The investigation of detection and sensing mechanism of spicy substance based on human TRPV1 channel protein-cell membrane biosensor

2021 ◽  
Vol 172 ◽  
pp. 112779
Author(s):  
Sa Xiao ◽  
Panpan Song ◽  
Fanjie Bu ◽  
Guangchang Pang ◽  
Aimin Zhou ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Trpv1 Channel ◽  
Sensing Mechanism ◽  
Channel Protein ◽  
Protein Cell

scholarly journals Pregabalin alleviates postherpetic neuralgia by downregulating spinal TRPV1 channel protein

2021 ◽  
Vol 20 (11) ◽  
pp. 2287-2292
Author(s):  
Zhenping Xiao ◽  
Mengjun Liao ◽  
Yunwu He ◽  
Yonglin Li ◽  
Wuzhou Yang ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Dorsal Horn ◽  
Postherpetic Neuralgia ◽  
New Drugs ◽  
Spinal Cord Tissue ◽  
Sprague Dawley ◽  
Trpv1 Channel ◽  
Channel Protein ◽  
Tnf Α ◽  
Prefrontal Lobe

Purpose: To determine the mechanism involved in pregabalin-induced alleviation of postherpetic neuralgia in a rat model.Methods: Ninety-sixty healthy Sprague-Dawley (SD) rats were assigned to sham, model andpregabalin groups (32 rats per group). A model of postherpetic neuralgia (PN) was established. The expressions of IL-1β and TNF-α in spinal cord tissue were determined 7 days after administration of treatments. The proportions of fluorescence areas in astrocytes in the dorsal horn, prefrontal lobe and hippocampus, and level of spinal cord TRPV1 channel protein in each group were evaluated.Results: Relative to model rats, IL-1β and TNF-α in spinal cord of pregabalin rats were significantly reduced (p < 0.05). The areas of fluorescence in astrocytes in dorsal horn of spinal cord, prefrontal lobe and hippocampus of model group were significantly increased, relative to sham, but were decreased in rats in pregabalin group (p < 0.05).Conclusion: Pregabalin significantly alleviates postherpetic neuralgia via mechanisms which may be related to the inflammatory response of spinal dorsal horn and downregulation of TRPV1 channel protein expression. This finding may be useful in developing new drugs for alleviating postherpetic neuralgia.

Upregulation of the large conductance voltage- and Ca2+-activated K+ channels by Janus kinase 2

2014 ◽  
Vol 306 (11) ◽  
pp. C1041-C1049 ◽  
Author(s):  
Zohreh Hosseinzadeh ◽  
Ahmad Almilaji ◽  
Sabina Honisch ◽  
Tatsiana Pakladok ◽  
GuoXing Liu ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Brefeldin A ◽  
Bk Channels ◽  
Bk Channel ◽  
Janus Kinase ◽  
Protein Abundance ◽  
Janus Kinase 2 ◽  
Channel Protein ◽  
Jak2 Inhibitor ◽  
Whole Cell Patch Clamp

The iberiotoxin-sensitive large conductance voltage- and Ca2+-activated potassium (BK) channels (maxi-K+-channels) hyperpolarize the cell membrane thus supporting Ca2+ entry through Ca2+-release activated Ca2+ channels. Janus kinase-2 (JAK2) has been identified as novel regulator of ion transport. To explore whether JAK2 participates in the regulation of BK channels, cRNA encoding Ca2+-insensitive BK channels (BKM513I+Δ899–903) was injected into Xenopus oocytes with or without cRNA encoding wild-type JAK2, gain-of-function V617FJAK2, or inactive K882EJAK2. K+ conductance was determined by dual electrode voltage clamp and BK-channel protein abundance by confocal microscopy. In A204 alveolar rhabdomyosarcoma cells, iberiotoxin-sensitive K+ current was determined utilizing whole cell patch clamp. A204 cells were further transfected with JAK2 and BK-channel transcript, and protein abundance was quantified by RT-PCR and Western blotting, respectively. As a result, the K+ current in BKM513I+Δ899–903-expressing oocytes was significantly increased following coexpression of JAK2 or V617FJAK2 but not K882EJAK2. Coexpression of the BK channel with V617FJAK2 but not K882EJAK2 enhanced BK-channel protein abundance in the oocyte cell membrane. Exposure of BK-channel and V617FJAK2-expressing oocytes to the JAK2 inhibitor AG490 (40 μM) significantly decreased K+ current. Inhibition of channel insertion by brefeldin A (5 μM) decreased the K+ current to a similar extent in oocytes expressing the BK channel alone and in oocytes expressing the BK channel and V617FJAK2. The iberiotoxin (50 nM)-sensitive K+ current in rhabdomyosarcoma cells was significantly decreased by AG490 pretreatment (40 μM, 12 h). Moreover, overexpression of JAK2 in A204 cells significantly enhanced BK channel mRNA and protein abundance. In conclusion, JAK2 upregulates BK channels by increasing channel protein abundance in the cell membrane.

scholarly journals Coarse-Grained Models for Protein-Cell Membrane Interactions

Polymers ◽  
2013 ◽  
Vol 5 (3) ◽  
pp. 890-936 ◽  
Author(s):  
Ryan Bradley ◽  
Ravi Radhakrishnan
Keyword(s):  
Cell Membrane ◽  
Coarse Grained ◽  
Membrane Interactions ◽  
Protein Cell

scholarly journals Regulation of Large Conductance Voltage-and Ca2+-Activated K+ Channels by the Janus Kinase JAK3

2015 ◽  
Vol 37 (1) ◽  
pp. 297-305 ◽  
Author(s):  
Jamshed Warsi ◽  
Yogesh Singh ◽  
Bernat Elvira ◽  
Zohreh Hosseinzadeh ◽  
Florian Lang
Keyword(s):  
Cell Proliferation ◽  
Cell Membrane ◽  
Bk Channel ◽  
Janus Kinase ◽  
Negative Regulator ◽  
K Channel ◽  
Protein Abundance ◽  
Wild Type ◽  
Protein Insertion ◽  
Channel Protein

Background/Aims: Janus kinase 3 (JAK3), a tyrosine kinase contributing to the regulation of cell proliferation and apoptosis of lymphocytes and tumour cells, has been shown to modify the expression and function of several ion channels and transport proteins. Channels involved in the regulation of cell proliferation include the large conductance voltage- and Ca2+-activated K+ channel BK. The present study explored whether JAK3 modifies BK channel protein abundance and current. Methods: cRNA encoding Ca2+-insensitive BK channel (BKM513I+Δ899-903) was injected into Xenopus oocytes with or without additional injection of cRNA encoding wild-type JAK3, constitutively active A568VJAK3, or inactive K851AJAK3. Voltage gated K+ channel activity was measured utilizing dual electrode voltage clamp. Moreover, BK channel protein abundance was determined utilizing flow cytometry in CD19+ B lymphocyte cell membranes from mice lacking functional JAK3 (jak3-/-) and corresponding wild-type mice (jak3+/+). Results: BK activity in BKM513I+Δ899-903 expressing oocytes was slightly but significantly decreased by coexpression of wild-type JAK3 and of A568VJAK3, but not by coexpression of K851AJAK3. The BK channel protein abundance in the cell membrane was significantly higher in jak3-/- than in jak3+/+ B lymphocytes. The decline of conductance in BK and JAK3 coexpressing oocytes following inhibition of channel protein insertion by brefeldin A (5 µM) was similar in oocytes expressing BK with JAK3 and oocytes expressing BK alone, indicating that JAK3 might slow channel protein insertion into rather than accelerating channel protein retrieval from the cell membrane. Conclusion: JAK3 is a weak negative regulator of membrane BK protein abundance and activity.

scholarly journals Calcium stimulates parathyroid hormone-related protein production in Leydig tumor cells through a putative cation-sensing mechanism

2000 ◽  
pp. 500-505 ◽  
Author(s):  
N Buchs ◽  
D Manen ◽  
JP Bonjour ◽  
R Rizzoli
Keyword(s):  
Parathyroid Hormone ◽  
Cell Membrane ◽  
Tumor Cells ◽  
Dependent Manner ◽  
Related Protein ◽  
Sensing Mechanism ◽  
Calcium Sensing ◽  
Parathyroid Hormone Related Protein ◽  
Leydig Tumor Cells ◽  
Cation Sensing

The production of parathyroid hormone-related protein (PTHrP) is regulated by a variety of hormones and growth factors. Previous research has shown that several PTHrP-producing cells are influenced by extracellular calcium (Ca(2+)(o)) concentration, with elevated levels increasing PTH-like activity released by cultured H500 rat Leydig tumor cells through a post-transcriptional mechanism. We have investigated the hypothesis that calcium stimulates PTHrP production in H500 cells by interacting with a cell membrane-associated cation-sensing receptor. Besides increased Ca(2+)(o) concentration, magnesium and the polycationic antibiotic neomycin also increased PTHrP production in a concentration-dependent manner. In the presence of the calcium ionophore, ionomycin, which markedly elevated cytosolic free calcium, the stimulation by Ca(2+)(o) of PTHrP could still be detected. These results indicate that increasing Ca(2+)(o) stimulates PTHrP production, possibly through a putative cell membrane-associated calcium-sensing mechanism. RT-PCR revealed the presence of a very small amount of calcium-sensing receptor coding mRNA.

Sarcolemmal permeability changes during early myocardial anoxia

1978 ◽  
Vol 36 (2) ◽  
pp. 642-643
Author(s):  
M. Ashraf ◽  
L. Landa ◽  
L. Nimmo ◽  
C. M. Bloor
Keyword(s):  
Cell Membrane ◽  
Membrane Permeability ◽  
Coronary Artery Occlusion ◽  
Artery Occlusion ◽  
Cell Membrane Permeability ◽  
Enzyme Release ◽  
Sprague Dawley ◽  
Sprague Dawley Rats ◽  
Sarcolemmal Permeability ◽  
Membrane Changes

Following coronary artery occlusion, the myocardial cells lose intracellular enzymes that appear in the serum 3 hrs later. By this time the cells in the ischemic zone have already undergone irreversible changes, and the cell membrane permeability is variably altered in the ischemic cells. At certain stages or intervals the cell membrane changes, allowing release of cytoplasmic enzymes. To correlate the changes in cell membrane permeability with the enzyme release, we used colloidal lanthanum (La+++) as a histological permeability marker in the isolated perfused hearts. The hearts removed from sprague-Dawley rats were perfused with standard Krebs-Henseleit medium gassed with 95% O2 + 5% CO2. The hypoxic medium contained mannitol instead of dextrose and was bubbled with 95% N2 + 5% CO2. The final osmolarity of the medium was 295 M osmol, pH 7. 4.

Flagellar Attachment in Selected Trypanosomes

1973 ◽  
Vol 31 ◽  
pp. 496-497
Author(s):  
J. J. Paulin
Keyword(s):  
Cell Membrane ◽  
Lateral Surface ◽  
The Body ◽  
Flagellar Pocket ◽  
Integral Component ◽  
Free Flagellum ◽  
Flagellar Axoneme

Movement in epimastigote and trypomastigote stages of trypanosomes is accomplished by planar sinusoidal beating of the anteriorly directed flagellum and associated undulating membrane. The flagellum emerges from a bottle-shaped depression, the flagellar pocket, opening on the lateral surface of the cell. The limiting cell membrane envelopes not only the body of the trypanosome but is continuous with and insheathes the flagellar axoneme forming the undulating membrane. In some species a paraxial rod parallels the axoneme from its point of emergence at the flagellar pocket and is an integral component of the undulating membrane. A portion of the flagellum may extend beyond the anterior apex of the cell as a free flagellum; the length is variable in different species of trypanosomes.

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