Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/s0065-3233(03)63010-x | DOI Listing |
J Cell Sci
January 2025
Program in Molecular Medicine, University of Massachusetts Chan Medical School, Suite 213 Biotech II, 373 Plantation Street, Worcester MA 01605, USA.
In humans, inositol polyphosphate-5-phosphatase e (INPP5E) mutations cause retinal degeneration as part of Joubert and MORM syndromes and can also cause non-syndromic blindness. In mice, mutations cause a spectrum of brain, kidney, and other anomalies and prevent the formation of photoreceptor outer segments. To further explore the function of Inpp5e in photoreceptors, we generated conditional and inducible knockouts of mouse Inpp5e where the gene was deleted either during outer segment formation or after outer segments were fully formed.
View Article and Find Full Text PDFCurr Pharm Des
January 2025
Department of Physiology, Medical School, Selcuk University, Konya, Turkey.
Introduction: Brain ischemia-reperfusion can cause serious and irreversible health problems. Recent studies have suggested that certain flavonoids may help stabilize the correctly folded structure of the visual photoreceptor protein rhodopsin and offset the deleterious effect of retinitis pigmentosa mutations.
Objective: The current study aimed to determine the effect of 3',4'-Dihydroxyflavonol (DiOHF) supplementation for 1 week on lipid peroxidation in the retina tissue following focal brain ischemia-reperfusion in rats.
Int J Mol Sci
January 2025
Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Sequences and three-dimensional structures of the four vertebrate arrestins are very similar, yet in sharp contrast to other subtypes, arrestin-1 demonstrates exquisite selectivity for the active phosphorylated form of its cognate receptor, rhodopsin. The N-terminus participates in receptor binding and serves as the anchor of the C-terminus, the release of which facilitates arrestin transition into a receptor-binding state. We tested the effects of substitutions of fourteen residues in the N-terminus of arrestin-1 on the binding to phosphorylated and unphosphorylated light-activated rhodopsin of wild-type protein and its enhanced mutant with C-terminal deletion that demonstrates higher binding to both functional forms of rhodopsin.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Departamento de Química Analítica, Química Física e Ingeniería Química, Universidad de Alcalá, Alcalá de Henares, Madrid E-28871, Spain.
The retinal Schiff base is a chromophore of significant biological relevance, as it is responsible for capturing sunlight in rhodopsins, which are photoactive proteins found in various living organisms. Additionally, this chromophore is subjected to various mechanical forces in different proteins, which alter its structure and, consequently, its properties. To thoroughly understand the mechanical response limits of the retinal excitation energy, a simple first-order formalism has been developed to quantify the chromophore's optimal mechanical response to applied external forces (on the order of tens of pN).
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Shengjing Hospital of China Medical University, 36 Sanhao Street, Shenyang, Liaoning Province, China. Electronic address:
G protein-coupled receptor 84 (GPR84), a member of the highly conserved rhodopsin-like superfamily, represents a promising target for therapeutic drug development. Its distinctive expression profiles in adipocytes, gut endocrine cells, and various myeloid immune cells underscore its critical roles in fundamental physiological processes, particularly in metabolic regulation and immune responses. Over the past two decades, emerging research has demonstrated that GPR84 regulates immune cell chemotaxis, phagocytosis, and inflammatory responses, playing a pivotal role in metabolic disorders, inflammatory diseases, and organ fibrosis.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!