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  • left heart catheterization
    Á½ɵµ°ü¹ý, Á½ÉÄ«Åן°Ë»ç¹ý, Á½ɵµÀÚ(¼ú).
  • left heart failure
    Á½ɺÎÀü.
  • left heart strain
    Á½ɱäÀå(ñ§ãýÑÌíå).
  • left hemianopsia
    ÁÂÃø¹Ý¸Í(ñ§ö°ÚâØî).
  • left hepatic artery<³ª> ramus sinister arteriae hepaticae propriae
    Á°£µ¿¸Æ
  • left hepatic branch artery<³ª> ramus sinister artery hepaticae propriae
    ¿Ü°úÁ°£Áö.
  • left hepatic duct
    ¿Þ°£°ü
  • left hepatic lobe
    ¿Þ°£¿±
  • left hepatic veins
    ¿Þ°£Á¤¸Æ
  • left horn
    ¿Þ»Ô
  • left hypogastric nerve
    ¿Þ¾Æ·§¹è½Å°æ
  • left iliac fossa =LIF
    ÁÂÀå°ñ¿Í(ÁÂÀå°ñ¿Í).
  • left iliac fossa =LIF
    ÁÂÀå°ñ¿Í(ñ§íóÍéèÀ).
  • left iliac fossa =LIF
    ÁÂÀå°ñ¿Í(ñ§ ÍéèÀ).
  • left inferior lobar bronchus
    ¿Þ¾Æ·¡¿±±â°üÁö
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LVSI left ventricular systolic index
LVSO left ventricular systolic output
LVSP left ventricular systolic pressure
LVSV left ventricular stroke volume
LVSW left ventricular stroke work
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PRL-R Prolactin receptors
PAR Protease activated receptors
RACK Receptors for activated C kinase
SARs Slowly adapting pulmonary stretch receptors
SAR Slowly adapting receptors
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Receptors for activated C Kinase Synonym for endosome.
(18 Nov 1997)
receptors, fsh Cell surface proteins that bind follicle-stimulating hormone (follitropin, fsh) with high affinity and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, gaba Cell-surface proteins that bind gaba with high affinity and trigger changes that influence the behaviour of cells. Gaba-a receptors control chloride channels formed by the receptor complex itself. They are blocked by bicuculline and usually have modulatory sites sensitive to benzodiazepines and barbiturates. Gaba-b receptors act through g-proteins on several effector systems, are insensitive to bicuculline, and have a high affinity for l-baclofen.
(12 Dec 1998)
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)
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, granulocyte-colony-stimulating factor Receptors that bind and internalise granulocyte-colony-stimulating factor. Their mw is believed to be 150 kD. These receptors are found mainly on a subset of myelomonocytic cells.
(12 Dec 1998)
receptors, granulocyte-macrophage colony-stimulating factor Receptors that bind and internalise the granulocyte-macrophage stimulating factor. Their mw is believed to be 84 kD. The most mature myelomonocytic cells, specifically human neutrophils, macrophages, and eosinophils, express the highest number of affinity receptors for this growth factor.
(12 Dec 1998)
receptors, growth factor Cell surface receptors that bind growth or trophic factors with high affinity, triggering intracellular responses which influence the growth, differentiation, or survival of cells.
(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)
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