibitory concentration) of 6.5 ± 2.4 μM and 4.9 ± 2.8 μM for SW13 and H295R cells, respectively. Combination index (EF24 associated with mitotane) suggested an additivity effect in both cell lines. Cell cycle analysis revealed an increase in subG0/G1 phase, while motility assay showed a decrease in migratory cell capacity, and similarly, clonogenic assay indicated that EF24 could reduce colony numbers. Furthermore, Wnt/β-catenin, NF-κB, MAPK, and PI3k/Akt pathways were modulated by Western blot analysis when treating cells with EF24 alone or combined with mitotane. In addition, intracellular reactive oxygen species levels increased in both cell lines. Conclusion: This work analyzed EF24 in adrenocortical tumor cell lines for the first time. These results suggest that EF24 could potentially impact on adrenocortical tumors, laying the foundation for further research in animal models.

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