Sertoli cells isolation

Allan CM, Garcia A, Spaliviero J, et al. Complete Sertoli cell proliferation induced by follicle-stimulating hormone (FSH) independently of luteinizing hormone activity evidence from genetic models of isolated FSH action. Endocrinology. 2004 145 1587-1593. 

Figure 2 depicts the current concept of the mode of action of FSH on granulosa or Sertoli cells. The protein domain of the FSH molecule binds to specific FSH receptors in plasma membrane, while the carbohydrate moieties of FSH are believed to interact with membrane components either within or adjacent to the receptor molecule. Isolation and characterization of the FSH receptors will contribute to elucidating the binding site and the role of the carbohydrate moieties in the transduction of the hormonal signal. The binding of FSH to the receptors is followed by the activation of adenyl cyclase resulting in the accumulation of cAMP. 

Sievertsson, H., Fryklund, L., Uthne, K., Hall, K., and Westermark, B., Isolation and chemistry of human somatomedins A and B. Ado. Metah. Disord. 8, 47-60 (1975). Skinner, M. K., and Griswold, M. D., Multiplication stimulating activity (MSA) can substitute for insulin to stimulate the secretion of testicular transferrin by cultured Sertoli cells. Cell Biol. Int. Bep. 7, 441-446 (1983). 

Studies of Na+ in cellular systems have been performed on cells such as superfused isolated rat cardiomyocytes, Methanobacterium thermoauto-trophicum, porcine vascular endothelial cells, the halotolerant bacterium Brevibacterium sp., Escherichia coli, murine TM3 Ley dig and TM4 Sertoli cell lines, and mouse 3T3 fibroblasts. These experiments have been employed to determine the NMR visibility of Na% its intracellular concentration, membrane transport properties and dynamics and its ionic mobility inside the cells, NMR studies have contributed to the study of Na/K/ ATPase. 

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