Coypu (Myocastor coypus bonaeriensis) Ovarian Morphology During the Oestrous Cycle.

The coypu (Myocastor coypus bonariensis) is an annual polyestrous hystricomorph rodent with variable-length oestrous cycles, which ovarian histoarchitecture during this period is not fully described. This study analyses variations in ovarian morphology during the oestrous cycle, focusing on follicular development and atresia. Eighteen sexually mature virgin females aged 7-9 months, weighing 4.

Molecular mapping of KCNE4-dependent regulation of Kv1.3.

The voltage-gated potassium channel Kv1.3 plays a crucial role in the immune system response. In leukocytes, the channel is co-expressed with the dominant negative regulatory subunit KCNE4, which associates with Kv1.

BioID-based intact cell interactome of the Kv1.3 potassium channel identifies a Kv1.3-STAT3-p53 cellular signaling pathway.

Kv1.3 is a multifunctional potassium channel implicated in multiple pathologies, including cancer. However, how it is involved in disease progression is not fully clear.

KCNE4-dependent modulation of Kv1.3 pharmacology.

The voltage-dependent potassium channel Kv1.3 is a promising therapeutic target for the treatment of autoimmune and chronic inflammatory disorders. Kv1.

Kv1.3 in the spotlight for treating immune diseases.

Introduction: Kv1.3 is the main voltage-gated potassium channel of leukocytes from both the innate and adaptive immune systems. Channel function is required for common processes such as Ca signaling but also for cell-specific events.

Routing of Kv7.1 to endoplasmic reticulum plasma membrane junctions.

Aim: The voltage-gated Kv7.1 channel, in association with the regulatory subunit KCNE1, contributes to the I current in the heart. However, both proteins travel to the plasma membrane using different routes.

Dynamics and spatial organization of Kv1.3 at the immunological synapse of human CD4+ T cells.

Formation of the immunological synapse (IS) is a key event during initiation of an adaptive immune response to a specific antigen. During this process, a T cell and an antigen presenting cell form a stable contact that allows the T cell to integrate both internal and external stimuli in order to decide whether to activate. The threshold for T cell activation depends on the strength and frequency of the calcium (Ca) signaling induced by antigen recognition, and it must be tightly regulated to avoid undesired harm to healthy cells.

The Phosphorylation of Kv1.3: A Modulatory Mechanism for a Multifunctional Ion Channel.

The voltage-gated potassium channel Kv1.3 plays a pivotal role in a myriad of biological processes, including cell proliferation, differentiation, and apoptosis. Kv1.

Membrane Channels in Health and Diseases.

The goal of this Special Issue, entitled "Membrane Channels in Health and Diseases (https://www [...

Palmitoylation of Voltage-Gated Ion Channels.

Protein lipidation is one of the most common forms of posttranslational modification. This alteration couples different lipids, such as fatty acids, phospho- and glycolipids and sterols, to cellular proteins. Lipidation regulates different aspects of the protein's physiology, including structure, stability and affinity for cellular membranes and protein-protein interactions.

Oligomerization and Spatial Distribution of Kvβ1.1 and Kvβ2.1 Regulatory Subunits.

Members of the regulatory Kvβ family modulate the kinetics and traffic of voltage-dependent K (Kv) channels. The crystal structure of Kv channels associated with Kvβ peptides suggests a α4/β4 composition. Although Kvβ2 and Kvβ1 form heteromers, evidence supports that only Kvβ2.

The Mitochondrial Routing of the Kv1.3 Channel.

Voltage-gated potassium channels control neuronal excitability and cardiac action potentials. In addition, these proteins are involved in a myriad of cellular processes. The potassium channel Kv1.

S-acylation-dependent membrane microdomain localization of the regulatory Kvβ2.1 subunit.

The voltage-dependent potassium (Kv) channel Kvβ family was the first identified group of modulators of Kv channels. Kvβ regulation of the α-subunits, in addition to their aldoketoreductase activity, has been under extensive study. However, scarce information about their specific α-subunit-independent biology is available.

Kv1.3 Controls Mitochondrial Dynamics during Cell Cycle Progression.

The voltage-gated potassium channel Kv1.3 is a potential therapeutic target for obesity and diabetes. The genetic ablation and pharmacological inhibition of Kv1.

Metal-Cocatalyst Interaction Governs the Catalytic Activity of M-Porphyrazines for Chemical Fixation of CO.

Chemical fixation of CO to produce cyclic carbonates can be a green and atomic efficient process. In this work, a series of porphyrazines (Pzs) containing electron-withdrawing groups and central M ions (where M = Mg, Zn, Cu, and Co) were synthesized and investigated as catalysts for the cycloaddition of CO to epoxides. Then, the efficiency of the Pzs was tested by varying cocatalyst type and concentration, epoxide, temperature, and pressure.

KCNE4-dependent functional consequences of Kv1.3-related leukocyte physiology.

The voltage-dependent potassium channel Kv1.3 plays essential roles in the immune system, participating in leukocyte activation, proliferation and apoptosis. The regulatory subunit KCNE4 acts as an ancillary peptide of Kv1.

Calmodulin-dependent KCNE4 dimerization controls membrane targeting.

The voltage-dependent potassium channel Kv1.3 participates in the immune response. Kv1.

A novel mitochondrial Kv1.3-caveolin axis controls cell survival and apoptosis.

The voltage-gated potassium channel Kv1.3 plays an apparent dual physiological role by participating in activation and proliferation of leukocytes as well as promoting apoptosis in several types of tumor cells. Therefore, Kv1.

Remodeling of Kv7.1 and Kv7.5 Expression in Vascular Tumors.

Voltage-dependent potassium (Kv) channels contribute to the excitability of nerves and muscles. In addition, Kv participates in several cell functions, including cell cycle progression and proliferation. Kv channel remodeling has been associated with neoplastic cell growth and cancer.

Endocytosis: A Turnover Mechanism Controlling Ion Channel Function.

Ion channels (IChs) are transmembrane proteins that selectively drive ions across membranes. The function of IChs partially relies on their abundance and proper location in the cell, fine-tuned by the delicate balance between secretory, endocytic, and degradative pathways. The disruption of this balance is associated with several diseases, such as Liddle's and long QT syndromes.

Functional Consequences of the Variable Stoichiometry of the Kv1.3-KCNE4 Complex.

The voltage-gated potassium channel Kv1.3 plays a crucial role during the immune response. The channel forms oligomeric complexes by associating with several modulatory subunits.

The unconventional biogenesis of Kv7.1-KCNE1 complexes.

The potassium channel Kv7.1 associates with the KCNE1 regulatory subunit to trigger cardiac currents. Although the Kv7.

Photobleaching Efficiency Parallels the Enhancement of Membrane Damage for Porphyrazine Photosensitizers.

Photostability is considered a key asset for photosensitizers (PS) used in medical applications as well as for those used in energy conversion devices. In light-mediated medical treatments, which are based on PS-induced harm to diseased tissues, the photoinduced cycle of singlet oxygen generation has always been considered to correlate with PS efficiency. However, recent evidence points to the fundamental role of contact-dependent reactions, which usually cause PS photobleaching.

Triple-Colocalization Approach to Assess Traffic Patterns and Their Modulation.

Confocal microscopy permits the analysis of the subcellular distribution of proteins. Colocalization between target proteins and specific markers of differential cell compartments provides an efficient approach to studying protein traffic. In this chapter, we describe an automated method to denoise confocal microscopy images and assess the colocalization of their stainings using ImageJ software.

The calmodulin-binding tetraleucine motif of KCNE4 is responsible for association with Kv1.3.

The voltage-dependent potassium (Kv) channel Kv1.3 regulates leukocyte proliferation, activation, and apoptosis, and altered expression of this channel is linked to autoimmune diseases. Thus, the fine-tuning of Kv1.