Effect of retinol and retinoic acid on permeability, electrical resistance and phase transition of lipid bilayers

Stillwell, William; Ricketts, Mark; Hudson, Hilton M.; Nahmias, Steven

doi:10.1016/0005-2736(82)90376-5

Cited by 42 publications

(12 citation statements)

References 28 publications

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“…Examples of biochemical phenomena that can be affected by retinoids include membrane fusion (Ahkong et al, 1973); cytoskeletal alterations (Lehtonen et al, 1983), protein glycosylation (e.g., DeLuca, 1977), lipid acylation (Tou, 1983), activation and repression of specific genes (e.g., Chytil, 1984;Sporn and Roberts, 19841, and changes in the physical properties of membranes consequent upon partitioning of retinoids into those structures (Stillwell et al, 1982). Phenomena added here are 0, release and change of morphology by neutrophils.…”

Section: Discussionmentioning

confidence: 99%

Retinoids stimulate the release of superoxide by neutrophils and change their morphology

Badwey

Robinson

Curnutte

et al. 1986

Journal Cellular Physiology

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All-trans-retinal stimulated the release of superoxide by human and guinea pig neutrophils 63 +/- 14 SD and 53 +/- 5 SD nmol of O2-/min/10(7) cells, respectively. Superoxide release by unstimulated cells was negligible. All-trans-retinal also induced morphological changes (i.e., evaginations) in these cells. Other retinoids were effective in instigating these phenomena. The similarities of these effects to those instigated by cis-unsaturated fatty acids (Badwey, J.A., et al., 1984, J. Biol. Chem., 259:7870-7877) are discussed in light of possible mechanisms.

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Section: Discussionmentioning

confidence: 99%

Retinoids stimulate the release of superoxide by neutrophils and change their morphology

Badwey

Robinson

Curnutte

et al. 1986

Journal Cellular Physiology

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“…In this respect free holo RBP is equivalent to the hormone and PA to the carrier protein. The need for the first carrier, RBP, can be attributed to the extreme insolubility [29], the sensitivity to oxidation [30] and the potential toxicity [31,32] of retinol. Since RBP is a small protein it should be well suited for extravascular transport of retinol.…”

Section: Discussionmentioning

confidence: 99%

Factors affecting the concentration of free holo retinol‐binding protein in human plasma

Fex

Felding

1984

Eur J Clin Investigation

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The total concentrations of retinol, retinol-binding protein and prealbumin were determined in plasma from twenty healthy men and sixty patients with various inflammatory conditions. These concentrations were all strongly correlated to each other and lower in the patient group. The concentration of free (not prealbumin-bound) holo retinol-binding protein, the presumed 'active' supplier of retinol to the tissues, was calculated. It was found not to be decreased in the patient group. Of the measured total concentrations and their possible ratios in the whole material, the retinol/prealbumin ratio showed the strongest correlation to the concentration of free holo retinol-binding protein. The importance of the concentration of free holo retinol-binding protein for the vitamin A supply to the cells was supported by calculations on data from the literature showing that this concentration better than the above-mentioned total concentrations distinguished between patients with normal and abnormal dark adaptation ability.

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“…We have recently reported that compounds known to increase the liquid crystalline fraction of membranes [e.g., cis-unsaturated fatty acids (27,28), retinoids (4,5)] induce high levels of 0°release by neutrophils (17,29). Cisunsaturated fatty acids stimulate purified phosphatidylinositol-specific phospholipase C activity in vitro (30,31), and this effect has been attributed to alteration of the physical properties of the lipid substrate (30 14).…”

Section: Discussionmentioning

confidence: 99%

“…2), by functioning as glycolipid intermediates in glycosylation reactions (e.g., see ref. 3), by increasing the liquid crystalline fraction of membranes (4,5), and by acting as inhibitors of protein kinase C (e.g., see refs. [6][7][8].…”

mentioning

confidence: 99%

all-trans-Retinal stimulates superoxide release and phospholipase C activity in neutrophils without significantly blocking protein kinase C.

Lochner¹,

Badwey²,

Horn³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACTall-trans-Retinal was previously shown to stimulate high levels of superoxide release by guinea pig neutrophils. When the cells, previously labeled with [3H]inositol, are treated with all-trans-retinal, they exhibit a decrease in the levels of [3H]inositol phospholipids and an increase in the accumulation of [3H]inositol phosphates. The maximal accumulation of inositol phosphates and the optimal rate of superoxide release occurred together at -7 min after stimulation. Retinoids are known to block the effects of phorbol esters on a wide variety of cells (6,15,16). However, we have recently reported that they stimulate high levels of O2 release by neutrophils (17). The mechanism of the stimulation by retinoids is of interest since this is a situation in which retinoids mimic, rather than inhibit, a cellular effect of phorbol esters. In this paper, we report effects of all-transretinal on phospholipase C and protein kinase C of neutrophils. (10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20) Ci/mmol; 1 Ci = 37 GBq) and [y-32P]ATP (2-10 Ci/mmol) were purchased from Dupont-NEN Products. all-trans-Retinal (Type XVI), phosphatidylserine, 1,2-dioleoyl-rac-glycerol, histone (type III-S), neomycin sulfate, and inositol phospholipid standards were obtained from Sigma. Anion exchange resin AG1-X8 (formate form) (200-400 mesh) was a product of Bio-Rad. Glycophase G glass beads (CPG/200) were obtained from Pierce. Sources of all other materials used have been described elsewhere (12,17). MATERIALS AND METHODS myo-[2-3H]InositolPreparation of Neutrophils. Guinea pig peritoneal neutrophils were prepared as described (18).Superoxide Release. Superoxide release by neutrophils was measured as outlined earlier (12). Solutions of all-transretinal (10 mM) were prepared in dimethyl sulfoxide immediately prior to use (17). Stock solutions of fMet-Leu-Phe and PMA were prepared in dimethyl sulfoxide and stored at -20°C until needed. These compounds were diluted with dimethyl sulfoxide so that the final concentration of solvent in the assays was 0.25% (vol/vol) in all cases. This concentration of solvent did not itself cause the effects noted.Labeling of Cells with [3H]Inositol. Neutrophil inositol phospholipids were labeled by incubating the cells (108 cells per ml) for 2 hr at 37°C in an isotonic Hepes buffer (124 mM NaCl/5 mM KCl/10 mM Hepes, pH 7.35) containing [3H]inositol (125 ,Ci/ml). The cells were washed in a modified Hanks' Hepes buffer (124 mM NaCl/5 mM KCl/0.5 mM CaCl2/0.2 mM MgCl2/10 mM Hepes, pH 7.35/5 mM glucose), resuspended in 50 ml of this buffer at a concentration of 2 x 106 cells per ml, and equilibrated to 37°C. They were stimulated with all-trans-retinal (25 ,uM), with fMetLeu-Phe (1 ,uM), or with PMA (0.05 AM) for various times, and the reactions were terminated by rapidly pouring the cell suspensions into 500-ml flasks containing 100 ml of the modified Hanks' Hepes buffer chilled to 4°C. The cells were transferred to 50-ml centrifuge tubes and collected by centrifugation for 10 min at 4°C. Cell pellets were lysed ...

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Effect of retinol and retinoic acid on permeability, electrical resistance and phase transition of lipid bilayers

Cited by 42 publications

References 28 publications

Retinoids stimulate the release of superoxide by neutrophils and change their morphology

Retinoids stimulate the release of superoxide by neutrophils and change their morphology

Factors affecting the concentration of free holo retinol‐binding protein in human plasma

all-trans-Retinal stimulates superoxide release and phospholipase C activity in neutrophils without significantly blocking protein kinase C.

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