We examine the autocrine activity of glycosyl inositol phosphate (InP-gly) on thyroid metabolism. The cAMP accumulation promoted by thyrotropin (TSH) or forskolin was modulated by InP-gly, stimulated by the lowest tested concentration (10(-8) M) and progressively inhibited by higher concentrations. Iodide uptake and iodine organification were decreased in a concentration-dependent manner by InP-gly alone, or in the presence of TSH. The IAP component of pertussis toxin blocked the inhibitory action of InP-gly on cAMP accumulation by reconstituted thyroid follicles (RTF), suggesting the participation of Gi protein. But the same treatment with IAP was without effect on iodine metabolism, suggesting that there is a second target for InP-gly, more distal than Gi protein, or coupled to another G protein which is insensitive to the toxin.
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http://dx.doi.org/10.1016/0898-6568(92)90085-m | DOI Listing |
Plant Physiol
January 2025
State Key Laboratory of Biocontrol, Guangdong Provincial Key Laboratory of Plant Stress Biology, School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, P R China.
Osmotic stress caused by drought, salinity, or cold conditions is an important abiotic factor that decreases membrane integrity and causes cell death, thus decreasing plant growth and productivity. Remodeling cell membrane composition via lipid turnover can counter the loss of membrane integrity and cell death caused by osmotic stress. Sphingolipids are important components of eukaryotic membrane systems; however, how sphingolipids participate in plant responses to osmotic stress remains unclear.
View Article and Find Full Text PDFJ Carbohydr Chem
April 2024
Department of Chemistry, University of Florida, 214 Leigh Hall, Gainesville, FL 32611, USA.
Glycosylphosphatidylinositol (GPI) anchors contain a unique α-D-glucosamine-(1→6)--inositol [αGlcN(1,6)Ins] motif in their conserved core structure. To facilitate investigations of the functional roles of this structural motif, two GPI analogues containing unnatural βGlcN(1,6)Ins, instead of αGlcN(1,6)Ins, and an alkyne group at different positions of the GPI core were designed and synthesized. To this end, an orthogonally protected pseudopentasaccharide derivative of GPIs with the βGlcN(1,6)Ins motif was convergently constructed via [3+2] glycosylation and used as the common intermediate to prepare both GPI analogues by streamlined synthetic protocols.
View Article and Find Full Text PDFCells
December 2024
Key Laboratory of Marine Drugs (Ministry of Education), Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, China.
CD24, a highly sialylated glycosyl-phosphatidyl-inositol (GPI) cell surface protein that interacts with sialic acid-binding immunoglobulin-like lectins (Siglecs), serves as an innate immune checkpoint and plays a crucial role in inflammatory diseases and tumor progression. Recently, cytoplasmic CD24 has been observed in samples from patients with cancer. However, whether sialylation governs the subcellular localization of CD24 in cancer remains unclear, and the impact of CD24 expression and localization on the clinical prognosis of cancer remains controversial.
View Article and Find Full Text PDFMetallomics
January 2025
Department of Environmental and Physical Sciences, Faculty of Science, Concordia University of Edmonton, Edmonton, Alberta, Canada.
Non-enzymatic glycation is the chemical reaction between the amine group of an amino acid and the carbonyl group of a reducing sugar. The final products of this reaction, advanced glycation end-products (AGEs), are known to play a key role in aging and many chronic diseases. The kinetics of the AGE formation reaction depends on several factors, including pH, temperature, and the presence of prooxidant metals, such as iron and copper.
View Article and Find Full Text PDFBJOG
December 2024
Fetal Medicine Unit, St George's University Hospital, London, UK.
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