| ¿µ¹® | malignant tumor | ÇÑ±Û | ¾Ç¼ºÁ¾¾ç |
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| ¼³¸í | Á¤»óÀûÀÎ Á¶Á÷ ¼¼Æ÷°¡ °¢Á¾ ¹°¸®Àû-ÈÇÐÀû-»ý¹°ÇÐÀûÀÎ ¹ß¾Ï ¹°ÁúÀÇ ÀÛ¿ë ¶Ç´Â ¿äÀο¡ ÀÇÇØ µ¹¿¬º¯À̸¦ ÀÏÀ¸ÄѼ Çü¼ºµÇ´Â Á¾¾ç. ¹«Á¦ÇÑÀÇ ¼¼Æ÷ºÐ¿·Î ¸Å¿ì ¿Õ¼ºÇÏ°Ô Áõ½ÄÇÏ¿© ÁÖÀ§Á¶Á÷À» ÆÄ±«-ħ½ÄÇÑ´Ù. ¶Ç ¾î¶² ÈÇй°ÁúÀ» ³»¾î ÁÖÀ§ÀÇ Á¶Á÷¼¼Æ÷¸¦ Ä§ÇØÇÒ »Ó¸¸ ¾Æ´Ï¶ó, Ç÷°ü ¹× ¸²ÇÁ°üÀ» µû¶ó ÀüÀÌÇÏ¿© Àü½ÅÀÇ Ä«ÄʽþƸ¦ÀÏÀ¸ÄÑ Á×À½À» ÃÊ·¡ÇÑ´Ù. »óÇǼºÀÎ °ÍÀ» ¾ÏÁ¾À̶ó Çϰí, ºñ»óÇǼºÀÎ °ÍÀ» À°Á¾À̶ó ÇÑ´Ù. |
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| ¿µ¹® | benign tumor | ÇÑ±Û | ¾ç¼ºÁ¾¾ç |
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| ¼³¸í | ¹ßÀ°¼Óµµ°¡ ¿Ï¸¸ÇÏ¿© ¼ºÀå¿¡ ÇѰ谡 ÀÖ°í, ÁÖÀ§¿ÍÀÇ °æ°è°¡ ¸íÈ®Çϸç, ´Ù¸¥ Á¶Á÷À¸·Î ÆÛÁöÁö ¾ÊÀ¸¸ç, ħÀ±À̳ª ÀüÀ̸¦ ÀÏÀ¸Å°Áö ¾Æ´ÏÇÏ´Â Á¾¾ç. ¼¶À¯Á¾À̳ª Áö¹æÁ¾ µûÀ§°¡ ÀüÇüÀûÀÎ ¿¹ÀÌ´Ù. ¾ç¼ºÁ¾¾çÀº Á¾¾çÀÌ Á¸ÀçÇÑ´Ù°í ÇØµµ 1Â÷ÀûÀ¸·Î ¼÷ÁÖÀÇ »ý¸íÀ» À§ÇùÇÏ´Â ÀÏÀº ¾ø´Ù. ¾ç¼ºÁ¾¾çÀÇ ¹ßÀ°Çü½ÄÀº ÁÖÀ§ÀÇ Á¶Á÷°£¿¡ ¿Õ·¡ÇÏ´Â ÀÏÀÌ ¾øÀÌ ÁÖÀ§ÀÇ Á¶Á÷À» ¹Ð¾î³»¸ç Áõ½ÄÇÑ´Ù. ¹ßÀ°¼Óµµ´Â ¿Ï¸¸Çϸç ÀüÀÌÇϰųª ÀýÁ¦ ÈÄ Àç¹ßÇÏ´Â ÀÏÀÌ ±ØÈ÷ µå¹°´Ù. Á¾¾ç¼ººÐÀº º¯ÀÌüÀ̱ä ÇÏÁö¸¸ ¼º¼÷ÇÑ Á¤»ó¼¼Æ÷¿Í °ÅÀÇ ´Ù¸¥ °ÍÀÌ ¾ø´Ù. Àü½Å¿¡ ´ëÇÑ ¿µÇâÀº ¾Ç¼ºÁ¾¾çÀÇ °æ¿ì ¾î´À Á¤µµ ¹ßÀ°ÇßÀ» ¶§ Àü½ÅÀÇ ¿µ¾ç»óŰ¡ ¼Õ»óµÇ¾î Ä«Äʽþư¡ µÇÁö¸¸ ¾ç¼ºÁ¾¾çÀÇ °æ¿ì ÀÌ·± ÀÏÀº °ÅÀÇ ¾ø´Ù. ¾ç¼ºÁ¾¾ç°ú ¾Ç¼ºÁ¾¾çÀÇ ¼º»óÀÇ Â÷ÀÌ¿¡ ¾ö¹ÐÇÑ °æ°è´Â ¾ø°í, °æ°è°æº¯À¸·Î º¸ÀÌ´Â Á¾¾çµµ ÀÖ´Ù. |
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| ¿µ¹® | Wilms' tumor | ÇÑ±Û | Àª¸§ÁîÁ¾¾ç |
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| ¼³¸í | ÄáÆÏ¿¡¼ ¹ß»ýÇÏ´Â ¾Ç¼ºÁ¾¾çÀ¸·Î ¼Ò¾Æ¿¡¼ ÀÚÁÖ ¹ß»ýÇÑ´Ù. ÈçÈ÷ ¼Ò¾Æ¿¡¼ º¹ºÎ³»Á¾¾çÀ» ¹ß°ß½Ã Áß¾Ó¼±À» ³Ñ¾î¼¸é ½Å°æ¸ð¼¼Æ÷Á¾À̰í, Áß¾Ó¼±À» ³ÑÁö ¾ÊÀ¸¸é Àª¸§ÁîÁ¾¾çÀ» ÀǽÉÇÒ ¸¸Å Áß¿äÇϰí ÈçÇÑ Á¾¾çÀÌ´Ù. ´ë°³ Áõ»óÀº ¾ø´Â ÆíÀ̸ç, ÁÖ·Î ¾Æ±âÀÇ ¸ñ¿åÀ» ½ÃÄÑÁÖ´Ù°¡ ¿ì¿¬È÷ ¹ß°ßµÈ º¹ºÎ³»Á¾±« ¶§¹®¿¡ º´¿øÀ» ã°Ô µÈ´Ù. Áø´Ü½Ã ÄÄÇ»ÅÍ´ÜÃþÃÔ¿µÀ¸·Î ÁÖÀ§ÀÇ ÀüÀ̰¡ ¾ø´ÂÁö¸¦ È®ÀÎÇØ¾ß Çϸç, ÀüÀ̰¡ ¾øÀ¸¸é Ç×¾ÏÈÇпä¹ý, ¹æ»ç¼±Ä¡·á¿ä¹ý, ±×¸®°í ¼ö¼ú¿ä¹ýÀÇ º´ÇÕ¿ä¹ý¿¡ ÀÇÇÑ Ä¡·áÈ¿°ú°¡ ³ô´Ù. |
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| ¿µ¹® | mucinous tumor | ÇÑ±Û | Á¡¾×Á¾¾ç |
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| ¼³¸í | Á¡¾×À¸·Î ±¸¼ºµÈ Á¾¾çÀ» ¸»Çϴµ¥ ÁÖ·Î ¿©¼ºÀÇ ³¼Ò¿¡¼ ¹ß»ýÇÏ´Â ³¶¼º(¹°ÁָӴϰ°Àº Á¾¾çÀ» ¸»ÇÔ) Á¾¾ç¿¡¼ ¸¹ÀÌ º¼ ¼ö ÀÖ´Ù. |
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| ¿µ¹® | tumor | ÇÑ±Û | Á¾¾ç |
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| ¼³¸í | Á¶ÀýÇÒ ¼ö ¾øÀÌ °è¼Ó ÁøÇàµÇ´Â ¼¼Æ÷ºÐ¿¿¡ ÀÇÇÑ Á¶Á÷ÀÇ »õ·Î¿î Áõ½Ä ¹× Áõ´ë. ½Å»ý¹°. (1) ºÐ·ù A. ħÀ±°ú ÀüÀÌÀÇ À¯¹«¿¡ µû¶ó i)¾ç¼ºÁ¾¾ç: ħÀ±°ú ÀüÀ̰¡ ¾ø°í ¿ªÇü¼ºÀÌ ³·Àº ¼¼Æ÷·Î ±¸¼ºµÊ. ´ë°³ Ä¡·á¿¡ ¹ÝÀÀÀÌ ³ô°í, »ý¸í¿¡ Å©°Ô ÁöÀåÀÌ ¾øÀ¸¸ç, Àç¹ßÇÏ´Â °æ¿ìµµ Àû´Ù. Áõ»óÀº ´ÜÁö ÁÖÀ§Á¶Á÷¿¡ ´ëÇÑ ¾Ð¹ÚÁ¤µµÀÌ´Ù. ii)¾Ç¼ºÁ¾¾ç: ħÀ±°ú ÀüÀ̰¡ ÀÖ°í Åðȵµ°¡ ³ôÀº ¼¼Æ÷·Î ±¸¼ºµÊ. ±â¿ø¼¼Æ÷°¡ »óÇÇÁ¶Á÷ÀÏ °æ¿ì ¾ÏÁ¾, ºñ»óÇǼºÀÏ °æ¿ì À°Á¾À¸·Î ³ª´©±âµµ ÇÑ´Ù. Ä¡·á¿¡ Àß ¹ÝÀÀÇÏÁö ¾Ê°í, Àç¹ßÀ» Àß Çϸç, »ýÁ¸À²ÀÌ ³·´Ù. ÈçÈ÷ ¸»ÇÏ´Â ¡°¾Ï¡±À» ÀǹÌÇÑ´Ù. B. Á¶Á÷ÇÐÀû Ư¡¿¡ µû¶ó »ùÁ¾, Áö¹æÁ¾, ±ÙÁ¾ µîÀ¸·Î ³ª´©±âµµ ÇÑ´Ù. (2) º´¸®Á¶Á÷ÇÐÀû Ư¡ A. À°¾ÈÀû ¼Ò°ß µ¢¾î¸®¸¦ Çü¼ºÇϱ⵵ Çϰí Á¤»óÁ¶Á÷¿¡ ½º¸çµéµíÀÌ ÆÇ»ó±¸Á¶¸¦ ÀÌ·ç±âµµ ÇÏ´Â µî ´Ù¾çÇÑ ÇüŸ¦ º¸ÀδÙ. ¾ç¼ºÀÇ °æ¿ì ÇǸ·À» °¡Áø °æ¿ì°¡ ¸¹°í ¾Ç¼ºÀÇ °æ¿ì ¾ø´Â °æ¿ì°¡ ¸¹´Ù. À°¾È¼Ò°ß¿¡ µû¶ó ´ÙÀ½°ú °°ÀÌ ³ª´«´Ù. ³¶¼º, À¶±â¼º, ±«»ç¼º, Æú¸³¸ð¾ç, ±Ë¾çÇü µîÀÌ ÀÖ´Ù. ¶Ç´Â ¼¼Æ÷ÀÇ Å©±â¿Í ¸ð¾çÀÌ ºñÁ¤»óÀûÀÎ ÇüÅ·Πº¯ÈÇÑ´Ù. ÇÙÀÇ ±Ø¼ºÀÌ »ç¶óÁö°í ÇÙÀÇ ¿°»ö¼ºÀÌ Â£¾îÁø´Ù. ¼¼Æ÷ÁúÀÇ ¿°»ö¼ºµµ º¯ÈÇÏ¸ç ¼¼Æ÷µé°£ÀÇ ¼¼Æ÷ÁֱⰡ ¸Å¿ì ´Ù¾çÇØÁ® ¸¹Àº ¼¼Æ÷ºÐ¿À» º¸ÀδÙ. ÀÌ·¯ÇÑ ÀÏ·ÃÀÇ º¯È¸¦ ¿ªÇü¼ºÀ̶ó ÇÑ´Ù. ¿ªÇü¼ºÀÇ Á¤µµ¿¡ µû¶ó Á¶Á÷ÇÐÀû µî±ÞÀ» ³ª´«´Ù. ¶ÇÇÑ °¢ Á¾¾ç¿¡ µû¶ó °¢±â ´Ù¸¥ º´¸®Á¶Á÷ÇÐÀû ¸íĪÀ» ºÙÀδÙ. |
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| CPA tumor | Cerebello-Pontine Angle(¼Ò³ú±³°¢ºÎ) tumor |
|---|---|
| IDEM tumor | Intra-Dural Extra-Medullary tumor |
| MEN | Multiple Endocrine Neoplasia ; AD Trait 1. MEN Type I(= Wermer Syndro... |
| GCT | general care and treatment; germ-cell tumor; giant cell thyroiditis; giant cell tumor |
| ICT | icteric, icterus; indirect Coombs test; inflammation of connective tissue; insulin coma therapy; int... |
| amyloid precursor protein | <protein> Individuals with Alzheimer's disease are characterised by extensive accumulation of amyloid in the brain, referred to as senile plaques. These consist of a core of amyloid fibrils surrounded by dystrophic neurites. The principal component of the amyloid fibrils is B/A4, a peptide derived from the larger APP. The specific role of amyloid protein is unclear but it is thought that amyloid deposits may cause neurons to degenerate. Amyloid deposits also occur in brains of older Down's Syndrome patients. (04 May 1997) |
|---|---|
| amyloid protein | Glycoprotein deposited extracellularly in tissues in amyloidosis. The glycoprotein may either derive from light chain of immunoglobulin (AIO (amyloid of immune origin): 5-18 kD glycoprotein, product of a single clone of plasma cells, the N terminal part of lambda or kappa light chain) or, in what used to be referred to as AUO, amyloid of unknown origin, from serum amyloid A (SAA), one of the acute phase proteins that increases many fold in inflammation. The polypeptides are organised as a _ pleated sheet making the material rather inert and insoluble. Minor protein components are also found. Should be distinguished from _ amyloid deposited in the brain and that is derived from amyloid precursor protein (see amyloidogenic glycoprotein. (18 Nov 1997) |
| amyloid protein aa | A nonimmunoglobulin amyloid isolated from amyloid fibrils deposited in amyloidosis secondary to chronic inflammatory diseases such as rheumatoid arthritis. Antisera to amyloid protein aa have been used to detect a related serum protein saa. (12 Dec 1998) |
| amyloid protein saa | A serum protein believed to be a circulating precursor to amyloid protein aa. It is present in low concentrations in normal sera, but found in much higher concentrations in sera of older persons and in patients with amyloidosis or with diseases known to predispose to amyloidosis. Very high levels of this protein have been reported during acute inflammatory episodes. Antisera to amyloid protein aa cross-react with protein saa. (12 Dec 1998) |
| amyloid tumour | A localised form of amyloidosis in which amyloid occurs as masses or nodules beneath the skin or mucous membranes, e.g., in the larynx. Synonym: amyloid tumour, focal amyloidosis. (05 Mar 2000) |
| beta-amyloid | <protein> The protein which forms thick deposits, or plaques, in the brains of people with Alzheimer's disease, a disease where memory skills gradually deteriorate with age. (13 Nov 1997) |
| cerebral amyloid angiopathy | <pathology> A condition where there is a deposition of amyloid (insoluble protein) in the walls of the arteries which supply the brain. This results in an increased risk of dementia and-or intracerebral haemorrhage. Cerebral amyloidosis or cerebral amyloid angiopathy, is a complication of primary amyloidosis. Origin: Gr. Pathos = disease (27 Sep 1997) |
| serum amyloid | In secondary amyloidosis the fibrils deposited in tissues are unrelated to immunoglobulin light chains (in contrast to the situation in primary amyloidosis) and are made of amyloid A protein (AA protein). This is derived from serum amyloid A (SAA) that is the apolipoprotein of a high density lipoprotein and an acute phase protein. Partial proteolysis converts SAA into the pleated sheet configuration of the amyloid fibrils. Amyloid P protein is also found as a minor component of the fibrils (in both primary and secondary amyloidosis) and is derived from serum amyloid P that has similarity to C-reactive protein. The physiological role remains obscure. (18 Nov 1997) |
| serum amyloid P component | Precursor of amyloid component P, found in basement membrane. Member of the pentraxin family. See: serum amyloid. (18 Nov 1997) |
| islet amyloid peptide | <hormone, protein> Peptide of 37 amino acids that selectively inhibits insulin stimulated glucose uptake in muscle. Structurally related to calcitonin gene-related peptide. (15 Oct 1997) |
| familial amyloid neuropathy | <neurology> A disorder in which various peripheral nerves are infiltrated with amyloid and their functions disturbed, an abnormal prealbumin is also formed and is present in the blood; characteristically, it begins during mid-life and is found largely in persons of Portuguese descent. Other rare clinical types occur. Inheritance: autosomal dominant. Synonym: familial amyloidosis, hereditary amyloidosis. (05 Mar 2000) |
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