| ¿µ¹® | iron deficiency anemia | ÇÑ±Û | ö°áÇ̺óÇ÷ |
|---|---|---|---|
| ¼³¸í | ÀûÇ÷±¸ÀÇ ±â´ÉÀº »ê¼Ò¸¦ ¿î¹ÝÇϴµ¥ ÀÖ´Ù. ÀûÇ÷±¸ ¼Ó¿¡ »ê¼Ò¿Í °áÇÕÀ» ÇÏ¿© »ê¼Ò¸¦ ¿î¹ÝÇÏ´Â Ç÷»ö¼Ò¶ó´Â ¹°ÁúÀÌ ÀÖ´Ù. öÀº ÀÌ Ç÷»ö¼ÒÀÇ Áß¿äÇÑ ºÎºÐÀ» ÀÌ·ç´Â °ÍÀ¸·Î öÀÌ ¾øÀ¸¸é Ç÷»ö¼Ò°¡ ¸¸µé¾îÁú ¼ö°¡ ¾ø´Ù. Ç÷»ö¼Ò°¡ ¾øÀ¸¸é ¿ª½Ã ÀûÇ÷±¸µµ ¸¸µé¾îÁöÁö ¾ÊÀ¸¹Ç·Î ü³»¿¡ öÀÌ ºÎÁ·ÇÏ¸é ºóÇ÷ÀÌ »ý±ä´Ù. ÀÌ Ã¶°áÇ̼º ºóÇ÷Àº ºóÇ÷ÀÇ ¿øÀÎ Áß¿¡¼ °¡Àå ÈçÇÑ °ÍÀÌ´Ù(¾à 25%¸¦ Â÷ÁöÇÑ´Ù). öÀúÀå·®ÀÇ ÀúÇÏ-°áÇÌ, Ç÷ûö³óµµÀÇ ÀúÇÏ, Æ®¶õ½ºÆä¸°·® »ó½Â, Æ®¶õ½ºÆä¸°Æ÷ȵµÀÇ ÀúÇÏ, Ç÷»ö¼Ò³óµµ ¶Ç´Â Ç츶ÅäÅ©¸®Æ®ÀÇ ÀúÇÏ, Àú»ö¼Ò¼º´ëÀûÇ÷±¸¸¦ Ư¡À¸·Î ÇÏ´Â ºóÇ÷·Î¼, »ýü ³»¿¡¼ öÀÌ Àå±â¿¡ °ÉÃÄ °áÇÌµÇ¸ç ±× ¶§¹®¿¡ Ç÷»ö¼Ò »ý»ê °¨¼Ò¿¡ ÀÇÇØ ÀϾÙ. âÀÚ¿¡¼ÀÇ Ã¶Èí¼ö·® ºÎÁ·, öÀÇ ¼ö¿ä Áõ´ë(À¯¾Æ±â, »çÃá±â, ÀÓ½Å), ö¼Ò½Ç°úÀ×(ÃâÇ÷)¿¡ ÀÇÇØ ÀϾ¸ç, ƯÈ÷ »çÃá±â¿¡¼ Æó°æ±â±îÁöÀÇ ¿©¼º¿¡°Ô ¸¹´Ù. Áõ»óÀ¸·Î¼´Â ¾ó±¼Ã¢¹é, ÇǷΰ¨, ÇǺÎâ¹é, ¼ÕÅé º¯È(½ºÇ¬ ¸ð¾ç) µîÀ» ³ªÅ¸³½´Ù. ±¸° ¿µ¿ª¿¡¼´Â ÇôÀÇ Á¢ÃËÅë, ¹ßÀû, °ÇÁ¶°¨, »ïÅ´°ï¶õÀ» ¼ö¹ÝÇϸé Ç÷¯¸Ó-ºó½¼(Plummer-Vinson)ÁõÈıºÀ̶ó°í ÇÑ´Ù. Ç÷¾× ¼Ò°ßÀº Ç÷ûöÀº ÀúÇÏÇϸç, ö°áÇÕ´É·ÂÀÇ »ó½Â, Àú»ö¼Ò¼º ÀÛÀºÀûÇ÷±¸¼ºÀ» ³ªÅ¸³½´Ù. |
||
| ¿µ¹® | liver cirrhosis | ÇÑ±Û | °£°æÈ(Áõ) |
|---|---|---|---|
| ¼³¸í | Á¤»óÀûÀÎ °£¼¼Æ÷ÀÇ ¸¹Àº ºÎºÐÀÌ ¼Ò½ÇÀÌ µÇ°í ´ë½Å¿¡ ¼¶À¯Á¶Á÷À¸·Î ´ëÄ¡µÇ¾î ÀÖ´Â °£ÀÇ º´Àû »óŸ¦ ¸»ÇÑ´Ù. °£¼¼Æ÷ÀÇ ¸¹Àº ¼Õ»óÀ» °¡Á®¿À´Â ¸ðµç º´¿¡¼ °£°æÈ°¡ ÀϾÙ. ±×·¯³ª ´ëºÎºÐÀÇ °£°æÈÀÇ ¿øÀÎÀº °£¿°°ú ¼ú¿¡ ÀÇÇÑ °£¼Õ»óÀÌ´Ù. °£°æÈÀÇ Áõ»óÀº ¿øÀο¡ µû¶ó¼ ´ÙÀ½°ú °°Àº µÎ °¡Áö·Î ³ª´ ¼ö°¡ ÀÖ´Ù. ù°´Â ¿ì¼± °£ÀÇ ±â´ÉÀÇ Àå¾Ö¿¡ ÀÇÇÑ Áõ»óÀÌ´Ù. °£¼¼Æ÷ÀÇ »ó´ç¼ö°¡ ¼¶À¯Á¶Á÷À¸·Î ´ëüµÇ¾î ÀÖ´Â »óÅÂÀ̹ǷΠ°£ÀÇ ±â´ÉÀÇ Àå¾Ö°¡ »ý±â´Â °ÍÀº ´ç¿¬ÇÏ´Ù. Ȳ´Þ µîÀÌ ´ëÇ¥Àû ¿¹¶ó ÇϰڴÙ. µÎ¹øÂ°´Â ¹®¸Æ¾ÐÇ×Áø(portal hypertension)¿¡ ÀÇÇÑ Áõ»óµéÀÌ´Ù. À§, ÀÛÀºÃ¢ÀÚ³ª ūâÀÚ¿¡¼ ¿µ¾çºÐÀ» Èí¼öÇϱâÀ§ÇÑ ¸ð¼¼Ç÷°üÁ¶Á÷Àº ¸ðµÎ °£À¸·Î ¿¬°áÀÌ µÈ´Ù. Áï ¼Òȱ⿡¼ Èí¼öÇÑ ¿µ¾çºÐÀÌ °¡µæÇÑ ÇÇ´Â ¸ðµÎ °£À¸·Î ¿¬°áµÇ´Âµ¥ À̰ÍÀ» ¹®¸Æ°è(portal system)¶ó°í ÇÑ´Ù. °£°æÈÀÇ °æ¿ì¿¡´Â ¼¶À¯¼ºÁ¶Á÷ÀÌ °£Á¶Á÷À» °ÅÀÇ ´ëÄ¡ÇÔÀ¸·Î Á¤»ó °£¼¼Æ÷³»¿¡¼± ³ÐÀº °ø°£À» Â÷ÁöÇÏ´ø °£³»ÀÇ Ç÷°üµéÀÌ ¼¶À¯Á¶Á÷¿¡ ´¸®°Ô µÈ´Ù. ±×·¯¸é À̰Ͱú ¿¬°áµÈ ¹®¸Æ°èÀÇ ¾Ð·Âµµ ³ô¾ÆÁö°Ô µÈ´Ù. ¹®¸Æ¾ÐÀÇ »ó½ÂÀÌ ÀÖ´Â °æ¿ì¿¡´Â ¹®¸Æ°è¿¡ ¿¬°áÀÌ µÇ¾î ÀÖ´Â ¸ðµç ºÎºÐÀÇ Á¤¸ÆÀÇ ¾Ð·ÂÀÌ ³ô¾ÆÁö°í Á¤¸ÆÀÇ ¼øÈ¯ÀÌ Á¤ÁöµÈ »óŰ¡ µÈ´Ù. Áö¶óÀÇ °æ¿ìµµ ¹®¸Æ°è¿¡ ¿¬°áµÈ Àå±âÀ̹ǷΠ¹®¸Æ¾Ð »ó½Â½Ã¿¡´Â Á¤¸ÆÀÇ ¼øÈ¯ÀÌ ¾ø¾îÁö°í, µ¿¸ÆÀ¸·Î À¯ÀÔÀÌ µÇ´Â Ç÷¾×Àº °è¼Ó µé¾î¿À¹Ç·Î Áö¶óÀÌ Ä¿Áö°Ô µÈ´Ù. ¶Ç ¼ÒȱâÀÇ ¸ð¼¼Ç÷°ü³»¿¡¼ÀÇ ¾Ð·Âµµ ³ô¾ÆÁö°Ô µÇ°í ±×·¯¸é ±× ¾Ð·Â¿¡ ÀÇÇØ¼ ¸¹Àº ¾çÀÇ ¼öºÐÀÌ ¸ð¼¼Ç÷°ü¹ÛÀ¸·Î ºüÁ®³ª¿À°Ô µÈ´Ù. ÀÌ ¼öºÐÀÌ ¸ð¿© º¹¼ö°¡ µÈ´Ù. |
||
| ¿µ¹® | liver function tests | ÇÑ±Û | °£±â´É°Ë»ç |
|---|---|---|---|
| ¼³¸í | Ç÷¾×°Ë»çÁß °¡Àå ¸¹ÀÌ ¾²ÀÌ´Â °Ë»ç¹ýÀ¸·Î ´ÙÀ½ 7°¡Áö¸¦ °Ë»çÇÏ°Ô µÈ´Ù. Ç÷ûÄÝ·¹½ºÅ×·Ñ, ÃѴܹéÁú, ¾ËºÎ¹Î, ºô¸®·çºó, GOT/GPT È¿¼Ò, ¾ËÄ®¸®ÀλêºÐÇØÈ¿¼Ò(alkaline phophatase) µîÀ» °Ë»çÇÏ°Ô µÇ´Â µ¥ °¢ °Ë»çÄ¡¿¡´Â ¸ðµÎ Àǹ̰¡ ÀÖÀ¸¸ç, ÀÌ °Ë»ç Çϳª·Î °£±â´ÉÀÇ Àü¹ÝÀûÀÎ »óÅ¿¡ ´ëÇØ¼ ¾Ë¾Æº¼ ¼ö ÀÖ´Ù. |
||
| ¿µ¹® | liver biopsy | ÇÑ±Û | °£»ý°Ë |
|---|---|---|---|
| ¼³¸í | »ç¶÷ÀÌ »ì¾ÆÀÖ´Â »óÅ¿¡¼ º´Å͸¦ Àß¶ó³»¾î Á÷Á¢ Çö¹Ì°æ µîÀ¸·Î º¸¾Æ Áø´ÜÀ» ³»¸®´Â Áø´Ü¹ýÀÌ´Ù. °£»ý°ËÀº ÁÖ·Î °£¿°À̳ª °£¾ÏÀÇ Áø´ÜÀ̳ª, Èñ±ÍÇÑ À¯Àüº´, ¼±Ãµº´ µîÀÇ È®Áø¿¡ ÀÌ¿ëµÈ´Ù. °£¿°¿¡¼´Â ÇöÀçÀÇ °£¿°ÀÌ ÁøÇ༺ÀÎÁö ȤÀº ºñÁøÇ༺ÀÎÁö ¶Ç´Â ÀÌ¹Ì °£°æÈ»óÅ·Π³Ñ¾î°¬´ÂÁö µîÀÇ ¿©ºÎ¸¦ ¾Ë¾Æº¸°Ô µÈ´Ù. |
||
| AFP | Alpha(¥á) Feto-Protein [HP 1826, 1858, 1859, 2265] ; Oncofetal Antigens &nbs... |
|---|---|
| MD | Doctor of Medicine [Lat. Medicinae Doctor]; magnesium deficiency; main duct; maintenance dose; major... |
| IGD | idiopathic growth hormone deficiency; interglobal distance; isolated gonadotropin deficiency |
| MCD | magnetic circular dichroism; mast-cell degranulation; mean cell diameter; mean of consecutive differ... |
| CLD | chloride diarrhea; chronic liver disease; chronic lung disease; congenital limb deficiency; crystal ... |
| GP | Glycogen Phosphorylase |
|---|---|
| MTAP | Methylthioadenosine phosphorylase |
| NP | Nucleoside phosphorylase |
| PHK | Phosphorylase kinase |
| PD-ECGF/TP | Platelet-derived endothelial cell growth factor/thymidine phosphorylase |
| muscle phosphorylase deficiency | Type V glycogen storage disease, affecting muscle, caused by deficiency of muscle phosphorylase. (05 Mar 2000) |
|---|---|
| alpha,alpha-trehalose phosphorylase | <enzyme> Chemical name: alpha-d-glucopyranosyl-alpha-d-glucopyranose orthophosphate glucosyltransferase Registry number: EC 2.4.1.64 Synonym: trehalose phosphorylase (26 Jun 1999) |
| alpha-glucan phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| maltodextrin phosphorylase | <enzyme> From E coli Registry number: EC 2.4.1.- Synonym: e350a (26 Jun 1999) |
| GDPmannose phosphorylase | <enzyme> A transferase that catalyses the transfer of GDP to the mannose of mannose-1-phosphate. Consider also the bifunctional enzyme, phosphomannose isomerase-guanosine diphospho-d-mannose pyrophosphorylase; rfbm has similarity to long-chain, iron-containing alcohol dehydrogenases Registry number: EC 2.7.7.13 Synonym: GDPmannose phosphorylase, GDP mannose pyrophosphorylase, GTP-alpha-d-mannose-1-phosphate guanylyltransferase, GDP-mannose pyrophosphorylase, rfbm gene product, rfbm protein (26 Jun 1999) |
| cellodextrin phosphorylase | <enzyme> Reverse reaction is used to synthesise cellodextrins Registry number: EC 2.4.1.49 (26 Jun 1999) |
| glycogen phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| phosphorylase a | <enzyme> The phosphorylated and more active form of phosphorylase that functions as a regulatory enzyme during glycogen breakdown. The phosphate groups are hydrolytically removed by phosphorylase phosphatase to form phosphorylase b and orthophosphate. Registry number: EC 2.4.1.- (12 Dec 1998) |
| phosphorylase b | <enzyme> The relatively inactive form of phosphorylase that is reactivated to form phosphorylase a by phosphorylase kinase, which catalyses the enzymatic phosphorylation of the serine residues at the expense of ATP. Registry number: EC 2.4.1.- (12 Dec 1998) |
| phosphorylase kinase | <enzyme> The enzyme that regulates the activity of phosphorylase and glycogen synthetase by addition of phosphate groups. A large and complex enzyme, itself regulated by phosphorylation. Integrates the hormonal and calcium signals in muscle. (18 Nov 1997) |
| phosphorylase kinase phosphatase | <enzyme> Aspect of phosphoprotein phosphatase EC 3.1.3.16 Registry number: EC 3.1.3.- (26 Jun 1999) |
| phosphorylase phosphatase | <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. Chemical name: (Phosphorylase a) phosphohydrolase Registry number: EC 3.1.3.17 (12 Dec 1998) |
| phosphorylase-rupturing enzyme | <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. Chemical name: (Phosphorylase a) phosphohydrolase Registry number: EC 3.1.3.17 (12 Dec 1998) |
| polynucleotide phosphorylase | <enzyme> An enzyme of the transferase class that catalyses the reaction RNA(n+1) and orthophosphate to yield RNA(n) and a nucleoside diphosphate, or the reverse reaction. ADP, idp, GDP, udp, and cdp can act as donors in the latter case. Chemical name: Polyribonucleotide:orthophosphate nucleotidyltransferase Registry number: EC 2.7.7.8 (12 Dec 1998) |
| liver phosphorylase deficiency |
glycogen storage disease, type VI.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
|
|---|
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|
Á¦Ç°¸í |
ÆÇ¸Å»ç |
º¸ÇèÄÚµå | ¼ººÐ/ÇÔ·® | ±¸ºÐ/º¸Çè±Þ¿© |
|---|