Cholesterol metabolism by purified cytochrome P-450scc is highly stimulated by octyl glucoside and stearic acid exclusively in large unilamellar phospholipid vesicles

Biochemistry ◽  
1989 ◽  
Vol 28 (21) ◽  
pp. 8397-8402 ◽  
Author(s):  
Mohan S. Dhariwal ◽  
Colin R. Jefcoate
Keyword(s):  
Stearic Acid ◽  
Cholesterol Metabolism ◽  
Phospholipid Vesicles ◽  
Octyl Glucoside

scholarly journals Role of cholesterol in the capping of surface immunoglobulin receptors on murine lymphocytes.

1983 ◽  
Vol 97 (1) ◽  
pp. 73-80 ◽  
Author(s):  
R L Hoover ◽  
E A Dawidowicz ◽  
J M Robinson ◽  
M J Karnovsky
Keyword(s):  
Stearic Acid ◽  
Surface Membrane ◽  
Protein S ◽  
Phospholipid Vesicles ◽  
Lipid Domain ◽  
Surface Immunoglobulin ◽  
Surface Immunoglobulins ◽  
Lipid Environment ◽  
Immunoglobulin Receptors

Previously, we have shown that the capping of surface immunoglobulins on murine lymphocytes can be affected by modulating the lipid environment of the surface membrane with free fatty acids. In the present study, murine lymphocytes were depleted of cholesterol by incubation with phospholipid vesicles. As the cellular cholesterol:phospholipid ratio decreased, the capping of the surface immunoglobulin was seen to decrease. This inhibition of capping could not be reversed by calcium and is not accompanied by changes in either the cytoskeletal element alpha-actinin or cellular ATP levels. Incubation of the cholesterol-depleted cells with cholesterol-containing phospholipid vesicles raised both the cholesterol:phospholipid ratio and capping levels to values close to those of untreated control cells. Remarkably, stearic acid, a saturated fatty acid, could also restore the capping levels in the cholesterol-depleted cells. On the basis of the present data and measurements of the fluorescence polarization of the probe diphenyl hexatriene, we propose a model in which the protein(s) involved in capping is located in a gel-like lipid domain, and that removal of cholesterol makes this domain less gel-like and inhibits capping. Restoration of the gel-like nature of this domain by the addition of either cholesterol or stearic acid enables the protein(s) to function normally.

A heteronuclear and homonuclear filtering strategy for studying the structure of membrane peptides in non-deuterated phospholipid vesicles

1998 ◽  
Vol 95 (2) ◽  
pp. 221-224
Author(s):  
B. T. Doan ◽  
C. Nezry ◽  
L. Rene ◽  
B. Badet ◽  
J. C. Beloeil
Keyword(s):  
Phospholipid Vesicles ◽  
Membrane Peptides

Thermally induced budding of phospholipid vesicles — a discontinuous process

1993 ◽  
Vol 3 (5) ◽  
pp. 631-645 ◽  
Author(s):  
J. Käs ◽  
E. Sackmann ◽  
R. Podgornik ◽  
S. Svetina ◽  
B. Žekš
Keyword(s):  
Phospholipid Vesicles ◽  
Thermally Induced ◽  
Discontinuous Process

Plasma Factor V Activation Is Prevented by Activated Protein C in the Presence of Phospholipid Vesicles, Not Platelets

1993 ◽  
Vol 69 (02) ◽  
pp. 124-129 ◽  
Author(s):  
Susan Solymoss ◽  
Kim Thi Phu Nguyen
Keyword(s):  
Western Blotting ◽  
Protein C ◽  
Thrombin Generation ◽  
Blood Platelets ◽  
Activated Protein C ◽  
Phospholipid Vesicles ◽  
Factor V ◽  
Two Stage ◽  
One Stage ◽  
Plasma Factor

SummaryActivated protein C (APC) is a vitamin K dependent anticoagulant which catalyzes the inactivation of factor Va and VIIIa, in a reaction modulated by phospholipid membrane surface, or blood platelets. APC prevents thrombin generation at a much lower concentration when added to recalcified plasma and phospholipid vesicles, than recalcified plasma and platelets. This observation was attributed to a platelet associated APC inhibitor. We have performed serial thrombin, factor V one stage and two stage assays and Western blotting of dilute recalcified plasma containing either phospholipid vesicles or platelets and APC. More thrombin was formed at a given APC concentration with platelets than phospholipid. One stage factor V values increased to higher levels with platelets and APC than phospholipid and APC. Two stage factor V values decreased substantially with platelets and 5 nM APC but remained unchanged with phospholipid and 5 nM APC. Western blotting of plasma factor V confirmed factor V activation in the presence of platelets and APC, but lack of factor V activation with phospholipid and APC. Inclusion of platelets or platelet membrane with phospholipid enhanced rather than inhibited APC catalyzed plasma factor V inactivation. Platelet activation further enhanced factor V activation and inactivation at any given APC concentration.Plasma thrombin generation in the presence of platelets and APC is related to ongoing factor V activation. No inhibition of APC inactivation of FVa occurs in the presence of platelets.

Glycoproteins IIb and IIIa and Platelet Thrombospondin in a Liposome Model of Platelet Aggregation

1986 ◽  
Vol 55 (02) ◽  
pp. 240-245 ◽  
Author(s):  
M E Rybak
Keyword(s):  
Platelet Aggregation ◽  
Direct Evidence ◽  
Phospholipid Vesicles ◽  
Aggregate Formation ◽  
Membrane Glycoproteins ◽  
Protein Orientation ◽  
Phosphatidylcholine Liposomes ◽  
Calcium Dependent ◽  
Lentil Lectin ◽  
Complete Reversal

SummaryPlatelet membrane glycoproteins IIb and IIIa and platelet thrombospondin were incorporated onto phosphatidylcholine liposomes, by freeze thawing and sonication. Protein orientation on the liposomes was confirmed by susceptibility to neuraminidase cleavage and binding to lentil lectin-Sepharose (GPIIb-IIIa liposomes) and to heparin-Sepharose (thrombospondin liposomes). Glycoproteins Ilb-IIIa bound 125I-fibrinogen with Kd of 7.5 × 10™7M. Binding was reversible and calcium-dependent. Ilb-IIIa liposomes underwent fibrinogen-dependent aggregation in the presence of 10 mM CaCl2. Maximal aggregate formation was observed with a combination of IIb-IIIa liposomes and thrombospondin liposomes. This aggregation was partially inhibited by preincubation with monoclonal antibodies to the IIb-IIIa complex. Addition of EDTA caused complete reversal of aggregates. Thrombospondin liposomes also underwent fibrinogen and calcium dependent aggregation, however, this aggregation was less than that observed with the GPIIb-IIIa liposomes. Maximal aggregate formation was observed with a mixture of IIb-IIIa liposomes and thrombospondin liposomes. These studies demonstrate that GPIIb-IIIa and thrombospondin can be incorporated into phospholipid vesicles with preservation of function. Direct evidence is provided to demonstrate that glycoprotein lib and Ilia and fibrinogen are sufficient for platelet aggregation and to demonstrate that thrombospondin may also contribute to platelet aggregation.

Cholesterol metabolism and chemo-resistance in breast cancer

2018 ◽  
Author(s):  
Sam Hutchinson ◽  
Sebastiano Battaglia ◽  
Hanne Roberg-Larsen ◽  
Thomas Hughes ◽  
James Thorne
Keyword(s):  
Breast Cancer ◽  
Cholesterol Metabolism
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