Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Enzyme kinetics.

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Angiotensin 1 converting enzyme (ACE) is essentially responsible for the conversion of angiotensin 1 in angiotensin II as well as regulating blood pressure and vascular remodeling. Elevated serum ACE levels are found in various pulmonary/non-pulmonary and granulomatous/non-granulomatous medical conditions; until 2001, the list of causes of elevated ACE did not include genetic mutations of the ACE gene. Recent studies on the subject found that ACE mutations typically produce very high ACE levels and activities (reaching as much as 10 to 15 times the normal range's upper limit) and that their overall prevalence may be largely underestimated. This review takes advantage of the results drawn from a recent survey on a newly discovered ACE mutation (specifically: the intron 25-IVS25+1G>A (c.3691+1G>A) in two Belgian families. Its main objective was to evaluate the frequency and nature of the different causes of ACE elevation in the Cliniques Universitaires St-Luc as well as offering a decisional algorithm on managing an ACE elevation based on our data and the literature. In this article, a section discusses the historical and current methods used for measuring plasmatic ACE. We included the results of our own retrospective study in order to compare them with the literature. On the whole, our observations corroborate with the published data, sarcoidosis being responsible for two thirds of ACE elevations above 2 times the test's upper limit. Ln this review, we also describe minutely some of other potential causes. Although 427 (out of 4818) of our center's measurements exceed the norm's upper limit of plasmatic ACE (0.5% of all our pACE determinations), we could not identify new proven cases or strongly suspected cases of ACE mutations based on ACE levels and the detailed clinical history. Nonetheless, ACE mutations must come to mind when confronted with very high plasmatic ACE values after the exclusion of common causes; after identification of a new case of ACE mutation, a familial investigation should be set in motion. L'enzyme de conversion de l'angiotensine I (ECA) est essentiellement responsable de la conversion de I'angiotensine I en angiotensine II ainsi que de la régulation de la pression artérielle et du remodelage vasculaire. Des taux élevés d'ECA sont retrouvés dans diverses maladies pulmonaires/non-pulmonaires et granulomateuses/non-granulomateuses ; jusqu'en 2001, la liste des causes d'élévation d'ECA n'incluait pas encore les mutations génétiques du gène de l'ECA. Des études récentes sur le sujet ont mis en évidence que les mutations de l'ECA entraînent typiquement des élévations très importantes du taux et de l'activité de l'ECA dans le sang (allant jusqu'à 10 à 15 fois la limite supérieure des valeurs normales) et que la prévalence globale de ces mutations serait sous-estimée. Cette revue de littérature a été motivée par les résultats d'une étude récente consacrée à l'évaluation d'une nouvelle mutation de l'ECA (spécifiquement : l'intron 25-IVS25+1G>A (c.3691+ lG>A)) dans deux familles belges. Elle a pour objectif d'évaluer la fréquence et la nature des différentes causes d'élévation de l'ECA aux cliniques universitaires St-Luc et de proposer un algorithme décisionnel de prise en charge d'une élévation de l'ECA sur base de ces données et de la littérature. Dans ce travail, une section traitera les méthodes historiques et courantes de dosage de l'ECA plasmatique. Nous y avons inclus les résultats observés dans notre propre étude rétrospective afin de les comparer avec ceux de la littérature. Dans l'ensemble, nos observations corroborent avec les données publiées, la sarcoïdose étant responsable de deux tiers de ces élévations de l'ECA au-delà de 2 fois la limite supérieure.Dans cette revue, les autres causes identifiées y sont également détaillées. Bien que 427 (sur 4818) de nos mesures dépassent la limite supérieure du taux normal d'ECA plasmatique (0.5% de tous les dosages), nous n'avons pas identifié de nouveau cas avéré ou fortement suspect de mutation de l'ECA sur base des taux et de l'histoire clinique détaillée. Les mutations génétiques d'ECA doivent néanmoins être suspectées en cas de valeurs très hautes d'ECA après exclusion des causes plus fréquentes ; après identification de la mutation, une investigation familiale doit être proposée.

Angiotensin-Converting Enzyme Inhibitors --- Review

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Protease inhibitors. --- Proteolytic enzymes. --- Virus inhibitors. --- Antiviruses --- Antiviral agents --- Viruses --- Peptide hydrolases --- Proteases --- Hydrolases --- Proteolytic enzyme inhibitors --- Proteolytic enzymes --- Enzyme inhibitors --- Inhibitors

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Using a multidisciplinary approach, this book describes the biochemical mechanisms associated with dysregulation of proteases and the resulting pathophysiological consequences. It highlights the role and regulation of different types of proteases as well as their synthetic and endogenous inhibitors. The role of proteases was initially thought to be limited to general metabolic digestion. However, we now know that the role of protein breakdown is much more complex, and proteases have multiple functions: they are coupled to turnover and can affect protein composition, function and synthesis. In addition to eliminating abnormal proteins, breakdown has many modulatory functions, including activating and inactivating enzymes, modulating membrane function, altering receptor channel properties, affecting transcription and cell cycles and forming active peptides. The ubiquity of proteases in nature makes them an important target for drug development. This in-depth, comprehensive is a valuable resource for researchers involved in identifying new targets for drug development. With its multidisciplinary scope, it bridges the gap between fundamental and translational research in the biomedical and pharmaceutical industries, making it thought-provoking reading for scientists in the field.

Medicine. --- Cancer research. --- Human physiology. --- Molecular biology. --- Pharmaceutical technology. --- Biomedicine. --- Human Physiology. --- Molecular Medicine. --- Pharmaceutical Sciences/Technology. --- Cancer Research. --- Proteolytic enzyme. --- Oncology. --- Tumors --- Pharmaceutical laboratory techniques --- Pharmaceutical laboratory technology --- Technology, Pharmaceutical --- Technology --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Physiology --- Human body --- Health Workforce --- Cancer research --- Molecular biochemistry --- Molecular biophysics --- Biochemistry --- Biophysics --- Biomolecules --- Systems biology

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Pursuing the questions of how we learn and how memory is made, Edward Kosower introduces a novel and rich approach to connecting molecular properties with the biological properties that enable us to write and read, to create culture and ethics, and to think. Here he examines what happens within a single cell in reaction to external stimuli, and shows the parallels between single cell and multicellular responses. To address the problem of "learning," Kosower explains the molecular mechanisms of responses to input from taste, olfactory, and visual receptors. He then shows how these and other processes serve as the basis for memory. This study covers such signals for the molecular process of learning as pheromones (the molecular signals mediating behavior), light (activates the G-protein receptor, rhodopsin), and acetylcholine (opens the nicotinic acetylcholine receptor). Kosower's discussion of the structure and function of these complex molecules has direct implications for such areas as molecular neurobiology, bioorganic chemistry, and drug design, in elucidating approaches to the structure of drug targets.Originally published in 1991.The Princeton Legacy Library uses the latest print-on-demand technology to again make available previously out-of-print books from the distinguished backlist of Princeton University Press. These editions preserve the original texts of these important books while presenting them in durable paperback and hardcover editions. The goal of the Princeton Legacy Library is to vastly increase access to the rich scholarly heritage found in the thousands of books published by Princeton University Press since its founding in 1905.

Molecular neurobiology. --- Cellular signal transduction. --- Molecular recognition. --- Action potential. --- Activation. --- Amino acid. --- Antibody. --- Bilayer. --- Binding protein. --- Biological Assay. --- Biological membrane. --- Biological neural network. --- Biomolecular structure. --- Biosynthesis. --- Catalysis. --- Caudate nucleus. --- Cell surface receptor. --- Chemical change. --- Chemical modification. --- Chemical synapse. --- Chemoreceptor. --- Chemotaxis. --- Chromatin. --- Chromophore. --- Conformational change. --- Creatine kinase. --- Demethylation. --- Electron transport chain. --- Enzyme. --- GABA receptor. --- GABAA receptor. --- Ganglion cell. --- Gel electrophoresis. --- Gene product. --- Globulin. --- Glycine receptor. --- Golgi apparatus. --- Golgi cell. --- Ion channel. --- LTP induction. --- Libration (molecule). --- Ligand (biochemistry). --- Lysine. --- Lysozyme. --- Mechanism of action. --- Mechanoreceptor. --- Membrane potential. --- Methylation. --- Methyltransferase. --- Microvillus. --- Molecular configuration. --- Molecular electronic transition. --- Molecular graphics. --- Molecular sieve. --- Molecule. --- Motor neuron. --- Muscarinic acetylcholine receptor. --- Mutagen. --- Neurofilament. --- Neuroglia. --- Neurokinin A. --- Neuron. --- Neuropeptide. --- Neurotransmitter. --- Nicotinic acetylcholine receptor. --- Olfactory receptor neuron. --- Organism. --- Peptide. --- Permease. --- Pheromone binding protein. --- Pheromone. --- Phosphodiesterase. --- Phosphorylation. --- Physical organic chemistry. --- Plasma protein binding. --- Post-translational modification. --- Protein methylation. --- Protein phosphorylation. --- Protein primary structure. --- Protein structure. --- Protein synthesis inhibitor. --- Protein. --- Proteolysis. --- RNA interference. --- Receptor (biochemistry). --- Receptor modulator. --- Receptors, Neurotransmitter. --- Regulation of gene expression. --- Retina. --- Rhodopsin kinase. --- Rhodopsin. --- Sensory neuron. --- Side chain. --- Signal processing. --- Signal transduction. --- Sodium channel. --- Stimulus (physiology). --- Synapsin I. --- Synapsis. --- Synaptosome. --- Teratology. --- Transducin. --- Transposable element.