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Journal articles on the topic 'Amino acids sensing'

Author: Grafiati

Published: 26 October 2024

Last updated: 31 July 2025

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1

Tang, Lei. "Sensing proteinogenic amino acids." Nature Methods 17, no. 2 (2020): 126. http://dx.doi.org/10.1038/s41592-020-0741-z.

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Poulsen, P., B. Wu, R. F. Gaber, Kim Ottow, H. A. Andersen, and M. C. Kielland-Brandt. "Amino acid sensing by Ssy1." Biochemical Society Transactions 33, no. 1 (2005): 261–64. http://dx.doi.org/10.1042/bst0330261.

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Saccharomyces cerevisiae senses extracellular amino acids using two members of the family of amino acid transporters, Gap1 or Ssy1; aspects of the latter are reviewed here. Despite resemblance with bona fide transporters, Ssy1 appears unable to facilitate transport. Exposure of yeast to amino acids results in Ssy1-dependent transcriptional induction of several genes, in particular some encoding amino acid transporters. Amino acids differ strongly in their potency, leucine being the most potent one known. Using a selection system in which potassium uptake was made dependent on amino acid signal

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Conigrave, A. D., H. C. Mun, and S. C. Brennan. "Physiological significance of L-amino acid sensing by extracellular Ca2+-sensing receptors." Biochemical Society Transactions 35, no. 5 (2007): 1195–98. http://dx.doi.org/10.1042/bst0351195.

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The calcium-sensing receptor is a multimodal, multimetabolic sensor that mediates the feedback-dependent control of whole body calcium metabolism. Remarkably, in addition to its role in Ca2+o (extracellular Ca2+) sensing, the CaR (Ca2+-sensing receptor) also responds to L-amino acids. L-amino acids appear to activate, predominantly, a signalling pathway coupled with intracellular Ca2+ mobilization, require a threshold concentration of Ca2+o for efficacy and sensitize the receptor to activation by Ca2+o. Here, we review the evidence that the CaR, like other closely related members of the class

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Ray, L. B. "Sensing amino acids at the lysosome." Science 347, no. 6218 (2015): 141–43. http://dx.doi.org/10.1126/science.347.6218.141-p.

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Ray, L. Bryan. "Sensing Amino Acids at the Lysosome." Science Signaling 8, no. 359 (2015): ec12-ec12. http://dx.doi.org/10.1126/scisignal.aaa6512.

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Zhou, Yanxiu, Bin Yu, and Kalle Levon. "Potentiometric Sensing of Chiral Amino Acids." Chemistry of Materials 15, no. 14 (2003): 2774–79. http://dx.doi.org/10.1021/cm030060e.

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Lynch, Ciarán C., Zeus A. De los Santos, and Christian Wolf. "Chiroptical sensing of unprotected amino acids, hydroxy acids, amino alcohols, amines and carboxylic acids with metal salts." Chemical Communications 55, no. 44 (2019): 6297–300. http://dx.doi.org/10.1039/c9cc02525a.

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Optical chirality sensing of unprotected amino acids, hydroxy acids, amino alcohols, amines and carboxylic acids based on a practical mix-and-measure protocol with readily available copper, iron, palladium, manganese, cerium or rhodium salts is demonstrated.

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Shi, Wei-Nan, Fei Fan, Tian-Rui Zhang, Jia-Yue Liu, Xiang-Hui Wang, and ShengJiang Chang. "Terahertz phase shift sensing and identification of a chiral amino acid based on a protein-modified metasurface through the isoelectric point and peptide bonding." Biomedical Optics Express 14, no. 3 (2023): 1096. http://dx.doi.org/10.1364/boe.484181.

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The efficient sensing of amino acids, especially the distinction of their chiral enantiomers, is important for biological, chemical, and pharmaceutical research. In this work, a THz phase shift sensing method was performed for amino acid detection based on a polarization-dependent electromagnetically induced transparency (EIT) metasurface. More importantly, a method for binding the specific amino acids to the functional proteins modified on the metasurface was developed based on the isoelectric point theory so that the specific recognition for Arginine (Arg) was achieved among the four differe

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Gaber, Richard F., Kim Ottow, Helge A. Andersen, and Morten C. Kielland-Brandt. "Constitutive and Hyperresponsive Signaling by Mutant Forms of Saccharomyces cerevisiae Amino Acid Sensor Ssy1." Eukaryotic Cell 2, no. 5 (2003): 922–29. http://dx.doi.org/10.1128/ec.2.5.922-929.2003.

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ABSTRACT Sensing of extracellular amino acids results in transcriptional induction of amino acid permease genes in yeast. Ssy1, a membrane protein resembling amino acid permeases, is required for signaling but is apparently unable to transport amino acids and is thus believed to be a sensor. By using a novel genetic screen in which potassium uptake was made dependent on amino acid signaling, we obtained gain-of-function mutations in SSY1. Some alleles confer inducer-independent signaling; others increase the apparent affinity for inducers. The results reveal that amino acid transport is not re

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Lushchak, Oleh. "Amino Acids: Sensing and Implication into Aging." Journal of Vasyl Stefanyk Precarpathian National University 2, no. 1 (2015): 51–60. http://dx.doi.org/10.15330/jpnu.2.1.51-60.

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An ability to sense and respond to nutrient availability is an important requisite for life.Nutrient limitation is among main factors to influence the evolution of most cellular processes.Different pathways that sense intracellular and extracellular levels of carbohydtrates, amino acids,lipids, and intermediate metabolites are integrated and coordinated at the organismal levelthrough neuronal and humoral signals. During food abundance, nutrient-sensing pathwaysengage anabolism and storage, whereas limitation triggers the mechanisms, such as themobilization of internal stores including through

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YAO, SHANG J., WEIJIAN XU, TERRI-LYNN DAY, JOHN F. PATZER, and SIDNEY K. WOLFSON. "Interference of Glucose Sensing by Amino Acids." ASAIO Journal 40, no. 1 (1994): 33–40. http://dx.doi.org/10.1097/00002480-199401000-00007.

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YAO, SHANG J., WEIJIAN XU, TERRI-LYNN DAY, JOHN F. PATZER, and SIDNEY K. WOLFSON. "Interference of Glucose Sensing by Amino Acids." Asaio journal 40, SUPPLEMENT 1 (1994): 33???40. http://dx.doi.org/10.1097/00002480-199401001-00007.

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Yao, Shang J., Weijian Xu, Terri-Lynn Day, John F. Patzer, and Sidney K. Wolfson. "Interference of Glucose Sensing by Amino Acids." ASAIO Journal 40, no. 1 (1994): 33–40. http://dx.doi.org/10.1097/00002480-199440010-00007.

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Dong, Jing, Xiao-Yao Dao, Xiao-Yu Zhang, Xiu-Du Zhang, and Wei-Yin Sun. "Sensing Properties of NH2-MIL-101 Series for Specific Amino Acids via Turn-On Fluorescence." Molecules 26, no. 17 (2021): 5336. http://dx.doi.org/10.3390/molecules26175336.

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Metal–organic frameworks (MOFs) have been demonstrated to be desired candidates for sensing definite species owing to their tunable composition, framework structure and functionality. In this work, the NH2-MIL-101 series was utilized for sensing specific amino acids. The results show that cysteine (Cys) can significantly enhance the fluorescence emission of NH2-MIL-101-Fe suspended in water, while NH2-MIL-101-Al exhibits the ability to sense lysine (Lys), arginine (Arg) and histidine (His) in aqueous media via turn-on fluorescence emission. Titration experiments ensure that NH2-MIL-101-Fe and

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Revanappa, Santhosh Kumar, Isha Soni, Manjappa Siddalinganahalli, Gururaj Kudur Jayaprakash, Roberto Flores-Moreno, and Chandrashekar Bananakere Nanjegowda. "A Fukui Analysis of an Arginine-Modified Carbon Surface for the Electrochemical Sensing of Dopamine." Materials 15, no. 18 (2022): 6337. http://dx.doi.org/10.3390/ma15186337.

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Amino acid-modified carbon interfaces have huge applications in developing electrochemical sensing applications. Earlier reports suggested that the amine group of amino acids acted as an oxidation center at the amino acid-modified electrode interface. It was interesting to locate the oxidation centers of amino acids in the presence of guanidine. In the present work, we modeled the arginine-modified carbon interface and utilized frontier molecular orbitals and analytical Fukui functions based on the first principle study computations to analyze arginine-modified CPE (AMCPE) at a molecular level

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Mun, Hee-Chang, Alison H. Franks, Emma L. Culverston, Karen Krapcho, Edward F. Nemeth, and Arthur D. Conigrave. "The Venus Fly Trap Domain of the Extracellular Ca2+-sensing Receptor Is Required for l-Amino Acid Sensing." Journal of Biological Chemistry 279, no. 50 (2004): 51739–44. http://dx.doi.org/10.1074/jbc.m406164200.

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We previously demonstrated that the human calcium-sensing receptor (CaR) is allosterically activated byl-amino acids (Conigrave, A. D., Quinn, S. J., and Brown, E. M. (2000)Proc. Natl. Acad. Sci. U. S. A.97, 4814–4819). However, the domain-based location of amino acid binding has been uncertain. We now show that the Venus Fly Trap (VFT) domain of CaR, but none of its other major domains, is required for amino acid sensing. Several constructs were informative when expressed in HEK293 cells. First, the wild-type CaR exhibited allosteric activation byl-amino acids as previously observed. Second,

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Ljungdahl, Per O. "Amino-acid-induced signalling via the SPS-sensing pathway in yeast." Biochemical Society Transactions 37, no. 1 (2009): 242–47. http://dx.doi.org/10.1042/bst0370242.

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Yeast cells rely on the SPS-sensing pathway to respond to extracellular amino acids. This nutrient-induced signal transduction pathway regulates gene expression by controlling the activity of two redundant transcription factors: Stp1 and Stp2. These factors are synthesized as latent cytoplasmic proteins with N-terminal regulatory domains. Upon induction by extracellular amino acids, the plasma membrane SPS-sensor catalyses an endoproteolytic processing event that cleaves away the regulatory N-terminal domains. The shorter forms of Stp1 and Stp2 efficiently target to the nucleus, where they bin

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Pettiwala, Aafrin M., and Prabhat K. Singh. "Optical Sensors for Detection of Amino Acids." Current Medicinal Chemistry 25, no. 19 (2018): 2272–90. http://dx.doi.org/10.2174/0929867324666171106161410.

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Background: Amino acids are crucially involved in a myriad of biological processes. Any aberrant changes in physiological level of amino acids often manifest in common metabolic disorders, serious neurological conditions and cardiovascular diseases. Thus, devising methods for detection of trace amounts of amino acids becomes highly elemental to their efficient clinical diagnosis. Recently, the domain of developing optical sensors for detection of amino acids has witnessed significant activity which is the focus of the current review article. Methods: We undertook a detailed search of the peer-

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Wauson, Eric M., Andrés Lorente-Rodríguez, and Melanie H. Cobb. "Minireview: Nutrient Sensing by G Protein-Coupled Receptors." Molecular Endocrinology 27, no. 8 (2013): 1188–97. http://dx.doi.org/10.1210/me.2013-1100.

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G protein-coupled receptors (GPCRs) are membrane proteins that recognize molecules in the extracellular milieu and transmit signals inside cells to regulate their behaviors. Ligands for many GPCRs are hormones or neurotransmitters that direct coordinated, stereotyped adaptive responses. Ligands for other GPCRs provide information to cells about the extracellular environment. Such information facilitates context-specific decision making that may be cell autonomous. Among ligands that are important for cellular decisions are amino acids, required for continued protein synthesis, as metabolic sta

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Wang, Yu, Rashmi Chandra, Leigh Ann Samsa, et al. "Amino acids stimulate cholecystokinin release through the Ca2+-sensing receptor." American Journal of Physiology-Gastrointestinal and Liver Physiology 300, no. 4 (2011): G528—G537. http://dx.doi.org/10.1152/ajpgi.00387.2010.

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Cholecystokinin (CCK) is produced by discrete endocrine cells in the proximal small intestine and is released following the ingestion of food. CCK is the primary hormone responsible for gallbladder contraction and has potent effects on pancreatic secretion, gastric emptying, and satiety. In addition to fats, digested proteins and aromatic amino acids are major stimulants of CCK release. However, the cellular mechanism by which amino acids affect CCK secretion is unknown. The Ca2+-sensing receptor (CaSR) that was originally identified on parathyroid cells is not only sensitive to extracellular

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Dato, Serena, Eneida Hoxha, Paolina Crocco, Francesca Iannone, Giuseppe Passarino, and Giuseppina Rose. "Amino acids and amino acid sensing: implication for aging and diseases." Biogerontology 20, no. 1 (2018): 17–31. http://dx.doi.org/10.1007/s10522-018-9770-8.

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Pradhan, Tuhin, Hyo Sung Jung, Joo Hee Jang, Tae Woo Kim, Chulhun Kang, and Jong Seung Kim. "Chemical sensing of neurotransmitters." Chem. Soc. Rev. 43, no. 13 (2014): 4684–713. http://dx.doi.org/10.1039/c3cs60477b.

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This review focuses on the chemosensors for neurotransmitters published for the last 12 years, covering biogenic amines (dopamine, epinephrine, norepinephrine, serotonin, histamine and acetylcholine), amino acids (glutamate, aspartate, GABA, glycine and tyrosine), and adenosine.

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Lutt, Nanticha, and Jacob O. Brunkard. "Amino Acid Signaling for TOR in Eukaryotes: Sensors, Transducers, and a Sustainable Agricultural fuTORe." Biomolecules 12, no. 3 (2022): 387. http://dx.doi.org/10.3390/biom12030387.

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Eukaryotic cells monitor and regulate metabolism through the atypical protein kinase target of rapamycin (TOR) regulatory hub. TOR is activated by amino acids in animals and fungi through molecular signaling pathways that have been extensively defined in the past ten years. Very recently, several studies revealed that TOR is also acutely responsive to amino acid metabolism in plants, but the mechanisms of amino acid sensing are not yet established. In this review, we summarize these discoveries, emphasizing the diversity of amino acid sensors in human cells and highlighting pathways that are i

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Silao, Fitz Gerald S., and Per O. Ljungdahl. "Amino Acid Sensing and Assimilation by the Fungal Pathogen Candida albicans in the Human Host." Pathogens 11, no. 1 (2021): 5. http://dx.doi.org/10.3390/pathogens11010005.

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Nutrient uptake is essential for cellular life and the capacity to perceive extracellular nutrients is critical for coordinating their uptake and metabolism. Commensal fungal pathogens, e.g., Candida albicans, have evolved in close association with human hosts and are well-adapted to using diverse nutrients found in discrete host niches. Human cells that cannot synthesize all amino acids require the uptake of the “essential amino acids” to remain viable. Consistently, high levels of amino acids circulate in the blood. Host proteins are rich sources of amino acids but their use depends on prote

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Meng, Delong, Qianmei Yang, Huanyu Wang, et al. "Glutamine and asparagine activate mTORC1 independently of Rag GTPases." Journal of Biological Chemistry 295, no. 10 (2020): 2890–99. http://dx.doi.org/10.1074/jbc.ac119.011578.

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Nutrient sensing by cells is crucial, and when this sensing mechanism is disturbed, human disease can occur. mTOR complex 1 (mTORC1) senses amino acids to control cell growth, metabolism, and autophagy. Leucine, arginine, and methionine signal to mTORC1 through the well-characterized Rag GTPase signaling pathway. In contrast, glutamine activates mTORC1 through a Rag GTPase–independent mechanism that requires ADP-ribosylation factor 1 (Arf1). Here, using several biochemical and genetic approaches, we show that eight amino acids filter through the Rag GTPase pathway. Like glutamine, asparagine s

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Brennan, Sarah C., Thomas S. Davies, Martin Schepelmann, and Daniela Riccardi. "Emerging roles of the extracellular calcium-sensing receptor in nutrient sensing: control of taste modulation and intestinal hormone secretion." British Journal of Nutrition 111, S1 (2014): S16—S22. http://dx.doi.org/10.1017/s0007114513002250.

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The extracellular Ca-sensing receptor (CaSR) is a sensor for a number of key nutrients within the body, including Ca ions (Ca2+) and l-amino acids. The CaSR is expressed in a number of specialised cells within the gastrointestinal (GI) tract, and much work has been done to examine CaSR's role as a nutrient sensor in this system. This review article examines two emerging roles for the CaSR within the GI tract – as a mediator of kokumi taste modulation in taste cells and as a regulator of dietary hormone release in response to l-amino acids in the intestine.

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Liu, Chunchen, Linbao Ji, Jinhua Hu, et al. "Functional Amino Acids and Autophagy: Diverse Signal Transduction and Application." International Journal of Molecular Sciences 22, no. 21 (2021): 11427. http://dx.doi.org/10.3390/ijms222111427.

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Functional amino acids provide great potential for treating autophagy-related diseases by regulating autophagy. The purpose of the autophagy process is to remove unwanted cellular contents and to recycle nutrients, which is controlled by many factors. Disordered autophagy has been reported to be associated with various diseases, such as cancer, neurodegeneration, aging, and obesity. Autophagy cannot be directly controlled and dynamic amino acid levels are sufficient to regulate autophagy. To date, arginine, leucine, glutamine, and methionine are widely reported functional amino acids that regu

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Feng, Haichao, Nan Zhang, Wenbin Du, et al. "Identification of Chemotaxis Compounds in Root Exudates and Their Sensing Chemoreceptors in Plant-Growth-Promoting Rhizobacteria Bacillus amyloliquefaciens SQR9." Molecular Plant-Microbe Interactions® 31, no. 10 (2018): 995–1005. http://dx.doi.org/10.1094/mpmi-01-18-0003-r.

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Chemotaxis-mediated response to root exudates, initiated by sensing-specific ligands through methyl-accepting chemotaxis proteins (MCP), is very important for root colonization and beneficial functions of plant-growth-promoting rhizobacteria (PGPR). Systematic identification of chemoattractants in complex root exudates and their sensing chemoreceptors in PGPR is helpful for enhancing their recruitment and colonization. In this study, 39 chemoattractants and 5 chemorepellents, including amino acids, organic acids, and sugars, were identified from 98 tested components of root exudates for the we

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Zou, Jia-Ming, Qiang-Sheng Zhu, Hui Liang, Hai-Lin Lu, Xu-Fang Liang, and Shan He. "Lysine Deprivation Regulates Npy Expression via GCN2 Signaling Pathway in Mandarin Fish (Siniperca chuatsi)." International Journal of Molecular Sciences 23, no. 12 (2022): 6727. http://dx.doi.org/10.3390/ijms23126727.

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Regulation of food intake is associated with nutrient-sensing systems and the expression of appetite neuropeptides. Nutrient-sensing systems generate the capacity to sense nutrient availability to maintain energy and metabolism homeostasis. Appetite neuropeptides are prominent factors that are essential for regulating the appetite to adapt energy status. However, the link between the expression of appetite neuropeptides and nutrient-sensing systems remains debatable in carnivorous fish. Here, with intracerebroventricular (ICV) administration of six essential amino acids (lysine, methionine, tr

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He, Fang, Chenlu Wu, Pan Li, et al. "Functions and Signaling Pathways of Amino Acids in Intestinal Inflammation." BioMed Research International 2018 (2018): 1–13. http://dx.doi.org/10.1155/2018/9171905.

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Intestine is always exposed to external environment and intestinal microorganism; thus it is more sensitive to dysfunction and dysbiosis, leading to intestinal inflammation, such as inflammatory bowel disease (IBD), irritable bowel syndrome (IBS), and diarrhea. An increasing number of studies indicate that dietary amino acids play significant roles in preventing and treating intestinal inflammation. The review aims to summarize the functions and signaling mechanisms of amino acids in intestinal inflammation. Amino acids, including essential amino acids (EAAs), conditionally essential amino aci

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Lee, Heather J., Hee-Chang Mun, Narelle C. Lewis, et al. "Allosteric activation of the extracellular Ca2+-sensing receptor by L-amino acids enhances ERK1/2 phosphorylation." Biochemical Journal 404, no. 1 (2007): 141–49. http://dx.doi.org/10.1042/bj20061826.

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The calcium-sensing receptor (CaR) mediates feedback control of Ca2+o (extracellular Ca2+) concentration. Although the mechanisms are not fully understood, the CaR couples to several important intracellular signalling enzymes, including PI-PLC (phosphoinositide-specific phospholipase C), leading to Ca2+i (intracellular Ca2+) mobilization, and ERK1/2 (extracellular-signal-regulated kinase 1/2). In addition to Ca2+o, the CaR is activated allosterically by several subclasses of L-amino acids, including the aromatics L-phenylalanine and L-tryptophan. These amino acids enhance the Ca2+o-sensitivity

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Wu, Zhihui, Jinghui Heng, Min Tian, et al. "Amino acid transportation, sensing and signal transduction in the mammary gland: key molecular signalling pathways in the regulation of milk synthesis." Nutrition Research Reviews 33, no. 2 (2020): 287–97. http://dx.doi.org/10.1017/s0954422420000074.

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AbstractThe mammary gland, a unique exocrine organ, is responsible for milk synthesis in mammals. Neonatal growth and health are predominantly determined by quality and quantity of milk production. Amino acids are crucial maternal nutrients that are the building blocks for milk protein and are potential energy sources for neonates. Recent advances made regarding the mammary gland further demonstrate that some functional amino acids also regulate milk protein and fat synthesis through distinct intracellular and extracellular pathways. In the present study, we discuss recent advances in the role

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Kordasht, Houman Kholafazad, Mohammad Hasanzadeh, Farzad Seidi, and Parastoo Mohammad Alizadeh. "Poly (amino acids) towards sensing: Recent progress and challenges." TrAC Trends in Analytical Chemistry 140 (July 2021): 116279. http://dx.doi.org/10.1016/j.trac.2021.116279.

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Abdullah, Mahmud O., Run X. Zeng, Chelsea L. Margerum, et al. "Mitochondrial hyperfusion via metabolic sensing of regulatory amino acids." Cell Reports 40, no. 7 (2022): 111198. http://dx.doi.org/10.1016/j.celrep.2022.111198.

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Smajilovic, Sanela, Petrine Wellendorph, and Hans Brauner-Osborne. "Promiscuous Seven Transmembrane Receptors Sensing L-α-amino Acids." Current Pharmaceutical Design 20, no. 16 (2014): 2693–702. http://dx.doi.org/10.2174/13816128113199990576.

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Conigrave, Arthur D., Hee-Chang Mun, and Hiu-Chuen Lok. "Aromatic l-Amino Acids Activate the Calcium-Sensing Receptor." Journal of Nutrition 137, no. 6 (2007): 1524S—1527S. http://dx.doi.org/10.1093/jn/137.6.1524s.

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Ishida, Hikaru, Norihisa Yasui, and Atsuko Yamashita. "Chemical range recognized by the ligand-binding domain in a representative amino acid-sensing taste receptor, T1r2a/T1r3, from medaka fish." PLOS ONE 19, no. 3 (2024): e0300981. http://dx.doi.org/10.1371/journal.pone.0300981.

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Taste receptor type 1 (T1r) proteins are responsible for recognizing nutrient chemicals in foods. In humans, T1r2/T1r3 and T1r1/T1r3 heterodimers serve as the sweet and umami receptors that recognize sugars or amino acids and nucleotides, respectively. T1rs are conserved among vertebrates, and T1r2a/T1r3 from medaka fish is currently the only member for which the structure of the ligand-binding domain (LBD) has been solved. T1r2a/T1r3 is an amino acid receptor that recognizes various l-amino acids in its LBD as observed with other T1rs exhibiting broad substrate specificities. Nevertheless, th

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Kraidlova, Lucie, Griet Van Zeebroeck, Patrick Van Dijck, and Hana Sychrová. "The Candida albicans GAP Gene Family Encodes Permeases Involved in General and Specific Amino Acid Uptake and Sensing." Eukaryotic Cell 10, no. 9 (2011): 1219–29. http://dx.doi.org/10.1128/ec.05026-11.

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ABSTRACTTheSaccharomyces cerevisiaegeneral amino acid permease Gap1 (ScGap1) not only mediates the uptake of most amino acids but also functions as a receptor for the activation of protein kinase A (PKA). Fungal pathogens can colonize different niches in the host, each containing various levels of different amino acids and sugars. TheCandida albicansgenome contains six genes homologous to theS. cerevisiae GAP1. The expression of these six genes inS. cerevisiaeshowed that the products of all sixC. albicansgenes differ in their transport capacities.C. albicansGap2 (CaGap2) is the true orthologue

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Yoon, Mee-Sup, Guangwei Du, Jonathan M. Backer, Michael A. Frohman, and Jie Chen. "Class III PI-3-kinase activates phospholipase D in an amino acid–sensing mTORC1 pathway." Journal of Cell Biology 195, no. 3 (2011): 435–47. http://dx.doi.org/10.1083/jcb.201107033.

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The rapamycin-sensitive mammalian target of rapamycin (mTOR) complex, mTORC1, regulates cell growth in response to mitogenic signals and amino acid availability. Phospholipase D (PLD) and its product, phosphatidic acid, have been established as mediators of mitogenic activation of mTORC1. In this study, we identify a novel role for PLD1 in an amino acid–sensing pathway. We find that amino acids activate PLD1 and that PLD1 is indispensable for amino acid activation of mTORC1. Activation of PLD1 by amino acids requires the class III phosphatidylinositol 3-kinase hVps34, which stimulates PLD1 act

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Sriramulu, Dinesh Diraviam. "Amino Acids Enhance Adaptive Behaviour of Pseudomonas Aeruginosa in the Cystic Fibrosis Lung Environment." Microbiology Insights 3 (January 2010): MBI.S4694. http://dx.doi.org/10.4137/mbi.s4694.

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Sputum of cystic fibrosis (CF) patients is a nutrient-rich environment. Higher amino acid content of CF sputum compared to normal sputum plays a major role in the CF-specific phenotype of P. aeruginosa. Presence of amino acids in the sputum-like environment influenced P. aeruginosa quorum-sensing activity and the formation of an unknown exopolysaccharide in the biofilm. Lipopolysaccharides isolated from P. aeruginosa grown in the presence of amino acids enhanced the release of cytokine IL-8 by human kidney and lung epithelial cells. The results of this study provide additional evidence on the

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Conigrave, Arthur D., and Edward M. Brown. "Taste Receptors in the Gastrointestinal Tract II.l-Amino acid sensing by calcium-sensing receptors: implications for GI physiology." American Journal of Physiology-Gastrointestinal and Liver Physiology 291, no. 5 (2006): G753—G761. http://dx.doi.org/10.1152/ajpgi.00189.2006.

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The extracellular calcium-sensing receptor (CaR) is a multimodal sensor for several key nutrients, notably Ca2+ions and l-amino acids, and is expressed abundantly throughout the gastrointestinal tract. While its role as a Ca2+ion sensor is well recognized, its physiological significance as an l-amino acid sensor and thus, in the gastrointestinal tract, as a sensor of protein ingestion is only now coming to light. This review focuses on the CaR’s amino acid sensing properties at both the molecular and cellular levels and considers new and putative physiological roles for the CaR in the amino ac

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Bentley, Keith W., Yea G. Nam, Jaslynn M. Murphy та Christian Wolf. "Chirality Sensing of Amines, Diamines, Amino Acids, Amino Alcohols, and α-Hydroxy Acids with a Single Probe". Journal of the American Chemical Society 135, № 48 (2013): 18052–55. http://dx.doi.org/10.1021/ja410428b.

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Daly, Kristian, Miran Al-Rammahi, Andrew Moran, Marco Marcello, Yuzo Ninomiya, and Soraya P. Shirazi-Beechey. "Sensing of amino acids by the gut-expressed taste receptor T1R1-T1R3 stimulates CCK secretion." American Journal of Physiology-Gastrointestinal and Liver Physiology 304, no. 3 (2013): G271—G282. http://dx.doi.org/10.1152/ajpgi.00074.2012.

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CCK is secreted by endocrine cells of the proximal intestine in response to dietary components, including amino acids. CCK plays a variety of roles in digestive processes, including inhibition of food intake, consistent with a role in satiety. In the lingual epithelium, the sensing of a broad spectrum of l-amino acids is accomplished by the heteromeric amino acid (umami) taste receptor (T1R1-T1R3). T1R1 and T1R3 subunits are also expressed in the intestine. A defining characteristic of umami sensing by T1R1-T1R3 is its potentiation by IMP or GMP. Furthermore, T1R1-T1R3 is not activated by Trp.

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Ratautė, Kristina, and Dalius Ratautas. "A Review from a Clinical Perspective: Recent Advances in Biosensors for the Detection of L-Amino Acids." Biosensors 14, no. 1 (2023): 5. http://dx.doi.org/10.3390/bios14010005.

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The field of biosensors is filled with reports and designs of various sensors, with the vast majority focusing on glucose sensing. However, in addition to glucose, there are many other important analytes that are worth investigating as well. In particular, L-amino acids appear as important diagnostic markers for a number of conditions. However, the progress in L-amino acid detection and the development of biosensors for L-amino acids are still somewhat insufficient. In recent years, the need to determine L-amino acids from clinical samples has risen. More clinical data appear to demonstrate th

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Wu, Boqian, Kim Ottow, Peter Poulsen, Richard F. Gaber, Eva Albers, and Morten C. Kielland-Brandt. "Competitive intra- and extracellular nutrient sensing by the transporter homologue Ssy1p." Journal of Cell Biology 173, no. 3 (2006): 327–31. http://dx.doi.org/10.1083/jcb.200602089.

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Recent studies of Saccharomyces cerevisiae revealed sensors that detect extracellular amino acids (Ssy1p) or glucose (Snf3p and Rgt2p) and are evolutionarily related to the transporters of these nutrients. An intriguing question is whether the evolutionary transformation of transporters into nontransporting sensors reflects a homeostatic capability of transporter-like sensors that could not be easily attained by other types of sensors. We previously found SSY1 mutants with an increased basal level of signaling and increased apparent affinity to sensed extracellular amino acids. On this basis,

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Idrees, Muhammad, Afzal R. Mohammad, Nazira Karodia, and Ayesha Rahman. "Multimodal Role of Amino Acids in Microbial Control and Drug Development." Antibiotics 9, no. 6 (2020): 330. http://dx.doi.org/10.3390/antibiotics9060330.

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Amino acids are ubiquitous vital biomolecules found in all kinds of living organisms including those in the microbial world. They are utilised as nutrients and control many biological functions in microorganisms such as cell division, cell wall formation, cell growth and metabolism, intermicrobial communication (quorum sensing), and microbial-host interactions. Amino acids in the form of enzymes also play a key role in enabling microbes to resist antimicrobial drugs. Antimicrobial resistance (AMR) and microbial biofilms are posing a great threat to the world’s human and animal population and a

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Hassan, Diandra S., Zeus A. De los Santos, Kimberly G. Brady, Steven Murkli, Lyle Isaacs та Christian Wolf. "Chiroptical sensing of amino acids, amines, amino alcohols, alcohols and terpenes with π-extended acyclic cucurbiturils". Organic & Biomolecular Chemistry 19, № 19 (2021): 4248–53. http://dx.doi.org/10.1039/d1ob00345c.

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Young, Steven H., and Enrique Rozengurt. "Amino acids and Ca2+ stimulate different patterns of Ca2+ oscillations through the Ca2+-sensing receptor." American Journal of Physiology-Cell Physiology 282, no. 6 (2002): C1414—C1422. http://dx.doi.org/10.1152/ajpcell.00432.2001.

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We determined the effect of aromatic amino acid stimulation of the human extracellular Ca2+-sensing receptor (CaR) on intracellular Ca2+ concentration ([Ca2+]i) in single HEK-293 cells. Addition of l-phenylalanine or l-tryptophan (at 5 mM) induced [Ca2+]i oscillations from a resting state that was quiescent at 1.8 mM extracellular Ca2+concentration ([Ca2+]e). Each [Ca2+]i peak returned to baseline values, and the average oscillation frequency was ∼1 min−1 at 37°C. Oscillations were not induced or sustained if the [Ca2+]e was reduced to 0.5 mM, even in the continued presence of amino acid. Aver

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Petersen, Karl-Uwe. "Pepsin and Its Importance for Functional Dyspepsia: Relic, Regulator or Remedy?" Digestive Diseases 36, no. 2 (2017): 98–105. http://dx.doi.org/10.1159/000481399.

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Background: Functional dyspepsia is a heterogeneous disorder lacking an established therapeutic strategy. Historical treatment attempts with pepsin products were shrugged off, as a simple calculation shows that quantitative substitution is pointless. However, such attempts might have been right for the wrong reason. Summary: Today, the role of pepsins is primarily seen in the provision of signalling amino acids (especially phenylalanine and tryptophan) and peptides, which initiate processes promoting digestion. Proteolysis benefits from pepsin variants showing, contrary to common belief, activ

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Forsberg, Hanna, and Per O. Ljungdahl. "Genetic and Biochemical Analysis of the Yeast Plasma Membrane Ssy1p-Ptr3p-Ssy5p Sensor of Extracellular Amino Acids." Molecular and Cellular Biology 21, no. 3 (2001): 814–26. http://dx.doi.org/10.1128/mcb.21.3.814-826.2001.

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ABSTRACT Ssy1p and Ptr3p are known components of a yeast plasma membrane system that functions to sense the presence of amino acids in the extracellular environment. In response to amino acids, this sensing system initiates metabolic signals that ultimately regulate the functional expression of several amino acid-metabolizing enzymes and transport proteins, including multiple, genetically distinct amino acid permeases. We have found that SSY5 encodes a third component of this amino acid sensing system. Mutations inSSY5 manifest phenotypes that are indistinguishable from those resulting from ei

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