Lipid interactions and membrane modification in phospholipase C treated erythrocyte membranes.

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Phospholipase A 2 modification of lipid-protein interactions of normal O,Rh(D) positive erythrocyte membranes increased the fluorescence intensity of the membrane bound probe, 1-anilinonaphthalenesulfonate (ANS) and increased the N[14 C]-ethyl maleimide ([14 C]-NEM) labeling of sulfhydryl groups in two proteins of molecular weight >, In marked contrast, phospholipase Cited by: lipid has been investigated.

Purified phospholipase C of Bacillus cereus was utilized in these studies. The rate and extent of digestion of E. coli phospholipids was independent of whether the lipid was associated with membrane protein or extracted from membranes and sonically dispersed.

This chapter discusses the level of ATPase activities in human erythrocyte membranes treated with various highly purified phospholipases and reactivation of the ATPases after delipidation by treatment with B.

cereus phospholipase C.

Details Lipid interactions and membrane modification in phospholipase C treated erythrocyte membranes. EPUB

It also discusses the lipid requirement of the (Na + K)-ATPase present in other membrane species, namel,y a microsomal preparation of the outer medulla Cited by: 2. The effects of temperature and of the action of a purified phospholipase C enzyme preparation on human red blood cell membranes has been investigated by chemical analyses, circular dichroism, and.

Phospholipase C is an interesting candidate enzyme as it can directly hydrolyze PIP 2, thereby reducing the concentration in the plasma membrane, and it is activated in a number of signaling pathways. We find that the reduction in cytoskeleton-membrane adhesion, caused by chlorpromazine, is prevented by U, an inhibitor of by: Plasma membrane composition was modified by phospholipase A2, phospholipase C and phospholipase D treatment and subsequent incorporation of various phospholipids.

Phospholipase. Effect of structural modification of membrane proteins on lipid-protein interactions in the human erythrocyte membranes. Bulletin of Experimental Biology and Medicine(5), DOI: /BF Simone Gordon, G.B.

Ralston. Abstract. The increased knowledge of the properties of membrane lipids (Ansell et al., ) and of lipid-protein interactions (Singer, ; Lenaz,; Vanderkooi, G., ) allows a better understanding of the role of lipids in membrane structure and heless, a unifying picture of such a role is lacking, and it is often tacitly assumed that lipids have different roles.

Abstract. The boundary of all cells is delineated Lipid interactions and membrane modification in phospholipase C treated erythrocyte membranes. book a thin membrane which separates the protoplasm from its environment.

The existence of this membrane was first suggested by de Vries (), Pfeffer () and Overton (), who demonstrated that plant cells respond osmotically to variations in external osmolarity. However, the physical reality of the cell membrane remained controversial.

Amongst the tested membranes (i.e., mitochondrial, erythrocytes and HT cell membranes), the least hydrolysis of HT cell membrane by RVVA-PLA 2-I can again be explained on the basis that it is not the overall quantity of PC in a membrane but either the availability of PC in a PLA 2-sensitive membrane and/or, physicochemical properties of a.

Simpkins H, Panko E, Tay S. Structural changes in the phospholipid regions of the axonal membrane produced by phospholipase C action. Biochemistry. Oct 12; 10 (21)– Süss R, Blobel G, Pitot HC.

Rat liver and hepatoma polysome-membrane interaction in vitro. Biochem Biophys Res Commun. May 3; 23 (3)–   This investigation examines oxidation conditions under which hemoglobin extracts membrane phospholipid from erythrocytes and model membranes.

In erythrocytes made echinocytic with exogenous phospholipid, addition of hemoglobin oxidized with hydrogen peroxide (H2O2) or Vitamin C (conditions that result in the formation of significant quantities of choleglobin), but not ferricyanide.

Using other probes (e.g., cholera toxin B subunit conjugates, antibodies or treatment with PlcHR2, a phospholipase C/SMase from Pseudomonas aeruginosa) and techniques (e.g., SDS-digested freeze.

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identify new lipid membrane deformation proteins, we applied liposome-based microscopic screeni ng, using unbiased-darkfield mi-croscopy. Using this method, we identified phospholipase C β1(PLCβ1) as a new candidate.

PLCβ1 is well characterized as an enzyme cata-lyzing the hydrolysis of phosphatidy linositol-4,5-bisphosphate (PIP 2).

not at 0#{}C,indicating that the membrane integration de-pended on membrane mobility or the state of its compo-nents. Serum albumin or low-density lipoproteins (LDL) blocked the uptake whereas ovalbumin or gelatin did not, suggesting that the uptake involved the interaction of lipid groups in DAF with the cell lipid bilayer.

In an earlier study,6 phospholipase C treatment of red blood cell membranes was shown not to affect significantly the CD spectrum of the protein portion of the membrane.

In the present experiments, this work has been confirmed and extended in several important respects. In the first place, a more highly purified phospholipase C preparation8 was.

Peripheral proteins covalently attached to a membrane lipid, such as through a phosphatidylinositol-glycan anchor (see Fig. ), are released by phospholipase C or D. Integral proteins can be extracted with detergents, which disrupt the hydrophobic interactions with the lipid bilayer, forming micelles with individual nrotein molecules.

The effects of pH, trypsin, and phospholipase C on the topographic distribution of acidic anionic residues on human erythrocytes was investigated using colloidal iron hydroxide labeling of mounted.

Low MG, Finean JB. The action of phosphatidylinositol-specific phospholipases C on membranes. Biochem J. Jan 15; (1)– [PMC free article] Low MG, Finean JB. Modification of erythrocyte membranes by a purified phosphatidylinositol-specific phospholipase C (Staphylococcus aureus). Biochem J.

Feb 15; (2)– tional equilibrium because of a lack of de novo lipid synthesis (10) and membrane traffic. Furthermore, the erythrocyte membrane is commonly considered as a model of mammalian cell membranes, and therefore, the information obtained should be of more general relevance.

The results show that there is a highly significant agreement. The erythrocyte membrane is probably one of the most widely studied biological membranes and has served in many respects as a stimulating model (Ref.

The total lipid content of the erythrocyte constitutes about 40% of its dry weight, and in molecular ratios. The two cell types are fused by treatment with Sendai virus to form a hybrid cell 3. Immediately after fusion, the mouse and human proteins are segregated 4.

After 40 min at 37 C, the red and green markers have fully intermixed. Sabeeha S. Merchant, John D. Helmann, in Advances in Microbial Physiology, Adaptation and Acclimation by Membrane Phospholipid Remodeling in Bacteria. Membrane phospholipids are responsible for a large fraction of the phosphorus content of both prokaryotic and eukaryotic cells.

Heterotrophic and phototrophic microorganisms face P-deficient growth conditions in unfertilized soils. Experiments with planar phospholipid membranes showed a direct interaction between Bcl-xL and ceramide channels. 36 After forming a ceramide channel in the membrane and achieving a stable conductance, Bcl-xL was added, resulting in complete loss of the membrane conductance (Fig.

35(a)).The decrease in conductance did not take place in one step but rather many small changes. The composition and condition of membrane lipids, the morphology of erythrocytes, and hemoglobin distribution were explored with the help of laser interference microscopy (LIM) and Raman spectroscopy.

It is shown that patients with cardiovascular diseases (CVD) have significant changes in the composition of their phospholipids and the fatty acids of membrane lipids.

Although most drugs bind to proteins and regulate their activity, some drugs act through a new therapeutic approach called membrane-lipid therapy and bind to lipids, thus modulating the structure of membranes.

Most cellular functions are highly dependent on the lipid environment because they are controlled by proteins in or around membranes. The most common membrane-bound form of this enzyme is covalently bound at its carboxyl terminal to phosphatidylinositol. This acetylcholine esterase can be released from the membrane by treatment with phosphatidylinositol-specific phospholipase C.

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The phospholipid serves as a hydrophobic tail to anchor the protein to the membrane. Cell membranes are crowded and complex environments. To investigate the effect of protein-lipid interactions on dynamic organization in mammalian cell membranes, we have performed coarse-grained molecular dynamics simulations containing > copies of an inwardly rectifying potassium (Kir) channel which forms specific interactions with the regulatory lipid phosphatidylinositol 4,5.

Modulation of erythrocyte Membrane proteins by membrane cholesterol and lipid fluidity. Biochemis –5. Boyle, The cytoskeleton of the red blood cell. Decreased iodination of the red cell surface following phospholipase C treatment (BBA ).

Biochimica et Biophysica Acta Based on the property of membrane lipids to be present in three different phases, the gel phase, the liquid-ordered phase (L o), and the liquid crystalline phase (L d), it was proposed that lipid-lipid interactions are required and sufficient for microdomain formation.

Membranes enriched in cholesterol, glycosphingolipids, and phospholipids. Membrane lipids participate in dynamic interactions that facilitate changes in their relative position in membranes, membrane thickness, surface packing, lateral and rotational mobility, and other properties. Some membrane-bound enzymes require specific lipid.

Nonmediated flip-flop of phospholipid analogues in the erythrocyte membrane as probed by palmitoylcarnitine: Basic properties and influence of membrane modification. The Journal of Membrane Biology(2), DOI: /BF B. Deuticke, U. Henseleit, C.W.M. Haest, K.B. Heller, T.M.A.R. Dubbelman. Enhancement of.

Secretory phospholipase A 2 (sPL A 2) catalyzes the hydrolysis of enzyme is sensitive to membrane structure, and its activity has been shown to increase in the presence of liquid-crystalline/gel (L α /L β) lipid this work, we explore whether lipid domains can also direct the activity of the enzyme by inducing hydrolysis of certain lipid .