A bola-phospholipid bearing tetrafluorophenylazido chromophore as a promising lipid probe for biomembrane photolabeling studies

2013 ◽  
Vol 11 (30) ◽  
pp. 5000 ◽  
Author(s):  
Yi Xia ◽  
Kheya Sengupta ◽  
Alain Maggiani ◽  
Fanqi Qu ◽  
Ling Peng
Keyword(s):  
Lipid Probe

Induction of surface fluidity in Trichinella spiralis larvae during penetration of the host intestine: simulation by cyclic AMP in vitro

Parasitology ◽  
1997 ◽  
Vol 114 (1) ◽  
pp. 71-77 ◽  
Author(s):  
J. MODHA ◽  
M. C. ROBERTS ◽  
M. W. KENNEDY ◽  
J. R. KUSEL
Keyword(s):  
Cyclic Amp ◽  
Trichinella Spiralis ◽  
Lateral Diffusion ◽  
Epithelial Tissue ◽  
Intestinal Epithelial ◽  
Parasitic Helminths ◽  
Intracellular Parasites ◽  
Fluid Properties ◽  
Lipid Probe

The lateral diffusion (DL) properties of the fluorescent lipid probe 5-N (octadecanoyl) aminofluorescein (AF18) inserted into the surface of muscle-stage larvae of Trichinella spiralis were investigated by fluorescence recovery after photobleaching. AF18 was not free to diffuse laterally in dormant larvae, and this remained unchanged after larval activation in vitro with trypsin and bile. However, a significant increase in surface fluidity of the probe was demonstrated (%R = 74·5; DL = 11·5 × 10−9 cm2/sec) when larvae invaded intestinal epithelial tissue following oral infection of mice. Membrane-permeant photoactivatable caged cyclic AMP was used to analyse the putative mechanism responsible for this increase in lateral diffusion in the parasite surface. Although incubation of larvae with 1–50 μM caged cAMP had no effect on surface fluidity, incubation with 100 μM caged cAMP induced a substantial increase in the lateral mobility of AF18 (%R = 64·3; DL = 8·3 × 10−11 cm2/sec) immediately following photo-activation of the caged messenger. This induced fluidity, however, was transient and the larval surface reverted to immobility within 15 min. These observations constitute the first reported measurement of the fluid properties of the surface of intracellular parasites, the first demonstration of the parasite surface fluidity altering as a result of host cell invasion and the first indication of a mechanism underlying changes in surface fluidity in parasitic helminths.

scholarly journals A Novel Fluorescent Lipid Probe for Dry Eye: Retrieval by Tear Lipocalin in Humans

2013 ◽  
Vol 54 (2) ◽  
pp. 1398 ◽  
Author(s):  
Po-Ting Yeh ◽  
Richard Casey ◽  
Ben J. Glasgow
Keyword(s):  
Dry Eye ◽  
Tear Lipocalin ◽  
Lipid Probe ◽  
Fluorescent Lipid

scholarly journals Lateral diffusion of the PH-20 protein on guinea pig sperm: evidence that barriers to diffusion maintain plasma membrane domains in mammalian sperm

1987 ◽  
Vol 104 (4) ◽  
pp. 917-923 ◽  
Author(s):  
AE Cowan ◽  
DG Myles ◽  
DE Koppel
Keyword(s):  
Plasma Membrane ◽  
Guinea Pig ◽  
Domain Boundary ◽  
Lateral Diffusion ◽  
Fold Increase ◽  
Membrane Domains ◽  
Mammalian Sperm ◽  
Acrosomal Membrane ◽  
Percent Recovery ◽  
Lipid Probe

PH-20 protein on the plasma membrane (PH-20PM) is restricted to the posterior head of acrosome-intact guinea pig sperm. During the exocytotic acrosome reaction the inner acrosomal membrane (IAM) becomes continuous with the posterior head plasma membrane, and PH-20PM migrates to the IAM. There it joins a second population of PH-20 protein localized to this region of the acrosomal membrane (PH-20AM) (Cowan, A.E., P. Primakoff, and D.G. Myles, 1986, J. Cell Biol. 103:1289-1297). To investigate how the localized distributions of PH-20 protein are maintained, the lateral mobility of PH-20 protein on these different membrane domains was determined using fluorescence redistribution after photobleaching. PH-20PM on the posterior head of acrosome-intact sperm was found to be mobile, with a diffusion coefficient and percent recovery typical of integral membrane proteins (D = 1.8 X 10(-10) cm2/s; %R = 73). This value of D was some 50-fold lower than that found for the lipid probe 1,1-ditetradecyl 3,3,3',3'-tetramethylindocarbocyanine perchlorate (C14diI) in the same region (D = 8.9 X 10(-9) cm2/s). After migration to the IAM of acrosome-reacted sperm, this same population of molecules (PH-20PM) exhibited a 30-fold increase in diffusion rate (D = 4.9 X 10(-9) cm2/s; %R = 78). This rate was similar to diffusion of the lipid probe C14diI in the IAM (D = 5.4 X 10(-9) cm2/s). The finding of free diffusion of PH-20PM in the IAM of acrosome-reacted sperm supports the proposal that PH-20 is maintained within the IAM by a barrier to diffusion at the domain boundary. The slower diffusion of PH-20PM on the posterior head of acrosome-intact sperm is also consistent with localization by barriers to diffusion, but does not rule out alternative mechanisms.

scholarly journals Identification of a lysosomal protein causing lipid transfer, using a fluorescence assay designed to monitor membrane fusion between rat liver endosomes and lysosomes

1995 ◽  
Vol 308 (3) ◽  
pp. 937-946 ◽  
Author(s):  
T Kuwana ◽  
B M Mullock ◽  
J P Luzio
Keyword(s):  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Fusion Event ◽  
Transfer Protein ◽  
Activator Protein ◽  
Gm2 Activator ◽  
Gm2 Activator Protein ◽  
Lipid Probe ◽  
Lysosomal Protein ◽  
Fluorescence Dequenching

In the present and previous studies [Mullock, Perez, Kuwana, Gray and Luzio (1994) J. Cell Biol. 126, 1173-1182], we have attempted to investigate endosome-lysosome fusion using an assay based on the dilution of the self-quenching fluorescent lipid probe octadecylrhodamine. Although some characteristics of fluorescence dequenching were consistent with those observed in other cell-free assays, we have now demonstrated that increased fluorescence was due to leakage of an intralysosomal lipid-transfer protein. This protein was purified and found to be a 22 kDa molecule with sequence, immunological and functional characteristics strongly suggesting that it is the rat homologue of human GM2-activator protein. Both the 22 kDa protein and recombinant human GM2-activator protein caused fluorescence dequenching either when mixed with octadecylrhodamine-loaded endosomes and lysosomal membranes or in a liposome system. The data were consistent with GM2-activator protein acting as an octadecylrhodamine-transfer protein. Antibodies to the 22 kDa protein added to cell-free endosome-lysosome content-mixing assays had no effect, although they could inhibit fluorescence dequenching caused by the protein. Thus this protein is not required in any fusion event involved in delivery of ligands from endosomes to lysosomes. The existence within an intracellular organelle of a protein capable of acting as an octadecylrhodamine-transfer protein suggests the need for caution in the interpretation of fluorescence-dequenching assays using mammalian subcellular fractions.

scholarly journals Lateral diffusion of surface immunoglobulin, Thy-1 antigen, and a lipid probe in lymphocyte plasma membranes

1979 ◽  
Vol 76 (10) ◽  
pp. 5163-5167 ◽  
Author(s):  
P. Dragsten ◽  
P. Henkart ◽  
R. Blumenthal ◽  
J. Weinstein ◽  
J. Schlessinger
Keyword(s):  
Plasma Membranes ◽  
Lateral Diffusion ◽  
Surface Immunoglobulin ◽  
Lipid Probe

Prolactin increases lipid fluidity and prolactin binding of rat prostatic membranes

1985 ◽  
Vol 248 (6) ◽  
pp. E687-E693
Author(s):  
J. R. Dave ◽  
R. J. Witorsch
Keyword(s):  
Serum Lipid ◽  
Membrane Lipid ◽  
Male Rats ◽  
Ventral Prostate ◽  
Prolactin Receptors ◽  
Lipid Fluidity ◽  
Ovine Prolactin ◽  
Endogenous Substances ◽  
Membrane Lipid Fluidity ◽  
Lipid Probe

The objective of these studies was to determine whether prolactin could modify the lipid fluidity of rat ventral and dorsolateral prostate membranes and subsequently modify the availability of prolactin receptors. Additional studies were also undertaken to determine the effects of prolactin on serum lipid fluidity. Adult male rats were injected with 0, 100, or 400 micrograms ovine prolactin/day subcutaneously for a period of 5 days. Serum and prostatic membrane lipid fluidity was measured by a fluorescence polarization method using a lipid probe 1,6-diphenylhexatriene. Prolactin binding in dextran-coated charcoal-pretreated prostatic membranes was determined by radioreceptor assay. This pretreatment has been reported by us to remove the endogenous substances that interfere with prolactin binding assay (J. R. Dave and R. J. Witorsch, Endocrinology 111: 2144-2146, 1982). Prolactin binding increased by approximately 44 and 72% in dorsolateral prostate and 16 and 39% in ventral prostate in 100- and 400-micrograms groups, respectively. Membrane fluidity increased by approximately 16 and 19% in dorsolateral prostate and 10 and 13% in ventral prostate in 100- and 400-micrograms groups, respectively. Serum lipid fluidity increased 50 and 79% in 100- and 400-micrograms groups, respectively.

Lateral transport of a lipid probe and labeled proteins on a cell membrane

Science ◽  
1977 ◽  
Vol 195 (4275) ◽  
pp. 307-309 ◽  
Author(s):  
J Schlessinger ◽  
D Axelrod ◽  
D. Koppel ◽  
W. Webb ◽  
E. Elson
Keyword(s):  
Cell Membrane ◽  
Lateral Transport ◽  
A Cell ◽  
Lipid Probe

scholarly journals Effects of lipid-probe interactions in biochemical fluorometric methods that assess HDL redox activity

2012 ◽  
Vol 11 (1) ◽  
Author(s):  
Theodoros Kelesidis ◽  
Srinivasa T Reddy ◽  
Diana Huynh ◽  
David Meriwether ◽  
Alan M Fogelman ◽  
...  
Keyword(s):  
Redox Activity ◽  
Lipid Probe

Effects of phytohormones on the surfaces of plant-parasitic nematodes

Parasitology ◽  
2002 ◽  
Vol 125 (2) ◽  
pp. 165-175 ◽  
Author(s):  
A. AKHKHA ◽  
J. KUSEL ◽  
M. KENNEDY ◽  
R. CURTIS
Keyword(s):  
Meloidogyne Incognita ◽  
Binding Proteins ◽  
Opposite Effect ◽  
Parasitic Nematodes ◽  
Direct Effects ◽  
Plant Parasitic Nematodes ◽  
High Concentrations ◽  
Lipid Probe ◽  
Plant Parasitic ◽  
Surface Changes

The direct effects of phytohormones (auxin and kinetin) and root diffusates on the surface lipophilicity of the plant parasitic nematodes Globodera rostochiensis and Meloidogyne incognita were investigated. The fluorescent lipid probe AF18 (5-N-(octodecanoyl) aminofluorescein) was used to detect surface changes. Root diffusates increased AF18 uptake by G. rostochiensis while it had no effect on M. incognita. Kinetin and auxin decreased AF18 uptake in G. rostochiensis, while they had the opposite effect on M. incognita. Auxin/kinetin ratio was also found to be important in triggering the surface changes, especially at high concentrations. Whether plant nematodes have auxin and/or kinetin binding proteins is discussed as well as the mechanism behind the surface lipophilicity changes due to root diffusates and phytohormones.

Sign in / Sign up

Export Citation Format

Share Document