| ¿µ¹® | bone | ÇÑ±Û | »À, °ñ |
|---|---|---|---|
| ¼³¸í | ±¸¼º£»À(»ÀÁ¶Á÷). ÀÌ Á¶Á÷Àº ±²ÀåÈ÷ ´Ü´ÜÇÑ Á¶Á÷À¸·Î »À¸ð¼¼Æ÷¿¡ ÀÇÇØ¼ »ý¼ºµÈ´Ù. »À¸ð¼¼Æ÷°¡ »ý¼ºÇÑ ÀÌ Á¶Á÷Àº »À¼¼Æ÷¶ó´Â ¼¼Æ÷¸¦ µ¿½É¿ø¸ð¾çÀ¸·Î ½×°í ÀÖ´Ù. žƽñ⿡´Â ¸ðµç »À°¡ ¿¬°ñÁ¶Á÷À¸·Î µÇ¾îÀÖ´Ù. ÀÌ·± ¿¬°ñÁ¶Á÷ÀÌ ¹ß»ýÇÏ¸é¼ Á¡Á¡ Ä®½·¿°ÀÇ Ä§Âø¿¡ ÀÇÇØ¼ »ÀÁ¶Á÷ÀÌ »ý±ä´Ù. ±×¸®°í ¾î¸°ÀÌÀÇ °æ¿ì¿¡´Â »À³¡ÆÇ(epiphyseal plate)¶ó´Â °÷ÀÌ Àִµ¥ À̰÷µµ ¿ª½Ã ¿¬°ñÁ¶Á÷À¸·Î µÇ¾îÀÖ¾î¼ Áö¼ÓÀûÀ¸·Î ¿¬°ñÁ¶Á÷À» ¸¸µé°í Ä®½·¿°ÀÇ Ä§ÂøÀÌ »ý°Ü¼ »ÀÀÇ ¼ºÀåÀÌ µÈ´Ù. ¾çÂÊ¿¡ ³Ð¾îÁø °÷À» »À³¡(epiphysis)¶ó°í ÇÏ°í ¸·´ë¸ð¾çÀÇ Áß°£ºÎºÐÀ» »À¸öÅë(diaphysis)¶ó°í Çϰí ÀÌ ¾çÂÊÀÇ ÀÌÇàºÎÀ§¸¦ »À¸öÅ볡(metaphysis)¶ó°í ÇÑ´Ù. »À³¡°ú »À¸öÅ볡ÀÇ °æ°èºÎÀ§¿¡ ¾î¸°ÀÌ¿¡°Ô¼± »À³¡ÆÇ(epiphyseal plate)¶ó´Â °ÍÀÌ Á¸ÀçÇϴµ¥, À̰÷Àº ¿¬°ñÁ¶Á÷À¸·Î µÇ¾îÀÖÀ¸¸ç »ÀÀÇ ±æÀ̼ºÀå¿¡ Áß¿äÇÑ ¿ªÇÒÀ» ÇÏ´Â °ÍÀÌ´Ù. ¾î¸¥ÀÌ µÇ¸é À̰÷ÀÇ ¿¬°ñÁ¶Á÷Àº ¸ðµÎ °ñÁ¶Á÷À¸·Î º¯ÈµÇ¾î ÁÙ¸ð¾çÀÇ ÈçÀûÀÌ ³²´Âµ¥, À̰ÍÀ» »À³¡¼±À̶ó°í ÇÑ´Ù. ±ä»À¸¦ Àý´ÜÇØ º¸¸é °ÑÀ¸·Î´Â ¸Å¿ì ´Ü´ÜÇϰí Á¶Á÷ÀÌ Ä¡¹ÐÇϰí, ±× ¾ÈÂÊ¿¡´Â °Ñ¿¡ ºñÇØ¼ ¹«¸£°í, Á¶Á÷ÀÌ ¼º±ä °÷ÀÌ ÀÖ´Â °É ¾Ë ¼ö°¡ ÀÖ´Ù. °ÑÀÇ ´Ü´ÜÇÑ °÷À» Ä¡¹Ð»À(compact bone) ȤÀº °ÑÁú»À(cortical bone)À̶ó°í ÇÑ´Ù. ¿©±â¿¡´Â »ÀÁ¶Á÷ÀÌ µ¿½É¿ø ¸ð¾çÀ» ÀÌ·ç°í Ä¡¹ÐÇÏ°Ô ¹è¿µÇ¾î ÀÖ°í ±× µ¿½É¿ø ³»ºÎ¿¡´Â »À¼¼Æ÷°¡ À§Ä¡Çϰí ÀÖ´Ù. ±×¸®°í µ¿½É¿øÀÇ Áß°£¿¡´Â °üÀÌ ÀÖ¾î¼ À̰÷À» ÅëÇØ¼ Ç÷¾×°ú ¿µ¾çºÐÀÌ °ø±ÞµÇ´Âµ¥ À̰üÀ» Á߽ɰü(ÇϹö½º°ü)À̶ó°í ÇÑ´Ù. ±×¸®°í ³»ºÎ¿¡ À§Ä¡ÇÑ ¼º±ä °÷À» °¹¼Ø»À(Sponge Bone)À̶ó°í ÇÑ´Ù. ¿ª½Ã »ÀÁ¶Á÷À¸·Î ÀÌ·ç¾îÁø °÷ÀÌÁö¸¸ ±× ¹è¿ÀÌ Ä¡¹Ð»À¿¡ ºñÇØ¼ ¼º±â°í ¿ÜºÎÀÇ Èû¿¡ ´ëÇÑ ÀúÇ×µµ ¾àÇÑ Á¶Á÷ÀÌ´Ù. ÀÌ Á¶Á÷ÀÇ ³»ºÎ¿¡´Â Ç÷¾×ÀÇ ¼¼Æ÷¸¦ »ý¼ºÇÏ´Â °ñ¼ö¶ó´Â °ÍÀÌ Á¸ÀçÇÑ´Ù. ªÀº »À(short bone)£¼Õ¸ñÀ̳ª ¹ß¸ñ¿¡¼ º¼ ¼ö Àִ ª°í ¸ð¾çÀÌ ºÒ±ÔÄ¢ÇÑ »À. ³³ÀÛ»À(flat bone)£¸Ó¸®³ª °ñ¹ÝÀÇ »À¿Í °°ÀÌ ³³ÀÛÇÑ ¸ð¾çÀÇ »À. Á¾ÀÚ»À(sesamoid bone)£ÀÛ°í ±¸ÇüÀÎ »À. °üÀýÁÖÀ§¿¡ Á¸ÀçÇÑ´Ù. °³°³Àο¡ µû¶ó¼ Á¸ÀçÇϱ⵵ ÇÏ°í ±×·¸Áö ¾Ê±âµµ ÇÑ´Ù. |
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| ¿µ¹® | bone age | ÇÑ±Û | »À³ªÀÌ, °ñ¿¬·É |
|---|---|---|---|
| ¼³¸í | »ý¸®Àû ¿¬·ÉÀÇ ÀÏÁ¾À¸·Î ³ªÀ̸¦ ´õÇÔ¿¡ µû¸¥ »ÀÀÇ ¼º¼÷µµ¸¦ Æò°¡ÇÏ¿© ¾î¸°ÀÌÀÇ Àü½Å¹ßÀ°À» ÆÇÁ¤ÇÏ´Â °ÍÀÌ´Ù. »À³ªÀÌ Æò°¡¿¡´Â ¼Õ¸ñ»À³ª ¹ß¸ñ»ÀÀÇ X¼±»çÁøÀ» ¹ÙÅÁÀ¸·Î °¢ ȰñÁß½ÉÀÇ Çüųª ¼ö¸¦ Æò°¡ÇÑ´Ù. ¼Õ¸ñ»ÀÀÇ È°ñ°³¼ö¸¦ ¼¼´Â ¹æ¹ýÀº °£´ÜÇØ¼ ±×ÀÇ ¼ö´Â ³ ÇØ¸¦ Æ÷ÇÔÇÑ ¿¬·É°ú °ÅÀÇ ÀÏÄ¡ÇÏÁö¸¸ »À¹ßÀ°ÀÇ Áö¼ÓÀ» °¡´ÆÇÒ ¼ö ÀÖ´Ù. |
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| ¿µ¹® | bone scan | ÇÑ±Û | »À½ºÄµ |
|---|---|---|---|
| ¼³¸í | »ÀÀÇ ¹«±âÁúÀº Ä®½·°ú Àλ꿰À¸·Î ÀÌ·ç¾îÁ® ÀÖ´Ù. ±×·¡¼ »À¿¡ º´ÅͰ¡ ÀÖ´Â °æ¿ì¿¡´Â »ÀÀÇ Àλ꿰ºÐÆ÷³ª ¾çÀÌ º¯ÈÇÏ°Ô µÈ´Ù. À̰ÍÀ» ÀÌ¿ëÇÏ¿© Àλ꿰¿¡´Ù°¡ ¹æ»ç¼±À» ³»º¸³»´Â ¹°ÁúÀ» ºÙ¿© ȯÀÚ¿¡°Ô Åõ¿©ÇÏ°í ±× ¹°ÁúÀÌ ³»º¸³»´Â ¹æ»ç¼±À» ÀÌ¿ëÇÏ¿© ¿µ»óÀ» ¸¸µé¾î¼ »ÀÀÇ Àü¹ÝÀûÀÎ »óųª º´ÅÍÀÇ ¹ß°ß¿¡ ÀÌ¿ëÇÏ´Â ¹æ¹ýÀ» »À½ºÄµ(bone scan)À̶ó°í ÇÑ´Ù. |
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| ¿µ¹® | mandibular bone, mandible | ÇÑ±Û | ¾Æ·¡ÅλÀ, ÇϾǰñ |
|---|---|---|---|
| ¼³¸í | ¾ó±¼À» ±¸¼ºÇÏ´Â »ÀÀÇ ÇÑ Á¾·ù·Î½á, ÈçÈ÷ ¸»ÇÏ´Â "ÅÎ"À» ÀÌ·ç´Â »À¸¦ ¸»ÇÑ´Ù. ¾ó±¼»À¸¦ ÀÌ·ç´Â »À´Â À§ÅλÀ(maxillary bone), ¾Æ·¡»À(mandibular bone), ´«¹°»À(lacrimal bone), ÄÚ»À(nasal bone), ±¤´ë»À(zygomatic bone), º¸½À»À(vomer) µîÀÌ ÀÖ´Ù. |
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| ¿µ¹® | red bone marrow | ÇÑ±Û | Àû»ö°ñ¼ö |
|---|---|---|---|
| ¼³¸í | ºÐÈÁßÀÇ °¥ºñ»À, ôÃß»À³ª ±× ¿ÜÀÇ ¸¹Àº ÀÛÀº »À¿¡ Àִ Ȱµ¿¼º °ñ¼öÀÌ´Ù. ÀûÇ÷±¸³ª °ú¸³¹éÇ÷±¸ÀÇ »ý»ê Àå¼ÒÀÌ´Ù. |
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| RA | radioactive; ragocyte; ragweed antigen; rapidly adapting [receptors]; reactive arthritis; reciprocal... |
|---|---|
| ALL | Acute Lymphocytic Leukemia ÇüÅÂÇÐÀû ºÐ·ù L1; Small, Homogenous(... |
| MEN | Multiple Endocrine Neoplasia ; AD Trait 1. MEN Type I(= Wermer Syndro... |
| ABC | absolute basophil count; absolute bone conduction; acalculous biliary colic; acid balance control; a... |
| ABCDES | abnormal alignment, bones-periarticular osteoporosis, cartilage-joint space loss, deformities, margi... |
| receptors, adrenergic, alpha | One of the two major pharmacological subdivisions of adrenergic receptors. The alpha-beta distinction was originally based on cellular effects of receptor activation but now relies on the relative affinities for certain synthetic ligands. Alpha-adrenergic receptors are further subdivided into several subclasses based on studies of endogenous and cloned receptors. (12 Dec 1998) |
|---|---|
| receptors, adrenergic, alpha-1 | A subclass of alpha-adrenergic receptors (receptors, adrenergic, alpha). Alpha-1 adrenergic receptors can be pharmacologically discriminated, e.g., by their high affinity for the agonist phenylephrine and the antagonist prazosin. They are widespread, with clinically important concentrations in the liver, the heart, vascular, intestinal, and genitourinary smooth muscle, and the central and peripheral nervous systems. (12 Dec 1998) |
| receptors, adrenergic, alpha-2 | A subclass of alpha-adrenergic receptors (receptors, adrenergic, alpha). Alpha-2 adrenergic receptors can be pharmacologically discriminated, e.g., by their high affinity for the agonist clonidine and the antagonist yohimbine. They are found on pancreatic beta cells, platelets, and vascular smooth muscle, as well as both pre- and postsynaptically in the central and peripheral nervous systems. (12 Dec 1998) |
| receptors, adrenergic, beta | One of the two major pharmacologically defined classes of adrenergic receptors. The alpha-beta distinction was originally based on the cellular effects of receptor activation but now relies on the relative affinities for characteristic synthetic ligands. Beta adrenergic receptors are further subdivided based on information from endogenous and cloned receptors. (12 Dec 1998) |
| receptors, adrenergic, beta-1 | A subclass of beta-adrenergic receptors (receptors, adrenergic, beta). Beta-1 adrenergic receptors are equally sensitive to epinephrine and norepinephrine and bind the agonist dobutamine and the antagonist metoprolol with high affinity. They are found in the heart, juxtaglomerular cells, and in the central and peripheral nervous systems. (12 Dec 1998) |
| receptors, adrenergic, beta-2 | A subclass of beta-adrenergic receptors (receptors, adrenergic, beta). Beta-2 adrenergic receptors are more sensitive to epinephrine than to norepinephrine and have a high affinity for the agonist terbutaline. They are widespread, with clinically important roles in skeletal muscle, liver, and vascular, bronchial, gastrointestinal, and genitourinary smooth muscle. (12 Dec 1998) |
| receptors, albumin | Cell surface proteins that bind albumin with high affinity and trigger intracellular changes influencing the behaviour of cells. (12 Dec 1998) |
| receptors, aldosterone | Cytoplasmic proteins that specifically bind aldosterone and mediate its cellular effects. The aldosterone-bound receptor acts in the nucleus to regulate the transcription of specific segments of DNA. (12 Dec 1998) |
| receptors, amino acid | Cell surface proteins that bind amino acids and trigger changes which influence the behaviour of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and gaba and glycine receptors are the most common receptors for fast inhibition. (12 Dec 1998) |
| receptors, ampa | Cell surface proteins that bind glutamate and directly gate ion channels in cell membranes. Ampa receptors were originally discriminated from other glutamate receptors by their affinity for the agonist ampa (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid). They are probably the most common mediators of fast excitatory synaptic transmission in the central nervous system. Several subtypes have been cloned, and for some types the traditional distinction from kainate receptors may not apply. (12 Dec 1998) |
| receptors, androgen | Proteins, generally found in the cytoplasm, that specifically bind androgens and mediate their cellular actions. The complex of the androgen and receptor migrates to the nucleus where it induces transcription of specific segments of DNA. (12 Dec 1998) |
| receptors, angiotensin | Cell surface proteins that bind angiotensins and trigger intracellular changes influencing the behaviour of cells. (12 Dec 1998) |
| receptors, antigen | Molecules on the surface of b- and T-lymphocytes that recognise and combine with specific antigens. (12 Dec 1998) |
| receptors, antigen, B-cell | Immunoglobulin molecules on the surface of B-lymphocytes that recognise and bind antigen. (12 Dec 1998) |
| receptors, antigen, T-cell | Molecules on the surface of T-lymphocytes that recognise and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (antigens, CD3). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (receptors, antigen, T-cell, alpha-beta) or gamma-delta (receptors, antigen, T-cell, gamma-delta) chains. (12 Dec 1998) |
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