| ¿µ¹® | receptor | ÇÑ±Û | ¼ö¿ëü |
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| ¼³¸í | ¼¼Æ÷Áú³» ¶Ç´Â ¼¼Æ÷Ç¥¸é¿¡ Á¸ÀçÇÏ´Â ºÐÀÚ±¸Á¶·Î¼ ƯÀ̹°Áú°ú ¼±ÅÃÀûÀ¸·Î °áÇÕÇÏ¸ç °áÇÕ¿¡ ÀÇÇØ ƯÀÌÇÑ »ý¸®Àû ÀÛ¿ëÀ» ³ªÅ¸³½´Ù. ÆéƼµåÈ£¸£¸ó, ½Å°æÀü´Þ¹°Áú, Ç׿ø, º¸Ã¼, ¸é¿ª±Û·ÎºÒ¸°¿¡ ´ëÇÑ ¼¼Æ÷Ç¥¸é ¼ö¿ëü¿Í ½ºÅ×·ÎÀ̵忡 ´ëÇÑ ¼¼Æ÷Áú³» ¼ö¿ëü°¡ ÀÖ´Ù. |
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| ¿µ¹® | white blood cell(WBC), leukocyte | ÇÑ±Û | ¹éÇ÷±¸ |
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| ¼³¸í | Ç÷¾×³»¿¡ °ñ¼ö±¸°è¼¼Æ÷¿Í ¸²ÇÁ°è¼¼Æ÷, ´ÜÇÙ±¸°è¼¼Æ÷¸¦ ¸ðµÎ ÅëÆ²¾î ¸»ÇÑ´Ù. ¹éÇ÷±¸ÀÇ Áõ°¡°¡ ÀÖÀ¸¸é ´ë°³ °¨¿°ÀÌ Àְųª, ȤÀº Å»¼öÇö»óÀÌ ÀÖÀ½À» ÀǹÌÇÑ´Ù. ¶ÇÇÑ Áö³ªÄ£ ¹éÇ÷±¸¼öÀÇ °¨¼Ò´Â ÀÎü³» ¸é¿ª±â´ÉÀÌ ¶³¾îÁ® ÀÖÀ½À» ÀǹÌÇϸç, ´Ù¸¥ Áúº´¿¡ ÀÇÇØ ³ªÅ¸³ª´Â ÀÌÂ÷ÀûÀÎ Çö»óÀÌ ¾Æ´ÑÁö ²À Áø´ÜÀ» ¹Þ¾Æº¸¾Æ¾ß ÇÑ´Ù. |
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| ¿µ¹® | mast cell | ÇÑ±Û | ºñ¸¸ ¼¼Æ÷ |
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| ¼³¸í | µ¿¹°ÀÇ °áÇÕ Á¶Á÷ °¡¿îµ¥ ³Î¸® ºÐÆ÷ÇÏ´Â ¼¼Æ÷. °áÇÕÁ¶Á÷°ú Á¡¸·Á¶Á÷ ³»¿¡ Àִ ȣ¿°±â¼º »ö¼Ò·Î ÀÌ¿°»ö¼º(metachromasia)À» ³ªÅ¸³»´Â °ú¸³À» °¡Áø ¹æÃßÇüÀÇ ¼¼Æ÷¿¡ ÀÛÀº µÕ±Ù ÇÙÀ» °¡Áø´Ù. ºñ¸¸¼¼Æ÷ÀÇ Ç¥¸é¿¡´Â IgE¿¡ ´ëÇÑ ¼ö¿ëü°¡ Á¸ÀçÇϸç, ¼ö¿ëü¿¡ °áÇÕÇÑ IgE ºÐÀڵ鳢¸® ´Ù°¡ÀÇ Ç׿ø¿¡ ÀÇÇØ ¼·Î ¿¬°áµÇ¸é ºñ¸¸¼¼Æ÷ °ú¸³Å»Ãâ ¹ÝÀÀÀÌ ÀϾ, È÷½ºÅ¸¹Î, ¼¼·ÎÅä´Ñ, ÇìÆÄ¸° µîÀÇ ÈÇÐÀü´Þ ¹°ÁúÀÌ ¹æÃâµÇ¾î, Áï½ÃÇü ¾Ë·¹¸£±â ¹ÝÀÀ µîÀÇ Áõ»óÀ» ÀÏÀ¸Å²´Ù. ÇǺÎ, À帷, Ç÷°ü ÁÖÀ§, Á¡¸· ÁÖº¯¿¡ ÀÖ´Ù. |
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| MC | mass casualties; mast cell; Master of Surgery [Lat. Magister Chirurgiae]; maximum concentration; Med... |
|---|---|
| ACC | accommodation; acetyl coenzyme A carboxylase; acinic cell carcinoma; acute care center; adenoid cyst... |
| ER | efficiency ratio; epigastric region; ejection rate; electroresection; emergency room; endoplasmic re... |
| RAR | rapidly adapting receptor; rat insulin receptor; retinoic acid receptor; right arm reclining; right ... |
| RCC | radiological control center; rape crisis center; ratio of cost to charges; receptor-chemoeffector co... |
| CRLR | Calcitonin Receptor-Like Receptor |
|---|---|
| EGF-receptor | Epidermal Growth Factor receptor |
| IRR | Insulin receptor- related receptor |
| alpha 2MR/LRP | alpha (2)-macroglobulin receptor/low density lipoprotein receptor-related protein |
| ORL1 | opioid receptor like receptor |
| gene rearrangement, alpha-chain T-cell antigen receptor | Ordered rearrangement of T-cell variable gene regions coding for the alpha-chain of antigen receptors. (12 Dec 1998) |
|---|---|
| gene rearrangement, beta-chain T-cell antigen receptor | Ordered rearrangement of T-cell variable gene regions coding for the beta-chain of antigen receptors. (12 Dec 1998) |
| gene rearrangement, delta-chain T-cell antigen receptor | Ordered rearrangement of T-cell variable gene regions coding for the delta-chain of antigen receptors. (12 Dec 1998) |
| gene rearrangement, gamma-chain T-cell antigen receptor | Ordered rearrangement of T-cell variable gene regions coding for the gamma-chain of antigen receptors. (12 Dec 1998) |
| genes, T-cell receptor | DNA sequences, in cells of the t-lymphocyte lineage, that code for T-cell receptors. The tcr genes are formed by somatic rearrangement (see gene rearrangement, t-lymphocyte and its children) of germline gene segments, and resemble ig genes in their mechanisms of diversity generation and expression. (12 Dec 1998) |
| genes, T-cell receptor alpha | DNA sequences encoding the alpha chain of the T-cell receptor. The genomic organization of the tcr alpha genes is essentially the same in all species and is similar to the organization of ig genes. (12 Dec 1998) |
| genes, T-cell receptor beta | DNA sequences encoding the beta chain of the T-cell receptor. The genomic organization of the tcr beta genes is essentially the same in all species and is similar to the organization of ig genes. (12 Dec 1998) |
| genes, T-cell receptor delta | DNA sequences encoding the delta chain of the T-cell receptor. The delta-chain locus is located entirely within the alpha-chain locus. (12 Dec 1998) |
| genes, T-cell receptor gamma | DNA sequences encoding the gamma chain of the T-cell receptor. The human gamma-chain locus is organised similarly to the tcr beta-chain locus. (12 Dec 1998) |
| receptor-CD3 complex, antigen, T-cell | Molecule composed of the non-covalent association of the T-cell antigen receptor (receptors, antigen, T-cell) with the CD3 complex (antigens, CD3). This association is required for the surface expression and function of both components. The molecule consists of up to seven chains: either the alpha/beta or gamma/delta chains of the T-cell receptor, and four or five chains in the CD3 complex. (12 Dec 1998) |
| T-cell receptor | <immunology> The antigen recognising receptor on the surface of T-cells. Heterodimeric (disulphide linked), one of the immunoglobulin superfamily of proteins, binds antigen in association with the major histocompatibility complex (MHC), leading to the activation of the cell. There are two subunits (_ and _, 42-44 kD in mouse, 50-40 kD in humans), each with variable and constant regions, that are associated noncovalently with T3 (20-30 kD). A second heterodimer on CD3 cells with _ (35 kD in mice, 55 kD in humans) and _ (45 kD in mice, 40 kD in humans) chains is a second T-cell antigen receptor that is not MHC restricted. The __ T-cell receptors (TCRs) are formed on very early T-cells in the thymus. (18 Nov 1997) |
| acetylcholine receptor antibodies | <neurology, investigation> A test used to measure the amount of antibodies to acetylcholine receptors on nerve endings. This is a diagnostic test for myasthenia gravis. A normal value is no antibodies in the bloodstream. Acetylcholine receptor (AChR) binding autoantibodies (i.e. Antibodies reactive with several epitopes other than the binding site for acetylcholine or alpha-bungarotoxin) are present in approximately 88% of patients with generalised myasthenia gravis, 70% of ocular myasthenia and in approximately 80% of myasthenia gravis in remission. Although serum concentrations of AChR binding autoantibodies do not in general correlate well with severity of weakness, there is typical decrease in concentration as weakness improves with immunosuppressive therapy. AChR blocking autoantibodies (i.e., antibodies reactive with the AChR binding site) are present in about 50% of patients with myasthenia gravis, 30% with ocular myasthenia gravis and 20% of myasthenia gravis in remission, AChR blocking autoantibodies are the only AChR autoantibodies present in about 1% of myasthenia gravis. AChR modulating autoantibodies (i.e., autoantibodies which cross-link AChRs and cause their removal from muscle membrane surfaces) are present in more than 90% of myasthenia gravis and occasionally are the only AchR autoantibodies detectable in mild, recent onset or ocular-restricted myasthenia gravis. Results for AChR modulating autoantibodies can be transiently false-positive due to curare-like drugs used during general anesthesia. AChR autoantibodies of one or more types are found in at least 80% of ocular myasthenia gravis. Although generally absent in neurological conditions other than myasthenia gravis(and consequently unlikely to cause confusion in neurodiagnosis), false-positive results for AChR autoantibodies occasionally occur in primary biliary cirrhosis, tardive dyskinesia, autoimmune thyroiditis, the elderly, amyotrophic lateral sclerosis patients treated with cobra venom and patients with thymoma in the absence of myasthenia gravis. Approximately 1% of patients with rheumatoid arthritis treated with D-penicillamine develop AChR autoantibodies and myasthenia gravis, both of which disappear when the drug is discontinued. Babies born to ~10% of myasthenia gravis mothers have a transient neonatal form of myasthenia gravis that responds well to anticholinesterase therapy and usually remits within 1 month as maternal IgG disappears. (29 Dec 1997) |
| amino acid receptor | <biochemistry> Ligand gated ion channels with specific receptors for amino acid transmitters. An extended protein superfamily that also includes subunits of the nicotinic acetylcholine receptor. (18 Nov 1997) |
| AMPA receptor | <cell biology> Glutamate operated ion channel. See: excitatory amino acid receptor channels. (05 Feb 1998) |
| ANP receptor | <molecular biology> Family of 3 receptors for atrial natriuretic peptide. ANP A and ANP B have intracellular guanylate cyclase and protein kinase like domains. ANP C, shares the extracellular ligand binding and transmembrane domains, but lacks the functional intracellular domains and is not thought to be involved in signal transduction. (18 Nov 1997) |
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