Enhancement of Lytic Activity by Leptin Is Independent From Lipid Rafts in Murine Primary Splenocytes
Autor: | Audrey Noacco, Marie-Chantal Farges, Aurore Collin, J. Talvas, Marie-Paule Vasson, Florence Caldefie-Chezet |
---|---|
Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
medicine.medical_specialty Leptin receptor Physiology Chemistry Leptin Clinical Biochemistry Cell Adipokine Cell Biology 3. Good health 03 medical and health sciences 030104 developmental biology 0302 clinical medicine medicine.anatomical_structure Endocrinology Lytic cycle 030220 oncology & carcinogenesis Internal medicine medicine Membrane fluidity Splenocyte Lipid raft |
Zdroj: | Journal of Cellular Physiology. 232:101-109 |
ISSN: | 0021-9541 |
DOI: | 10.1002/jcp.25394 |
Popis: | Leptin, a pleiotropic adipokine, is known as a regulator of food intake, but it is also involved in inflammation, immunity, cell proliferation, and survival. Leptin receptor is integrated inside cholesterol-rich microdomains called lipid rafts, which, if disrupted or destroyed, could lead to a perturbation of lytic mechanism. Previous studies also reported that leptin could induce membrane remodeling. In this context, we studied the effect of membrane remodeling in lytic activity modulation induced by leptin. Thus, primary mouse splenocytes were incubated with methyl-β-cyclodextrin (β-MCD), a lipid rafts disrupting agent, cholesterol, a major component of cell membranes, or ursodeoxycholic acid (UDCA), a membrane stabilizer agent for 1 h. These treatments were followed by splenocyte incubation with leptin (absence, 10 and 100 ng/ml). Unlike β-MCD or cholesterol, UDCA was able to block leptin lytic induction. This result suggests that leptin increased the lytic activity of primary spleen cells against syngenic EO771 mammary cancer cells independently from lipid rafts but may involve membrane fluidity. Furthermore, natural killer cells were shown to be involved in the splenocyte lytic activity. To our knowledge it is the first publication in primary culture that provides the link between leptin lytic modulation and membrane remodeling. J. Cell. Physiol. 232: 101-109, 2017. © 2016 Wiley Periodicals, Inc. |
Databáze: | OpenAIRE |
Externí odkaz: |