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April 1, 1976Journal of Biological ChemistryOpen Access

Evidence for a phospholipid requirement in the specific binding of glucocorticoids to receptors of fibroblasts and thymic lymphocytes.

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Authors

HSHenri SchulteMedizinische Hochschule HannoverCNCarl J. NielsenUnited States Army Medical Research and Development CommandJSJulianne J. SandoCarter Center

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Implication

In vitro experimental study demonstrates that phospholipase digestion impairs glucocorticoid receptor binding in rodent cells, suggesting phospholipids are essential for receptor function.

Key Points

  • To determine whether phospholipids are structurally necessary for the specific binding of glucocorticoids to their soluble receptors.
  • Treated soluble glucocorticoid receptor preparations from mouse fibroblasts and rat thymic lymphocytes with boiled phospholipase A from bee and snake venoms as well as phospholipase C.
  • Tested the effects of calcium dependence, phospholipid addition, competitive inhibitors, and lysophosphatide exposure to evaluate direct digestion versus detergent-induced inactivation.
  • Phospholipase A drastically reduced specific steroid binding capacity at low concentrations in a calcium-dependent manner, which was blocked by exogenous phospholipid or competitive inhibitors.
  • Digestion with phospholipase C also inactivated steroid binding, and assays with lysophosphatide ruled out a mechanism caused solely by detergent byproducts.

Cite This Study

Schulte et al. (1976) studied this question.

synapsesocial.com/papers/6a905da2039ece43b30d4847https://doi.org/10.1016/s0021-9258(17)33584-6
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