scholarly journals Cell Responses to Extracellular α-Synuclein

Molecules ◽  
2019 ◽  
Vol 24 (2) ◽  
pp. 305 ◽  
Author(s):  
Alexei A. Surguchev ◽  
Fatemeh Nouri Emamzadeh ◽  
Andrei Surguchov
Keyword(s):  
Cell Surface ◽  
Close Association ◽  
Lewy Bodies ◽  
Cell Surface Receptors ◽  
Unfolded Proteins ◽  
Surface Receptors ◽  
Cell Responses ◽  
Biochemical Pathways ◽  
The Family

Synucleins are small naturally unfolded proteins involved in neurodegenerative diseases and cancer. The family contains three members: α-, β-, and -synuclein. α-Synuclein is the most thoroughly investigated because of its close association with Parkinson's disease (PD), dementia with Lewy bodies and multiple system atrophy. Until recently, the synuclein's research was mainly focused on their intracellular forms. However, new studies highlighted the important role of extracellular synucleins. Extracellular forms of synucleins propagate between various types of cells, bind to cell surface receptors and transmit signals, regulating numerous intracellular processes. Here we give an update of the latest results about the mechanisms of action of extracellular synucleins, their binding to cell surface receptors, effect on biochemical pathways and the role in neurodegeneration and neuroinflammation.

scholarly journals Integrins as architects of cell behavior

2016 ◽  
Vol 27 (19) ◽  
pp. 2885-2888 ◽  
Author(s):  
Charles H. Streuli
Keyword(s):  
Extracellular Matrix ◽  
Mammary Gland ◽  
Cell Surface ◽  
Cell Function ◽  
External Environment ◽  
Cell Behavior ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Mammary Gland Differentiation

Integrins are cell surface receptors that bind cells to their physical external environment, linking the extracellular matrix to cell function. They are essential in the biology of all animals. In the late 1980s, we discovered that integrins are required for the ability of breast epithelia to do what they are programmed to do, which is to differentiate and make milk. Since then, integrins have been shown to control most other aspects of phenotype: to stay alive, to divide, and to move about. Integrins also provide part of the mechanism that allows cells to form tissues. Here I discuss how we discovered that integrins control mammary gland differentiation and explore the role of integrins as central architects of other aspects of cell behavior.

scholarly journals Differential Regulation of the Uridine Nucleotide-activated P2Y4 and P2Y6 Receptors

2000 ◽  
Vol 276 (15) ◽  
pp. 11939-11948 ◽  
Author(s):  
Amy E. Brinson ◽  
T. Kendall Harden
Keyword(s):  
Cell Surface ◽  
Inositol Phosphate ◽  
Complete Recovery ◽  
Differential Regulation ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Astrocytoma Cells ◽  
Truncation Mutant ◽  
Uridine Nucleotide

Agonist-promoted regulation of the uridine nucleotide-activated human P2Y4 receptor (P2Y4-R) and P2Y6 receptor (P2Y6-R) was studied. Incubation of P2Y4-R-expressing 1321N1 human astrocytoma cells with the cognate agonist UTP resulted in rapid desensitization of the inositol phosphate response and a 50% loss of cell surface receptors. In contrast, incubation of P2Y6-R-expressing cells with the cognate agonist UDP caused neither rapid desensitization nor rapid loss of cell surface receptors. Removal of UTP from the medium of UTP-pretreated cells resulted in rapid and complete recovery of surface P2Y4-R even after 12 h of agonist treatment. Although extended incubation with UDP also caused a loss of surface P2Y6-R, rapid recovery of surface P2Y6-R did not occur following removal of agonist. Pharmacological studies indicated that neither protein kinase C nor other Ca2+-activated kinases were involved in agonist-promoted desensitization or loss of surface P2Y4-R or P2Y6-R. Mutational analyses were carried out to identify domains involved in agonist-dependent regulation of P2Y4-R. Sequential truncation of the carboxyl-terminal domain revealed that sequence between amino acids 332 and 343 was necessary for UTP-promoted desensitization and internalization. Further mutational analyses of the three serines in this domain confirmed that Ser-333 and Ser-334 play a major role in these agonist-promoted changes in P2Y4-R. Experiments were carried out with [32P]Pi-labeled cells to ascertain the role of phosphorylation in regulation of P2Y4-R. Incubation with UTP for 2 min caused a marked increase in phosphorylation of both the wild-type P2Y4-R and the P2Y4–343 truncation mutant. In contrast, no UTP-promoted phosphorylation of the P2Y4–332 truncation mutant was observed. Taken together, these results demonstrate differential regulation of uridine nucleotide-activated P2Y4-R and P2Y6-R and indicate that Ser-333 and Ser-334 in the carboxyl terminus of P2Y4-R are important for UTP-dependent phosphorylation, desensitization, and loss of surface receptors.

scholarly journals The Role of Cell Surface Receptors in the Activation of Human B Cells by Phosphorothioate Oligonucleotides

2000 ◽  
Vol 165 (3) ◽  
pp. 1438-1445 ◽  
Author(s):  
Hua Liang ◽  
Charles F. Reich ◽  
David S. Pisetsky ◽  
Peter E. Lipsky
Keyword(s):  
B Cells ◽  
Cell Surface ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Human B Cells

scholarly journals Studies on the role of specific cell surface receptors in the removal of lipoprotein (a) in man.

1983 ◽  
Vol 71 (5) ◽  
pp. 1431-1441 ◽  
Author(s):  
F Krempler ◽  
G M Kostner ◽  
A Roscher ◽  
F Haslauer ◽  
K Bolzano ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptors ◽  
Specific Cell ◽  
Lipoprotein A ◽  
Surface Receptors ◽  
Specific Cell Surface

RECEPTOR-DEPENDENT SENSITIVITY OF NF-κB TO LOW PHYSIOLOGICAL LEVEL

2013 ◽  
Vol 21 (03) ◽  
pp. 1350018
Author(s):  
PANPAN YANG ◽  
TIANSHOU ZHOU
Keyword(s):  
Cell Surface ◽  
Receptor Activation ◽  
Cell Surface Receptors ◽  
High Dose ◽  
Physiological Level ◽  
Information Encoding ◽  
Surface Receptors ◽  
Receptor Number ◽  
Activation Rates

In the NFκB signaling pathway, cells respond to different concentrations of the TNFα signal by means of NFκB transcription factors. Previous studies showed that most cells are activated under high-dose stimulations and NFκB activation results in oscillations in nuclear NFκB abundance. Here, by analyzing sensitivity gain for the response of the nuclear NFκB to the number of cell-surface receptors under low-dose stimulations, we show that changes in the receptor number can give rise to significant changes in the nonsaturation part of the dose–response curve, where the receptor activation rates are very sensitive to stimulations. In addition, the number of the activated receptors tends to increase in a large range of stimulation dose and can significantly influence the expression of the downstream genes. These results imply that the number of cell-surface receptors plays a role of information encoding like frequency or amplitude encoding described in previous studies.

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