| MSF | macrophage slowing factor; macrophage spreading factor; Medicins sans Frontieres [Doctors without Bo... |
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| PIF | paratoid isoelectric focusing variant protein; peak inspiratory flow; proinsulin-free; prolactin-inh... |
| SPF | skin protection factor; specific-pathogen free; spectrophotofluorometer; S-phase fraction; split pro... |
| TGF | T-cell growth factor; transforming growth factor; tuboglomerular feedback; tumor growth factor |
| FSF | Fibrin Stabilizing Factor(Factor XIII) |
hypophosphatemic rickets (저인산 혈성 구루병, 저인산염 혈성 구루병
| receptors, gaba-a | Cell surface proteins which bind gaba and control an integral membrane chloride channel. Gaba-a receptors are the most prevalent inhibitory neurotransmitter receptors in the brain. Several isoforms have been cloned, and they belong to a superfamily which includes nicotinic receptors, glycine receptors, and 5ht-3 receptors. Most gaba-a receptors have separate modulatory sites sensitive to benzodiazepines and to barbiturates. (12 Dec 1998) |
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| receptors, gaba-b | Cell surface proteins which bind gaba and influence cells via interactions with g-proteins. Gaba-b receptors are pharmacologically characterised by their insensitivity to the blocker bicuculline and sensitivity to the agonist l-baclofen. They are found both presynaptically and postsynaptically, and act variously by inhibition of adenylate cyclase, activation of phospholipase a2, activation of potassium channels, and inactivation of voltage-activated calcium channels. (12 Dec 1998) |
| receptors, gastrointestinal hormone | Cell surface proteins that bind gastrointestinal hormones with high affinity and trigger intracellular changes influencing the behaviour of cells. most gastrointestinal hormones also act as neurotransmitters so these receptors are also present in the central and peripheral nervous systems. (12 Dec 1998) |
| receptors, glucagon | Cell surface receptors that bind glucagon with high affinity and trigger intracellular changes which influence the behaviour of cells. Activation of glucagon receptors causes a variety of effects; the best understood is the initiation of a complex enzymatic cascade in the liver which ultimately increases the availability of glucose to body organs. (12 Dec 1998) |
| receptors, glucocorticoid | Cytoplasmic proteins that specifically bind glucocorticoids and mediate their cellular effects. The glucocorticoid receptor-glucocorticoid complex acts in the nucleus to induce transcription of DNA. Glucocorticoids were named for their actions on blood glucose concentration, but they have equally important effects on protein and fat metabolism. Cortisol is the most important example. (12 Dec 1998) |
| receptors, glutamate | Cell-surface proteins that bind glutamate and trigger changes which influence the behaviour of cells. Glutamate receptors include ionotropic receptors (ampa, kainate, and n-methyl-d-aspartate receptors), which directly control ion channels, and metabotropic receptors which act through second messenger systems. Glutamate receptors are the most common mediators of fast excitatory synaptic transmission in the central nervous system. They have also been implicated in the mechanisms of memory and of many diseases. (12 Dec 1998) |
| receptors, glycine | Cell surface receptors that bind glycine with high affinity and trigger intracellular changes which influence the behaviour of cells. Glycine receptors in the central nervous system have an intrinsic chloride channel and are usually inhibitory. (12 Dec 1998) |
| receptors, gonadotropin | Those protein complexes or molecular sites on the surfaces of gonadal and other sensitive cells that bind gonadotropins and thereby modify the functions of those cells; hcg, lh, and fsh are the major specific gonadotropins. (12 Dec 1998) |
| receptors, histamine | Cell-surface proteins that bind histamine and trigger intracellular changes influencing the behaviour of cells. Histamine receptors are widespread in the central nervous system and in peripheral tissues. Three types have been recognised and designated h1, h2, and h3. They differ in pharmacology, distribution, and mode of action. (12 Dec 1998) |
| receptors, histamine h1 | A class of histamine receptors discriminated by their pharmacology and mode of action. most histamine h1 receptors operate through the inositol phosphate/diacylglycerol second messenger system. Among the many responses mediated by these receptors are smooth muscle contraction, increased vascular permeability, hormone release, and cerebral glyconeogenesis. (12 Dec 1998) |
| receptors, histamine h2 | A class of histamine receptors discriminated by their pharmacology and mode of action. Histamine h2 receptors act via g-proteins to stimulate adenylate cylase. Among the many responses mediated by these receptors are gastric acid secretion, smooth muscle relaxation, inotropic and chronotropic effects on heart muscle, and inhibition of lymphocyte function. (12 Dec 1998) |
| receptors, histamine h3 | A class of histamine receptors discriminated by their pharmacology and mode of action. Histamine h3 receptors were first recognised as inhibitory autoreceptors on histamine-containing nerve terminals and have since been shown to regulate the release of several neurotransmitters in the central and peripheral nervous systems. (12 Dec 1998) |
| receptors, HIV | Cellular receptors that bind the human immunodeficiency virus that causes aids. Included are CD4 antigens, found on t4 lymphocytes, and monocytes/macrophages, which bind to the HIV envelope protein gp120. (12 Dec 1998) |
| receptors, IgE | Specific molecular sites on the surface of b- and T-lymphocytes which combine with iges. Two subclasses exist: low affinity receptors (fc epsilon ri) and high affinity receptors (fc epsilon rii). (12 Dec 1998) |
| receptors, IgG | Specific molecular sites on the surface of various cells, including B-lymphocytes and macrophages, that combine with iggs. Three subclasses exist: fc gamma ri (the CD64 antigen, a low affinity receptor), fc gamma rii (the CD32 antigen, a high affinity receptor), and fc gamma riii (the CD16 antigen, a low affinity receptor). (12 Dec 1998) |