| 영문 | hyaline membrane disease | 한글 | 유리질막병 |
|---|---|---|---|
| 설명 | 허파 성숙도의 미숙으로 허파꽈리를 팽창시키는 물질(표면활성제)이 부족하여 호흡곤란이 초래되는 병으로서 미숙아에 호발하는데, 출생시 임신기간보다도 허파 성숙 정도가 더 관여된다. 단일 병으로서는 사망률이 가장 높으며(약 30%), 신생아의 대표적인 병이다. 임상적으로는 미숙아, 생후 6~8시간내 호흡곤란증세 출현과 생후 24~48시간의 증상 악화, 생후 2~3일간 인공적으로 산소를 공급하지 않으면 호흡을 계속시킬 수가 없으며 점점더 산소의 공급 의존도가 높아지며, 동맥혈액속의 산소농도가 내려가고 이산화탄소의 농도가 높으며, 흉부 방사선 소견을 참작하여 진단한다. 환아는 숙련된 간호 인력과 첨단 의료 장비가 설치된 신생아 집중 치료실에서 치료하여야 한다. 예후는 증세의 경중에 따라 다르고 사망률은 30~50% 된다. 어떤 아기에 있어서는 치료 후에 눈이나 기관지허파 계통에 장애를 일으키는 산소중독증이 보고되고 있다. |
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| 영문 | plasma membrane | 한글 | 형질막 |
|---|---|---|---|
| 설명 | 원형질 표면을 덮는 엷은막. 두께는 5~25μm이다. 광학현미경으로는 관찰할 수 없지만 전자현미경으로 관찰이 가능하다. 원형질막의 분자구조는 레시틴이나 콜레스테롤 등의 표면 활성물질 분자가 2분자층으로 그 표면에 배열되며, 이것을 각 1분자층의 단백질 분자가 양쪽에서 샌드위치한 단위막 구조이다. 전자현미경적으로 이 단위는 암-명-암의 3층(각 약 20nm)으로 구별된다. 원형질의 투과성에 중요한 구실을 하며, 생리상태가 변하면 그 투과성도 신속히 변한다. 또, 손상이 되면 쉽게 새로 형성된다. |
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| SC | conditioned stimulus; sacrococcygeal; Sanitary Corps; scalenus [muscle]; scapula; Schwann cell; scia... |
|---|---|
| TCC | terminal complement complex; thromboplastic cell component; transitional-cell carcinoma; trichloroca... |
| APSAC | 1) Acylating the Plasminogen Streptokinase Activated Complex 2) Anisoylat... |
| APSAC | acylated plasminogen-streptokinase activator complex; anisoylated plasminogen streptokinase activato... |
| ARC | accelerating rate calorimetry; acquired immunodeficiency syndrome-related complex; active renin conc... |
| receptors, complement 3d | Molecular sites on or in B-lymphocytes, follicular dendritic cells, lymphoid cells, and epithelial cells that recognise and combine with complement 3d. Human cr2 serves as a receptor for both c3dg and the gp350/220 glycoprotein of herpes virus 4, human, and binds the monoclonal antibody okb7, which blocks binding of both ligands to the receptor. (12 Dec 1998) |
|---|---|
| chromosome complement | The whole set of chromosomes for the species. In humans, the chromosome complement (which is also called the karyotype) consists of 46 chromosomes. (12 Dec 1998) |
| complement | <immunology> A term originally used to refer to the heat labile factor in serum that causes immune cytolysis, the lysis of antibody coated cells and now referring to the entire functionally related system comprising at least 20 distinct serum proteins that is the effector not only of immune cytolysis but also of other biologic functions. Complement activation occurs by two different sequences, the classic and alternative pathways. The proteins of the classic pathway are termed components of complement and are designated by the symbols C1 through C9. C1 is a calcium dependent complex of three distinct proteins C1q, C1r and C1s. The proteins of the alternative pathway (collectively referred to as the properdin system) and complement regulatory proteins are known by semisystematic or trivial names. Fragments resulting from proteolytic cleavage of complement proteins are designated with lower case letter suffixes, for example, C3a. Inactivated fragments may be designated with the suffix i, for example C3bi. Activated components or complexes with biological activity are designated by a bar over the symbol for example C1 or C4b, 2a. The classic pathway is activated by the binding of C1 to classic pathway activators, primarily antigen-antibody complexes containing IgM, IgG1, IgG3, C1q binds to a single IgM molecule or two adjacent IgG molecules. The alternative pathway can be activated by IgA immune complexes and also by nonimmunologic materials including bacterial endotoxins, microbial polysaccharides and cell walls. Activation of the classic pathway triggers an enzymatic cascade involving C1, C4, C2 and C3, activation of the alternative pathway triggers a cascade involving C3 and factors B, D and P. Both result in the cleavage of C5 and the formation of the membrane attack complex. Complement activation also results in the formation of many biologically active complement fragments that act as anaphylatoxins, opsonins or chemotactic factors. (05 Jan 1998) |
| complement 1 | The first complement component to act in the cytolysis reaction. It is a trimolecular complex held together with ca ions and when activated, has esterase activity which initiates the next step in the sequence. (12 Dec 1998) |
| complement 1 inactivators | Compounds which inhibit, antagonise, or inactivate complement 1. A well-known inhibitor is a serum glycoprotein believed to be alpha-2-neuroaminoglycoprotein. It inhibits the activated (esterase) form of complement 1 as well as kinin-forming, coagulation, and fibrinolytic systems. Deficiency of this inactivator has been found in patients with hereditary angioneurotic oedema. These compounds are members of the serpin superfamily. (12 Dec 1998) |
| complement 1q | <chemical> Subcomponent of complement 1 (c1) which recognises and binds to the heavy chain of IgG or IgM initiating the classical complement pathway. The interaction of c1q and immunoglobulin activates c1r and c1s. The activated c1r and c1s molecules are cleaved off the complex by c1-inhibitor, allowing the collagen-like region of c1q to become accessible for interaction with cell membrane c1q receptors. Chemical name: Complement C1q (12 Dec 1998) |
| complement 1r | <enzyme> Subcomponent of complement 1 which, when activated by c1q, activates subcomponent c1s by proteolytic cleavage. Registry number: EC 3.4.21.41 (12 Dec 1998) |
| complement 1s | <enzyme> The activated form of complement 1 which has hydrolase activity. In the classical pathway, it splits first c4 and then c2 into active components, thereby generating a new enzyme referred to as eac142 or c42 or c3 convertase. Registry number: EC 3.4.21.42 (12 Dec 1998) |
| complement 2 | The third component in the complement reaction sequence. It is a beta-globulin with a molecular weight of 117,000, a serum concentration of 30 micrograms/ml and a sedimentation coefficient of 4. It activates c3. (12 Dec 1998) |
| complement 3 | The fourth component to attach in the complement reaction sequence. It is a beta-globulin with a sedimentation coefficient of 5.5, a molecular weight of 185,000 and a serum concentration of 1.3 micrograms/ml. Its fragments have anaphylatoxic, chemotactic, and histaminic action and affect smooth muscle. (12 Dec 1998) |
| complement 3a | <chemical> Smaller fragment formed when c3 convertase splits c3 into c3a and c3b. C3a is a 77-amino acid peptide that includes a carboxy-terminal arginine which is crucial for its biological activities. C3a causes symptoms of immediate hypersensitivity (anaphylaxis) including smooth muscle contraction, mast cell histamine release, and local inflammation. It is considered an anaphylatoxin along with c4a, c5a, and c5a des-arginine. Chemical name: Complement C3a (12 Dec 1998) |
| complement 3b | <chemical> The larger fragment formed when c3 convertase splits c3 into c3a and c3b. In both the classical and alternate pathway, c3b participates in immune adherence and enhances phagocytosis. It also forms a cellular intermediate which continues the complement process. In the alternate pathways, c3b initiates a positive feedback activation of c3pase. Chemical name: Complement C3b (12 Dec 1998) |
| complement 3b inactivators | Compounds which inhibit, antagonise, or inactivate complement 3b. A well-known inhibitor is a beta-globulin which cleaves c3b into inactive fragments c3c and c3d. C3bina plays a key role in the regulation of the complement system by blocking the cytolytic sequence and preventing recruitment of the properdin amplification loop. (12 Dec 1998) |
| complement 3c | <chemical> An inactivated form of complement 3b (c3b). Complement 3b is inactivated with the help of two regulatory factors, complement factor h and complement factor I. Complement factor h (c3b inactivator accelerator) makes c3b susceptible to the serine protease, complement factor I (formerly called kaf, c3binf, or enzyme 3b inactivator), to form ic3b. Then complement factor I and a trypsin-like proteolytic enzyme further cleave ic3b into c3c and c3dg. Chemical name: Complement C3c (12 Dec 1998) |
| complement 3 convertase | <enzyme> The enzyme which in both the classical and alternate complement pathways cleaves complement 3 into anaphylatoxin (c3a) and c3b. Registry number: EC 3.4.21.43 (12 Dec 1998) |