Phytochrome-mediated light signal transmission to the phosphorylation of proteins in the plasma membrane and the soluble fraction of etiolated pea stem sections

1994 ◽  
Vol 24 (3) ◽  
pp. 163-167 ◽  
Author(s):  
Tohru Hamada ◽  
Kohji Hasunuma
Keyword(s):  
Plasma Membrane ◽  
Soluble Fraction ◽  
Signal Transmission ◽  
Light Signal ◽  
Phosphorylation Of Proteins

scholarly journals Surface glycoproteins of human spermatozoa

1986 ◽  
Vol 82 (1) ◽  
pp. 11-22
Author(s):  
M. Kallajoki ◽  
I. Virtanen ◽  
J. Suominen
Keyword(s):  
Plasma Membrane ◽  
Gel Electrophoresis ◽  
Soluble Fraction ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Human Spermatozoa ◽  
Galactose Oxidase ◽  
Sperm Cells ◽  
Neuraminidase Treatment ◽  
Triton X

The surface membrane glycoprotein composition of human spermatozoa has been studied by introducing radioactive label into galactosyl (Gal) and N-acetylgalactosaminyl (GalNAc) residues by using the galactose oxidase/NaB3H4 method. Triton X-100 extracts and Triton X-100-resistant cytoskeletal residues were subjected to analysis by polyacrylamide gel electrophoresis. The distribution of the radiolabel in sperm cells was studied by light-microscopic auto-radiography. The grains were evenly distributed on the cells by the labelling methods used. The Triton X-100 treatment did not affect sperm morphology at the light-microscopic level, but in transmission electron microscopy the plasma membrane covering the acrosome was removed totally, together with most of the acrosomal membranes and acrosomal contents. Plasma membrane residues were, however, always found in the postacrosomal region. Borohydride alone without oxidative pretreatment labelled two polypeptides of molecular weights (Mr) 48,000 and 43,000 in the Triton X-100-soluble fraction. When the Gal/GalNAc residues were labelled by galactose oxidase pretreatment 120,000, 105,000, 78,000 and 68,000 Mr glycoproteins were revealed. When additional neuraminidase treatment was used to remove terminal sialic acid residues, the total labelling intensity was increased two- to fivefold and additional 36,000 and 20,000 Mr glycoproteins were revealed. The Triton X-100-resistant cytoskeletal residue contained 53–75% of the total radioactivity bound in sperm cells. When these components were analysed by polyacrylamide gel electrophoresis, all the major bands found in the Triton X-100-soluble fraction were detected and also some radioactivity was incorporated into the major bands visualized by protein staining. In the present study we describe several human sperm glycoproteins, which seem to be distributed evenly on the sperm cells. Detergent extraction, producing cytoskeletal models, appeared to leave most of the glycoproteins detectable in the extraction residues also with the apparent enrichment of a single 68,000 Mr glycoprotein.

scholarly journals Spontaneous Membrane Nanodomain Formation in the Absence or Presence of the Neurotransmitter Serotonin

2020 ◽  
Vol 8 ◽  
Author(s):  
Anna Bochicchio ◽  
Astrid F. Brandner ◽  
Oskar Engberg ◽  
Daniel Huster ◽  
Rainer A. Böckmann
Keyword(s):  
Phase Transition ◽  
Plasma Membrane ◽  
Specific Binding ◽  
Signal Transmission ◽  
Acyl Chain ◽  
Md Simulations ◽  
High Temporal Resolution ◽  
Detailed Knowledge ◽  
Transient Nature ◽  
Different Temperatures

Detailed knowledge on the formation of biomembrane domains, their structure, composition, and physical characteristics is scarce. Despite its frequently discussed importance in signaling, e.g., in obtaining localized non-homogeneous receptor compositions in the plasma membrane, the nanometer size as well as the dynamic and transient nature of domains impede their experimental characterization. In turn, atomistic molecular dynamics (MD) simulations combine both, high spatial and high temporal resolution. Here, using microsecond atomistic MD simulations, we characterize the spontaneous and unbiased formation of nano-domains in a plasma membrane model containing phosphatidylcholine (POPC), palmitoyl-sphingomyelin (PSM), and cholesterol (Chol) in the presence or absence of the neurotransmitter serotonin at different temperatures. In the ternary mixture, highly ordered and highly disordered domains of similar composition coexist at 303 K. The distinction of domains by lipid acyl chain order gets lost at lower temperatures of 298 and 294 K, suggesting a phase transition at ambient temperature. By comparison of domain ordering and composition, we demonstrate how the domain-specific binding of the neurotransmitter serotonin results in a modified domain lipid composition and a substantial downward shift of the phase transition temperature. Our simulations thus suggest a novel mode of action of neurotransmitters possibly of importance in neuronal signal transmission.

Signal transduction and signal transmission

e-Neuroforum ◽  
2010 ◽  
Vol 16 (3) ◽  
Author(s):  
A. Gießl ◽  
H. Regus-Leidig ◽  
J. H. Brandstätter
Keyword(s):  
Dynamic Range ◽  
Single Photon ◽  
Signal Transmission ◽  
Light Signal ◽  
Rod Photoreceptor ◽  
Physical Stimulus ◽  
Light Sensing ◽  
Broad Dynamic Range ◽  
Processing Pathways ◽  
Rod And Cone Photoreceptors

AbstractVision begins in highly specialized light-sensing neurons, the rod and cone photoreceptors. Their task is to absorb photons, transduce the physical stimulus into neuronal sig­nals, transmit the signals to the parallel signal processing pathways of the subsequent reti­nal network with the highest possible fidelity and continuously adapt to changes in stim­ulus intensities. If you imagine a pitch-black night with only a few photons hitting the ret­ina and being absorbed by the photoreceptors and a bright sunny day with the photore­ceptors being bombarded by billions of photons, you realize that a photoreceptor faces two fundamental challenges: it has to detect the light signal with the greatest sensitivity, e.g. a single photon leads to a change in the membrane potential of a rod photoreceptor and, at the same time, encode light intensities covering a broad dynamic range of sev­eral orders of magnitude. To fulfill these demands, photoreceptors have developed separate, structurally and functionally specialized compartments, which are the topic of this article: the outer segment for signal transduc­tion and the terminal with its highly complex ribbon synapse for signal transmission.

Capacitation Induces Tyrosine Phosphorylation of Proteins in the Boar Sperm Plasma Membrane

1999 ◽  
Vol 262 (3) ◽  
pp. 787-792 ◽  
Author(s):  
Frits M. Flesch ◽  
Ben Colenbrander ◽  
Lambert M.G. van Golde ◽  
Barend M. Gadella
Keyword(s):  
Plasma Membrane ◽  
Tyrosine Phosphorylation ◽  
Phosphorylation Of Proteins ◽  
Boar Sperm ◽  
Sperm Plasma Membrane

40Gbit∕s light signal transmission in long-range surface plasmon waveguides

2007 ◽  
Vol 91 (17) ◽  
pp. 171117 ◽  
Author(s):  
Jung Jin Ju ◽  
Suntak Park ◽  
Min-su Kim ◽  
Jin Tae Kim ◽  
Seung Koo Park ◽  
...  
Keyword(s):  
Long Range ◽  
Surface Plasmon ◽  
Signal Transmission ◽  
Light Signal

scholarly journals Insulin stimulates the tyrosyl phosphorylation and activation of the 52 kDa peripheral plasma-membrane cyclic AMP phosphodiesterase in intact hepatocytes

1989 ◽  
Vol 261 (3) ◽  
pp. 897-904 ◽  
Author(s):  
N J Pyne ◽  
W Cushley ◽  
H G Nimmo ◽  
M D Houslay
Keyword(s):  
Plasma Membrane ◽  
Cyclic Amp ◽  
Insulin Treatment ◽  
Prior Treatment ◽  
High Affinity ◽  
Phosphorylation Of Proteins ◽  
Cyclic Amp Phosphodiesterase ◽  
Peripheral Plasma ◽  
Phosphoamino Acid Analysis ◽  
Tyrosyl Phosphorylation

The 52 kDa subunit of the peripheral-plasma-membrane insulin-stimulated high-affinity cyclic AMP phosphodiesterase can be specifically detected by the antibody PM1 by Western-blotting procedures and also can be immunoprecipitated from a hepatocyte extract. PM1-mediated immunoprecipitation from hepatocyte extracts showed that insulin treatment of intact 32P-labelled hepatocytes caused the rapid phosphorylation of the peripheral-plasma-membrane cyclic AMP phosphodiesterase. Phosphoamino acid analysis and the use of a phosphotyrosine-specific antibody indicated that phosphorylation occurred on tyrosyl residue(s) of this phosphodiesterase. Prior treatment of hepatocytes with glucagon (10 nM) completely blocked the insulin-mediated tyrosyl phosphorylation of this 52 kDa protein, as detected with both the PM1 and the anti-phosphotyrosine antibodies. Treatment of hepatocytes with glucagon alone did not increase the phosphorylation state of the peripheral-plasma-membrane cyclic AMP phosphodiesterase. The specific anti-phosphotyrosine antibody also detected the insulin-stimulated phosphorylation of proteins of 180 kDa, 95 kDa and 39 kDa. Prior treatment of hepatocytes with glucagon decreased the ability of insulin to phosphorylate the 180 kDa and 39 kDa species, but not the 95 kDa species.

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