PerformLyte—A Prodosomed PL425 PEC Phytoceutical-Enriched Electrolyte Supplement—Supports Nutrient Repletion, Healthy Blood pH, Neuromuscular Synergy, Cellular and Metabolic Homeostasis
Abhai Kumar, Debasis Bagchi in Antioxidants and Functional Foods for Neurodegenerative Disorders, 2021
Chloride: In human physiology, chloride ions help in the maintenance of regulating fluid balance, blood volume, electrolyte homeostasis, intracellular and extracellular fluid homeostasis, blood pressure, preservation of electrical neutrality, and pH of body fluids in a human body.125–127 The chloride ion is an important biomarker for a vast range of clinical conditions and, as a routine practice, is analytically determined in the sweat, urine, feces, and blood. Following intake of edible salt from diverse food sources, a human body gets chloride, which is absorbed in the intestine, while the excess amount gets excreted in the urine.125–128 However, excessive chloride levels indicate serious metabolic disorders, including metabolic acidosis or alkalosis, and a disruption in chloride channel expression and function, leading to multiple diseases and disorders in diverse organs.126–128
Respiratory system
Jagdish M. Gupta, John Beveridge in MCQs in Paediatrics, 2020
7.27. In the lung of cystic fibrosis (CF) patientsthere is a failure of chloride and water secretion into the respiratory mucus layer.there is excessive reabsorption of sodium from the respiratory mucus layer.all chloride channels are CF transmembrane regulator dependent.the transport defect can be overcome by administration of beta-sympathomimetics.the transport defect is most severe in those patients with two delta 508 genes.
Cell structure, function and adaptation
C. Simon Herrington in Muir's Textbook of Pathology, 2020
The half-life of cellular proteins varies from seconds to months or years. The haemoglobin protein in red blood cells lasts for more than 100 days before the cell is removed from the circulation. The regulation of cellular proteins is a complex and important process for cell viability and function. If damaged protein accumulates it may inhibit normal protein function or injure the cell directly. Genetic abnormalities resulting in abnormal proteins are implicated in many diseases. In cystic fibrosis (see Chapter 8) a transmembrane chloride channel is dysfunctional, and this results in abnormal mucus secretion that leads to the phenotype seen clinically. In storage diseases, such as α1-antitrypsin disease, an abnormal protein is produced that cannot be efficiently secreted from the cell. The protein accumulates and can cause damage to the liver cells resulting in hepatitis, which may progress to cirrhosis (see Chapter 11). In addition, the absence of functional anti-protease in plasma leads to an increased risk of emphysema developing in the lungs (see Chapter 8). Mutation of tumour-suppressor genes can result in the formation of proteins with abnormal folding characteristics. Sometimes these inhibit the function of the corresponding normal protein (a dominant negative effect) and so contribute to the pathogenesis of cancer (see Chapter 6). Normally, damaged protein is marked for degradation by being bound to a carrier protein called ubiquitin, a process known as ubiquitination. This ubiquitinated protein is then removed from the cellular pool and degraded in the proteasome.
Emerging medicines to improve the basic defect in cystic fibrosis
Published in Expert Opinion on Emerging Drugs, 2022
Isabelle Fajac, Isabelle Sermet-Gaudelus
The CFTR protein is expressed at the apical membrane of many epithelial cells with direct relationships between abnormal expression or function, and CF pathology. When open or activated, the CFTR channel allows passive diffusion of chloride and bicarbonate ions down their electrochemical gradient. It has also many other roles such as inhibition of sodium transport through the epithelial sodium channel and regulation of other chloride channels [8]. CFTR mutations lead to a loss of CFTR activity due to either reduced quantity or impaired function of the protein. In the airways, a defective CFTR protein leads to impaired mucociliary clearance, infection and inflammation, bronchiectasis, and respiratory failure. To date, around 2,000 CFTR mutations have been described and around 250 variants have evidence supporting a disease-causing effect [9]. In the last decade, very innovative drugs called CFTR modulators that improve the defective CFTR protein function have been approved for marketing in patients with CF.
Persistent diarrhoea: current knowledge and novel concepts
Published in Paediatrics and International Child Health, 2019
Robert H. J. Bandsma, Kamran Sadiq, Zulfiqar A. Bhutta
Absorption of sodium and chloride ions forms a fundamental mechanism for absorption of fluids. Transporters of the solute carrier 9 (SLC9) family of sodium–hydrogen exchangers and the SLC26 family of anion exchangers are responsible for this process. Hereafter, these ions can be exported across the basolateral membrane via the Na+/K+ ATPase and potassium chloride co-transporter [17]. In the distal colon specifically, sodium ions can also be absorbed through the heterotrimeric epithelial sodium channel [18]. Bacteria such as campylobacter or their enterotoxins have been shown to inhibit the activity of these transporters, thereby inducing diarrhoea [19–21]. Chloride is also actively secreted via the cystic fibrosis transmembrane conductance regulator chloride channels and calcium-activated chloride channels. In cholera or rotavirus infection, stimulation of active chloride secretion is a direct cause of diarrhoea [22,23]. Specific aetiological and contributing factors are discussed in the following paragraphs.
The slow light and dark oscillation of the clinical electro‐oculogram
Published in Clinical and Experimental Optometry, 2018
Paul A Constable, David Ngo
There is now strong evidence for the light oscillation being the result of changes in basolateral chloride conductance that is regulated by bestrophinn‐12013 and the L‐type Ca2+2011 channel that responds to a change in light intensity producing the light peak and subsequent oscillation. The nature of the dark oscillation is open to speculation and may result from non‐photic basal changes in chloride conductance. Some potential chloride channels could be considered. One is the cystic fibrosis transmembrane conductance regulator that has been proposed to contribute to the light peak.2005 However, the dark trough and light peak and fast oscillation are not affected in individuals with cystic fibrosis, suggesting that the cystic fibrosis transmembrane conductance regulator is not directly involved in the formation of these oscillations.2006
Related Knowledge Centers
- Chloride
- Protein Dimer
- Resting Potential
- Transmembrane Domain
- Ion Channel
- Voltage-Gated Ion Channel
- Ligand-Gated Ion Channel
- Calcium-Dependent Chloride Channel
- Sequence Homology
- Cbs Domain