Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0344329 (collapse)
 28,634 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mean molecular area vs. lateral surface pressure isotherms were determined for monolayers containing cholesterol, 4-cholesten-3-one (cholestenone), or binary mixtures of the two. At all lateral surface pressures examined, cholestenone had a larger mean molecular area requirement than cholesterol. Results with the binary mixtures of cholesterol and cholestenone suggested that the sterols did not mix ideally (non additive mean molecular area) with each other in the monolayer; the observed mean molecular area for mixtures was less than would be expected based on ideal mixing. The mixed sterol monolayers also displayed a reduction in the lateral collapse pressure which appeared to be a linear function of the mole fraction of cholestenone in the monolayer, suggesting that cholesterol and cholestenone were completely miscible in the mixed monolayer. The pure cholesterol monolayer was next used to examine the cholesterol oxidase-catalyzed (Brevibacterium sp.) oxidation of cholesterol to cholestenone at different lateral surface pressures at 22 degrees C. The difference in mean molecular area requirements of cholesterol and cholestenone was directly used to convert monolayer area changes (at constant lateral surface pressure) into average reaction rates. It was observed that the average catalytic activity of cholesterol oxidase increased linearly with increased lateral surface pressure in the range of 1 to 20 mN/m. In addition, the enzyme was capable to oxidize cholesterol in monolayers with a lateral surface pressure close to the collapse pressure of cholesterol monolayers (collapse pressure 45 mN/m; oxidation was observed at 40 mN/m). The adsorption of cholesterol oxidase to an inert sterol monolayer film at low surface pressures (around 9 mN/m) was marginal, although clearly detectable at very low (0.5-4 mN/m) lateral surface pressures, suggesting that the enzyme did not penetrate deeply into the monolayer in order to reach the 3 beta-hydroxy group of cholesterol. This interpretation is further supported by the finding that a maximally compressed cholesterol monolayer (40 mN/m) was readily susceptible to enzyme-catalyzed oxidation. It is concluded that cholesterol oxidase is capable of oxidizing cholesterol in laterally expanded monolayers as well as in tightly packed monolayers, where the lateral surface pressure is close to the collapse pressure. The kinetic results suggested that the rate-limiting step in the overall process was the substrate availability per surface area (or surface concentration) at the water/lipid interface.
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PMID:Enzyme-catalyzed oxidation of cholesterol in pure monolayers at the air/water interface. 153 72

In this study we have characterized the monolayer behavior of analogues of cholesterol having different side-chain structures and their interaction with phosphatidylcholines in mixed monolayers and small unilamellar vesicles (SUVs). Two series of side-chain analogues of cholesterol were synthesized, one with an unbranched side chain (the n-series, from 3 to 7 carbons in length), and the other with a single methyl-branched side chain (the iso-series, from 5 to 10 carbons in length). The length and conformation of the sterol side chain markedly influenced both the mean molecular area of the pure sterols and their monolayer stability (i.e., collapse pressure). Shorter side chains gave smaller mean molecular areas and decreased monolayer stability. The sterols from the n-series also had smaller mean molecular areas than the corresponding sterols in the iso-series. In mixed 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC)/sterol monolayers (equimolar ratio; at 22 degrees C), all of the sterols tested decreased the monolayer stability as judged by the lower collapse pressure with sterol than without sterol. A similar trend was observed in mixed monolayers containing 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine (SOPC), except that sterols from the iso-series with a chain length of 8 or 10 carbon atoms actually stabilized the monolayer compared with the sterol-free SOPC monolayer. The ability of the sterols to condense the molecular packing of DPPC was similar with all sterols (3-5% condensation at 10 mN/m), irrespective of the length or structure of the side chain. 5-Androsten-3 beta-ol, however, which lacks the side chain, did not at all condense the monolayer packing of DPPC. With SOPC mixed monolayers, all side chain containing sterols caused a 18-20% condensation (at 10 mN/m) of monolayer packing. The condensing effect of 5-androsten-3 beta-ol on SOPC packing was again much smaller (about 10%) compared with that of the side-chain sterols. The rate of sterol oxidation by cholesterol oxidase (at 37 degrees C) in DPPC-containing SUVs increased as a function of increasing the side-chain length (iso-series). With sterols from the n-series, the same trend was seen, except that the n-C7 analogue was oxidized much slower than the n-C4, n-C5, and n-C6 analogues. With SOPC SUVs, a similar side-chain dependent oxidation pattern was observed. Our results support and extend previous knowledge about the importance of the sterol side chain in determining sterol-sterol and sterol-phospholipid interactions, both in mono- and bilayers.
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PMID:Effect of sterol side-chain structure on sterol-phosphatidylcholine interactions in monolayers and small unilamellar vesicles. 814 47

In this study we have examined the cholesterol oxidase (Streptomyces cinnamomeus) catalyzed conversion of either 5-cholesten-3 beta-ol or 5-cholesten-3-one into 4-cholesten-3-one in pure sterol or mixed phospholipid-containing monolayers at the air/buffer interface. The mean molecular area requirement of 5-cholesten-3-one in a pure monolayer was slightly smaller than the comparable area required by 5-cholesten-3 beta-ol (although the collapse pressure was markedly lower for 5-cholesten-3-one), and both sterols were about equally capable of condensing the lateral packing density of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine at a lateral surface pressure of 20 mN/m. Both sterols were converted by cholesterol oxidase to 4-cholesten-3-one, the reaction being faster with 5-cholesten-3-one as compared to 5-cholesten-3-beta-ol. When the temperature-dependency of the cholesterol oxidase catalyzed conversion of the sterols to 4-cholesten-3-one was examined, the Arrhenius activation energy was calculated to +30 kJ/mol and +27 kJ/mol for 5-cholesten-3 beta-ol and 5-cholesten-3-one, respectively, when the sterols were presented to the enzyme as pure sterol monolayers at a lateral surface pressure of 20 mN/m. With a mixed monolayer containing 40 mol% sterol and 60 mol% EPC, the corresponding activation energies were +107 kJ/mol and +96 kJ/mol for 5-cholesten-3 beta-ol and 5-cholesten-3-one, respectively. With the monolayer system used, it appeared that the over all rate-limiting step in the enzyme-catalyzed conversion of 5-en-sterols to 4-en-3-one was the desorption of the sterol molecules from the monolayer into the active site of the enzyme at the interface. This appeared to be true both with pure sterol monolayers as well as with mixed monolayers containing phosphatidylcholine.
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PMID:Oxidation/isomerization of 5-cholesten-3 beta-ol and 5-cholesten-3-one to 4-cholesten-3-one in pure sterol and mixed phospholipid-containing monolayers by cholesterol oxidase. 843 56