| ¿µ¹® | receptor | ÇÑ±Û | ¼ö¿ëü |
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| ¿µ¹® | surface tension | ÇÑ±Û | Ç¥¸éÀå·Â |
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| ¿µ¹® | white blood cell(WBC), leukocyte | ÇÑ±Û | ¹éÇ÷±¸ |
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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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| SA | salicylic acid; saline [solution]; salt added; sarcoidosis; sarcoma; scalenus anticus; secondary ame... |
|---|---|
| MC | mass casualties; mast cell; Master of Surgery [Lat. Magister Chirurgiae]; maximum concentration; Med... |
| SC | conditioned stimulus; sacrococcygeal; Sanitary Corps; scalenus [muscle]; scapula; Schwann cell; scia... |
| SCM | Schwann cell membrane; sensation, circulation, and motion; Society of Computer Medicine; soluble cyt... |
| ACC | accommodation; acetyl coenzyme A carboxylase; acinic cell carcinoma; acute care center; adenoid cyst... |
| CSH | Cell surface hydrophobicity |
|---|---|
| ICSA | Islet cell surface antibodies |
| CSA | cell surface antigen |
| BSA | A/body surface area |
| ASL | Airway surface liquid |
| 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) |
| receptors, cell surface | Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behaviour of the target cell. Cell surface receptors, unlike enzymes, do not chemically alter their ligands. (12 Dec 1998) |
| cell surface marker | <cell biology> Any molecule characteristic of the plasma membrane of a cell or in some cases of a specific cell type. 5' nucleotidase and Na/K ATPase are often used as plasma membrane markers. (26 Mar 1998) |
| SP220K cell surface matrix proteinase | <enzyme> Inactive form has guanidinobenzoatase activity; active form has gelatinolytic activity Registry number: EC 3.4.21.- Synonym: sp220k enzyme (26 Jun 1999) |
| 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) |
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