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纤维蛋白原诱导的红细胞聚集:纤维蛋白原分子中的红细胞结合位点。

Fibrinogen-induced erythrocyte aggregation: erythrocyte-binding site in the fibrinogen molecule.

作者信息

Maeda N, Seike M, Kume S, Takaku T, Shiga T

机构信息

Department of Physiology, School of Medicine, Ehime University, Japan.

出版信息

Biochim Biophys Acta. 1987 Nov 2;904(1):81-91. doi: 10.1016/0005-2736(87)90089-7.

DOI:10.1016/0005-2736(87)90089-7
PMID:2959322
Abstract

The effect of fibrinogen and fibrinogen-derived products on the velocity of rouleau formation of human erythrocytes was quantitatively examined with a rheoscope combined with a video-camera, an image analyzer and a computer. (i) The velocity of rouleau formation by naturally occurring low-molecular-weight fibrinogen of 305 kDa and by desialylated fibrinogen was the same as that by native fibrinogen of 340 kDa. (ii) Concerning fibrinogen degradation products by plasmin, the velocity of rouleau formation decreased upon going from fibrinogen greater than fragment X greater than fragment Y (the ratio of molar concentration of fibrinogen, fragment X and fragment Y for giving a certain velocity of rouleau formation was approx. 1:2:5). The effect of fragments X and Y on the fibrinogen-induced rouleau formation was additive. (iii) Fragments D and E could not induce rouleau formation and did not affect the fibrinogen-, fragment X- and fragment Y-induced rouleau formation. (iv) Fibrinopeptides A and B and artificial tetrapeptides (Gly-Pro-Arg-Pro and Gly-His-Arg-Pro) did not affect the fibrinogen-induced rouleau formation. (v) The possible erythrocyte-binding site in fibrinogen molecule for leading to rouleaux was proposed to be in A alpha-chain (probably, around residues No. 207-303) near the terminal domain of the trinodular structure of fibrinogen.

摘要

使用结合了摄像机、图像分析仪和计算机的血流仪,定量检测了纤维蛋白原及其衍生产品对人红细胞缗钱状形成速度的影响。(i)305 kDa的天然低分子量纤维蛋白原和去唾液酸化纤维蛋白原的缗钱状形成速度与340 kDa的天然纤维蛋白原相同。(ii)关于纤溶酶产生的纤维蛋白原降解产物,从纤维蛋白原到大于X片段大于Y片段,缗钱状形成速度降低(为达到一定缗钱状形成速度,纤维蛋白原、X片段和Y片段的摩尔浓度比约为1:2:5)。X片段和Y片段对纤维蛋白原诱导的缗钱状形成的影响是相加的。(iii)D片段和E片段不能诱导缗钱状形成,也不影响纤维蛋白原、X片段和Y片段诱导的缗钱状形成。(iv)纤维蛋白肽A和B以及人工四肽(甘氨酸-脯氨酸-精氨酸-脯氨酸和甘氨酸-组氨酸-精氨酸-脯氨酸)不影响纤维蛋白原诱导的缗钱状形成。(v)纤维蛋白原分子中可能导致缗钱状形成的红细胞结合位点被认为位于纤维蛋白原三结节结构末端结构域附近的Aα链(可能在第207 - 303位残基附近)。

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Fibrinogen-induced erythrocyte aggregation: erythrocyte-binding site in the fibrinogen molecule.纤维蛋白原诱导的红细胞聚集:纤维蛋白原分子中的红细胞结合位点。
Biochim Biophys Acta. 1987 Nov 2;904(1):81-91. doi: 10.1016/0005-2736(87)90089-7.
2
Inhibition of fibrin polymerization by fragment d is affected by calcium, Gly-Pro-Arg and Gly-His-Arg.片段D对纤维蛋白聚合的抑制作用受钙、甘氨酰-脯氨酰-精氨酸和甘氨酰-组氨酰-精氨酸的影响。
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[Action of proteolytic enzymes on fibrinogen].[蛋白水解酶对纤维蛋白原的作用]
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Regulation of fibrinogen biosynthesis: effect of fibrin degradation products, low-molecular-weight peptides of fibrinogenolysis, and fibrinopeptides A and B.纤维蛋白原生物合成的调控:纤维蛋白降解产物、纤维蛋白溶解的低分子量肽以及纤维蛋白肽A和B的作用
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Generation of forms of fragment E with differing thrombin-binding properties during digestion of fibrinogen by plasmin.纤溶酶消化纤维蛋白原过程中具有不同凝血酶结合特性的片段E形式的产生。
Biochem J. 1992 Feb 1;281 ( Pt 3)(Pt 3):613-8. doi: 10.1042/bj2810613.
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Contribution of glycoproteins to fibrinogen-induced aggregation of erythrocytes.糖蛋白对纤维蛋白原诱导的红细胞聚集的作用。
Biochim Biophys Acta. 1990 Feb 16;1022(1):72-8. doi: 10.1016/0005-2736(90)90401-9.
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Erythrocyte aggregation: bridging by macromolecules and electrostatic repulsion by sialic acid.红细胞聚集:由大分子桥接和唾液酸的静电排斥作用。
Biochim Biophys Acta. 1991 Aug 26;1067(2):221-6. doi: 10.1016/0005-2736(91)90047-c.
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Fibrinogen and platelet aggregation. Role of the glycopeptidic part and of the fibrinopeptide B. Description of a new technique of fibrinoglycopeptide isolation.纤维蛋白原与血小板聚集。糖肽部分及纤维蛋白肽B的作用。一种纤维蛋白糖肽分离新技术的描述。
Biochem Biophys Res Commun. 1978 May 30;82(2):442-50. doi: 10.1016/0006-291x(78)90895-1.
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Fibrinogen Barcelona I. Congenital dysfibrinogenemia characterized by defective release of fibrinopeptide A and fibrinogen degradation products.纤维蛋白原巴塞罗那I型。以纤维蛋白肽A释放缺陷和纤维蛋白原降解产物为特征的先天性异常纤维蛋白原血症。
Thromb Res. 1987 Mar 1;45(5):437-49. doi: 10.1016/0049-3848(87)90307-0.

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