DONGYANG WANG, YI CHEN, JING HUANG, YOU ZHANG, CHONGKUI SUN, YINGQIANG SHEN^*

BIOCELL, Vol.47, No.2, pp. 329-338, 2023, DOI:10.32604/biocell.2023.023489

Abstract Glucocorticoids (GC) are widely used to counter the adverse events during cancer therapy; nonetheless, previous studies pointed out that GC may reduce the efficacy of chemotherapy on cancer cells, especially in epidermal growth factor receptor (EGFR)-targeted therapy of head and neck squamous cell carcinoma (HNSCC) remaining to be elucidated. The primary aim of the present study was to probe into the GC-induced resistance of EGFR-targeted drug afatinib and the underlying mechanism. HNSCC cell lines (HSC-3, SCC-25, SCC-9, and H-400) and the human oral keratinocyte (HOK) cell lines were assessed for GC receptor (GR) expression. The promoting tumor growth effect of… More >

MARISA L. ZALLOCCHI^*1, MARIA C. DAMASCO¹, JUAN C. CALVO^1,2, CARLOS P. LANTOS¹, LAURA B. MATKOVIC¹

BIOCELL, Vol.30, No.3, pp. 469-477, 2006, DOI:10.32604/biocell.2006.30.469

Abstract Prior to this work, we found that adrenal as well as extra-adrenal factors activate the response of renal 11ß-hydroxysteroid dehydrogenase 2 to stressful situations. These results -showing ways through which the organism hinders the pathological occupation of mineralocorticoid receptors by glucocorticoids leading to sodium retention and hypertension- prompted the present study on the nature of the above-mentioned extraadrenal factors. Serotonin was chosen because of its properties as a widely distributed neurohormone, known to interact with glucocorticoids at many sites, also exhibiting increased levels and effects under stressful situations. We studied serotonin effects on 11ß-hydroxysteroid dehydrogenase 2 activity in a cell… More >

Arman Nayebosadri¹, Julie Y. Ji^2*

Molecular & Cellular Biomechanics, Vol.13, No.1, pp. 57-85, 2016, DOI:10.3970/mcb.2016.013.069

Abstract The glucocorticoid receptor (GR) has multiple phosphorylation sites that can be activated by MAPKs, which have been previously shown to be activated in response to cyclic stretch in endothelial cells. It is possible therefore that physiological and/or pathological degree of cyclic stretch may also initiate phosphorylation-induced changes in GR subcellular localization as we previously showed with shear stress. However, little is known about the effects of cyclic stretch on glucocorticoid receptor (GR) activity in endothelial cells. We used control and lamin shRNA BAECs and subjected them to ligand (dexamethasone) treatment, physiological stretch (10% at 1 Hz), or pathological stretch (20%… More >