PubMed · 8235646
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J Travis. 1993-11-19. Cell biologists explore 'tiny caves'.. https://doi.org/10.1126/science.8235646
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Caveolin is a 22-kDa membrane protein found associated with a coat material decorating the inner membrane surface of caveolae. A remarkable feature of this protein is its ability to migrate from caveolae directly to the endoplasmic reticulum (ER) when membrane cholesterol is oxidized. We now present evidence caveolin is involved in transporting newly synthesized cholesterol from the ER directly to caveolae. MA104 cells and normal human fibroblasts transported new cholesterol to caveolae with a half-time of approximately 10 min. The cholesterol then rapidly flowed from caveolae to non-caveolae membrane. Cholesterol moved out of caveolae even when the supply of fresh cholesterol from the ER was interrupted. Treatment of cells with 10 microg/ml progesterone blocked cholesterol movement from ER to caveolae. Simultaneously, caveolin accumulated in the lumen of the ER, suggesting cholesterol transport is linked to caveolin movement. Caveolae fractions from cells expressing caveolin were enriched in cholesterol 3-4-fold, while the same fractions from cells lacking caveolin were not enriched. Cholesterol transport to the cell surface was nearly 4 times more rapid in cells expressing caveolin than in matched cells lacking caveolin.
The intracellular mechanisms that regulate the function of human neutrophils are not well understood. Receptor-initiated signaling events result in the production of several second messengers (e.g., Ca2+, diacylglycerol, phosphatidic acid, and arachidonic acid) with the potential to activate members of the protein kinase C (PKC) family of signaling enzymes. The mixture of second messenger signaling molecules produced usually varies, depending on the particular receptor engaged. Previous work suggests that PKC has complex regulatory effects on neutrophil function. This may be due to the presence of multiple isoforms of the enzyme family, responding differentially to the second messengers produced. In studies to identify the PKC isoforms present in human neutrophils, we discovered the presence of the PKC isoform delta in these cells. Like other previously identified isoforms (alpha, beta I, beta II, and zeta), delta is a cytosolic enzyme in unstimulated neutrophils and partially translocates to membrane-containing fractions in cells stimulated by either the PKC activator PMA or the chemoattractant FMLP. Partial purification of cytosolic PKC gave two peaks of activity. The beta isoforms predominated in peak I, while the delta isoform predominated in peak II. The identification of delta indicates that neutrophils contain at least one member of the Ca(2+)-independent, diacylglycerol-dependent subfamily of PKC isoforms. Thus, this isoform may participate in Ca(2+)-independent, but diacylglycerol-dependent signaling events in these cells.