Results 41 to 50 of about 313,816 (251)

Nociceptive Sensitization by Activation of Protease-Activated Receptor 2 in a Rat Model of Incisional Pain

Brain Sciences, 2021
Postoperative pain and consequent inflammatory responses after tissue incision adversely affects many surgical patients due to complicated mechanisms.
Kanta Kido, Norika Katagiri, Hiromasa Kawana, Shigekazu Sugino, Masanori Yamauchi, Eiji Masaki   +5 more
doaj   +1 more source

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

FEBS Letters, EarlyView.
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes, Jan Brysch, Carmen Gelze, Lilli Meier, Daniel Kümmel   +4 more
wiley   +1 more source

Neurological Symptoms of COVID-19: The Zonulin Hypothesis

Frontiers in Immunology, 2021
The irruption of SARS-CoV-2 during 2020 has been of pandemic proportions due to its rapid spread and virulence. COVID-19 patients experience respiratory, digestive and neurological symptoms.
Sílvia Llorens, Sílvia Llorens, Eduardo Nava, Eduardo Nava, Mónica Muñoz-López, Mónica Muñoz-López, Álvaro Sánchez-Larsen, Tomás Segura, Tomás Segura, Tomás Segura   +9 more
doaj   +1 more source

pH‐mediated activation of the lysosomal arginine sensor SLC38A9

FEBS Letters, EarlyView.
Cells monitor nutrient levels via the lysosomal transporter SLC38A9 to activate the mechanistic target of rapamycin complex 1 (mTORC1). This study reveals that SLC38A9 function is regulated by pH. We identified histidine 544 as a critical pH sensor that undergoes conformational changes to control amino acid efflux from lysosomes; therefore, it ...
Xuelang Mu, Ampon Sae Her, Tamir Gonen
wiley   +1 more source

Potent Agonists of the Protease Activated Receptor 2 (PAR₂) [PDF]

Journal of Medicinal Chemistry, 2011
Novel peptidomimetic pharmacophores to PAR(2) were designed based on the known activating peptide SLIGRL-NH(2). A set of 15 analogues was evaluated with a model cell line (16HBE14o-) that highly expresses PAR(2). Cells exposed to the PAR(2) activating peptide with N-terminal 2-furoyl modification (2-furoyl-LIGRLO-NH(2)) initiated increases in ...
Scott, Boitano, Andrea N, Flynn, Stephanie M, Schulz, Justin, Hoffman, Theodore J, Price, Josef, Vagner   +5 more
openaire   +2 more sources

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

FEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai, Mohyeddine Omrane, Nassima Benzoubir, Didier Samuel, Ama Gassama‐Diagne   +4 more
wiley   +1 more source

Protease-activated receptor-2 (PAR2) in cardiovascular system

Vascular Pharmacology, 2005
Vascular system is constituted by a complex and articulate network, e.g. arteries, arterioles, venules and veins, that requires a high degree of coordination between different elemental cell types. Proteinase-activated receptors (PARs) constitute a recent described family of 7-transmembrane G protein-coupled receptors that are activated by proteolysis.
BUCCI, MARIAROSARIA, ROVIEZZO, FIORENTINA, CIRINO, GIUSEPPE   +2 more
openaire   +3 more sources

Conserved Structure and Adjacent Location of the Thrombin Receptor and Protease-Activated Receptor 2 Genes Define a Protease-Activated Receptor Gene Cluster [PDF]

Molecular Medicine, 1996
Thrombin is a serine protease that elicits a variety of cellular responses. Molecular cloning of a thrombin receptor revealed a G protein-coupled receptor that is activated by a novel proteolytic mechanism. Recently, a second protease-activated receptor was discovered and dubbed PAR2.
M, Kahn, K, Ishii, W L, Kuo, M, Piper, A, Connolly, Y P, Shi, R, Wu, C C, Lin, S R, Coughlin   +8 more
openaire   +2 more sources

Rab14 regulates the transport of human papillomavirus to the trans‐Golgi network for infectious cell entry

FEBS Letters, EarlyView.
This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
wiley   +1 more source

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

FEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source