颈动脉粥样硬化与脑梗死复发的关系

目的探讨颈动脉粥样硬化与脑梗死复发的关系。方法连续收集急性脑梗死住院患者268例,通过颈动脉彩超检查颈动脉粥样硬化情况,随访观察有无脑梗死复发。结果随访12个月内,268例脑梗死患者有25例（9.33%）复发脑梗死,复发和未复发脑梗死患者颈动脉斑块检出率差异无统计学意义（P〉0.05）;复发脑梗死患者低回声、混合性回声斑块的出现率及颈总动脉、颈动脉分叉处血管内中膜厚度值明显高于未复发患者（P〈0.05）。结论颈动脉内中膜厚度增厚及伴有低回声和混合密度回声斑块患者脑梗死复发率增高。     

缺血性脑卒中患者纤维蛋白原和C-反应蛋白水平与颈动脉粥样硬化的关系

目的 探讨缺血性脑卒中患者颈动脉粥样硬化与纤维蛋白原和高教C-反应蛋白水平的关系。方法 对缺血性脑卒中患者应用颈部多普勒超声检测颈部血管内中膜厚度覆斑块形成情况，并同期检测患者血纤维蛋白原和高敏C-反应蛋白浓度。结果 125例患者中40例发现有颈动脉粥样硬化病变，其中16例经超声检查诊断为颈动脉粥样硬化斑块，24例诊断为颈动脉内中膜增厚。颈动脉粥样硬化病变的患者平均纤维蛋白原和高敏C-反应蛋白水平显著高于无颈动脉粥样硬化组（P〈0．05和P〈0．01）。并且随着平均纤维蛋白原水平和高敏C-反应蛋白水平升高颈动脉粥样硬化病变的发生率升高。结论 缺血性脑卒中颈动脉粥样硬化和纤维蛋白原、高敏C-反应蛋白水平之间有密切的相关性。     

缺血性脑卒中患者颈动脉粥样斑块发生与踝肱指数相关性研究

目的：探讨缺血性脑卒中患者颈动脉粥样斑块发生与踝肱指数的相关性。方法对236例缺血性脑卒中患者（观察组）和260名健康人（对照组）应用彩色多普勒超声检测颈部血管内中膜厚度及斑块形成情况,使用多普勒超声仪测量踝肱指数,并分析踝肱指数与颈动脉粥样硬化的程度和稳定性的相关性。结果236例观察组患者中,检出颈动脉粥样硬化斑块183例（77．5％）,对照组为60例（23．1％）,缺血性脑卒中颈动脉粥样硬化斑块发生率明显高于对照组（P ＜0．01）。观察组22例踝肱指数异常,发生率为9．3％;对照组有 6例踝肱指数异常,发生率为2．3％,2组比较差异有统计学意义（P ＜0．01）。缺血性脑卒中患者颈动脉内膜增厚组踝肱指数明显低于正常组,颈动脉内膜斑块形成组患者的踝肱指数明显低于增厚组（P ＜0．05）,颈动脉内膜不稳定斑块组踝肱指数明显低于稳定斑块组（P ＜0．05）。Logistic 回归分析显示颈动脉粥样硬化斑块、踝肱指数与缺血性脑卒中明显相关（OR 分别为1．118、0．054,P 均＜0．05）。结论颈动脉粥样硬化与缺血性脑卒中有关,踝肱指数可作为预测缺血性脑卒中发生的指标之一。     

脑微出血与颈动脉粥样硬化相关性分析

目的探讨脑微出血与颈动脉粥样硬化的关系。方法以B超检测颈动脉，按动脉粥样硬化程度将患者分为：颈动脉正常组（正常组）78例、颈动脉内中膜增厚组（增厚组）46例、斑块组36例，共3组，各组同时作头部核磁共振MRI，常规行自旋回波T1和T2加权轴位扫描，梯度同波T2加权采用Flash序列，了解有无脑微出血。结果颈动脉正常组、增厚组、斑块组脑微出血发生分别为12、16、21例。脑微出血发生在颈动脉内中膜增厚组（增厚组）和斑块组较颈动脉正常组增高（P〈0.05）。结论脑微出血与颈动脉粥样硬化程度呈正相关，检测颈动脉B超对预测脑微出血有重要意义。     

颈动脉粥样硬化与急性脑梗死相关性的探讨

【目的】探讨颈动脉内中膜厚度（IMT）及斑块性质与急性脑梗死发生的相关性。【方法】将经CT或MRI确诊的64例急性脑梗死患者分为脑梗死侧组和非脑梗死侧组,应用彩色超声仪对患者的颈动脉进行检测,并进行颈动脉内中膜厚度及颈动脉粥样硬化不同性质斑块发生率和狭窄程度比较。【结果】脑梗死侧组脑梗死患者颈总动脉IMT及颈动脉斑块发生率比非脑梗死侧组明显高,两组之间有显著性差异（P〈0.05）。【结论】颈动脉粥样硬化性病变及斑块的病理性质与脑梗死密切相关,超声多普勒检测颈动脉粥样硬化及斑块可预测急性脑梗死的发生。     

彩超下探讨颈动脉斑块与脑梗死的相关性研究

目的:通过彩超分析颈动脉斑块,探讨其与脑梗死发病的相关性。方法:选择2016年5月-2018年5月邓州市中心医院收治的100例脑梗死患者和100例健康体检者分别作为观察组和对照组,应用彩色多普勒超声诊断仪分别检测和比较两组患者的内中膜厚度(IMT)、斑块类型、斑块形态以及斑块发病部位。结果:与对照组相比,观察组颈动脉内中膜增厚发生率(92%vs31%),内中膜厚度(1.3±0.4mm)vs(0.7±0.3mm),颈动脉粥样硬化斑块形成率显著增高(82%vs22%),斑块类型多为不稳定型软斑,发病部位多为颈总动脉分叉处。结论:颈动脉粥样硬化斑块形成与脑血管疾病密切相关,颈动脉粥样硬化是造成脑梗死的重要致病因素,通过彩超可以明确脑梗死患者颈动脉粥样硬化斑块特征,具有较高的诊断价值,并通过彩超早期筛查,可以早期发现脑梗死危险患者,预防脑梗死的发生。     

超声检测颈动脉粥样硬化与冠心病的相关性分析

目的：通过对颈动脉内中膜厚度及颈动脉粥样硬化斑块的检测，探讨颈动脉粥样硬化病变的发生与冠心病的关系。方法：应用彩色多普勒超声诊断仪测定160例患者的颈动脉内中膜厚度及观察粥样斑块的发生情况，冠心病组110例，对照组50例。结果：冠心病组颈动脉内中膜厚度明显大于对照组（P〈0．01）。颈动脉粥样硬化斑块检出率明显高于对照组（P〈0．01）。结论：颈动脉与冠状动脉粥样硬化间存在着密切关系，超声测定颈动脉内中膜厚度可作为预测冠心病的非侵入性检查手段。     

颈动脉粥样硬化与脑梗死复发临床关系探讨

目的探讨颈动脉粥样硬化与脑梗死复发的关系。方法收集脑梗死住院患者241例,通过颈动脉彩超检查颈动脉粥样硬化情况,随访观察有无脑梗死复发。结果 241例脑梗死患者有23例复发性脑梗死,脑梗死复发和未复发患者颈动脉斑块检出率差异无统计学意义(P>0.05);复发脑梗死患者颈总动脉、颈动脉分叉处血管内中膜厚度值(CCA-IMT、ICA-IMT、BIF-IMT)明显高于未复发患者(P<0.01)。结论颈动脉内中膜厚度增厚患者脑梗死复发率增高。     

颈动脉超声检查在脑梗死患者中的应用

目的：探讨颈动脉超声检查在脑梗死患者中的应用价值。方法对144例脑梗死患者和106名健康查体者进行颈动脉超声检查,观察颈动脉内中膜厚度、斑块发生情况及血管狭窄情况。结果脑梗死组较对照组内中膜明显增厚,斑块检出率明显增高。脑梗死组与对照组检出斑块中均以强回声斑块最为多见。脑梗死组与对照组在血管狭窄程度上差异有统计学意义（P＜0.01）。结论动脉粥样硬化是脑梗死发生的主要危险因素之一。颈动脉超声检查可以观察和了解颈动脉粥样硬化的病变及其程度,提示脑血管病变是否处于高危状态,对脑梗死患者的预防和治疗有重要的实用价值。     

46例脑梗死患者颈动脉超声检测分析

目的探讨脑梗死患者颈动脉粥样硬化的超声及临床意义。方法对46例脑梗死患者行颈动脉超声检查,并与46例中老年非脑梗死组作对照。结果脑梗死组颈动脉内中膜厚度和斑块数高于对照组（P〈0.01）,狭窄程度两组差异无统计学意义（P〉0.05）;脑梗死组颈动脉超声阳性率明显高于对照组（P〈0.01）。结论脑梗死患者均有不同程度颈动脉粥样硬化,对高危人群行颈动脉超声检查,有助于脑梗死的早期防治。     

Evaluation of new apolipoprotein C-II and apolipoprotein C-III automatized immunoturbidimetric kits

BACKGROUND: Apolipoprotein C-II and apolipoprotein C-III play an important and complex role in plasma triglycerides metabolism, respectively, as inhibitor and activator of lipoprotein lipase. Thus, they appear to be suitable markers for clinical studies of triglyceride-rich lipoproteins and related cardiovascular risk. Our aim was to evaluate, for routine analysis, the accuracy to quantify these apolipoprotein in human sera. METHODS: Precision (intra- and inter-run), limit of detection and quantification, linearity, common interferents (lipids, haemoglobin, bilirubin) and reference intervals were determined according to guidelines of the French Society of Clinical Biology and ISO Norm 5725 specifications. RESULTS: Intra- and inter-run CVs were respectively less than 5.0% and 7.5%. Linearities extended from 10.8 mg/L to 112.9 mg/L for apolipoprotein C-II and from 31.8 mg/L to 375.5 mg/L for apolipoprotein C-III. Haemolysis (up to 227.6 micromol/L haemoglobin) and lipemia (up to 19.3 mmol/L triglycerides) do not interfere, contrary to bilirubin, which has a positive effect above 350 micromol/L. Comparison of methods shows good agreement between immunoturbidimetric and electro-immunodiffusion methods for measuring apolipoprotein C-III in 62 samples within a wide range (n = 62, r = 0.954, y = 3.81 x -14.4). CONCLUSION: This study shows the reliability of these kits for measuring apolipoprotein C-II and apolipoprotein C-III in human sera, and their suitability for routine analysis.     

Phenotypes of apolipoprotein B and apolipoprotein E after liver transplantation.

Apolipoprotein (apo) E and the two B apolipoproteins, apoB48 and apoB100, are important proteins in human lipoprotein metabolism. Commonly occurring polymorphisms in the genes for apoE and apoB result in amino acid substitutions that produce readily detectable phenotypic differences in these proteins. We studied changes in apoE and apoB phenotypes before and after liver transplantation to gain new insights into apolipoprotein physiology. In all 29 patients that we studied, the postoperative serum apoE phenotype of the recipient, as assessed by isoelectric focusing, converted virtually completely to that of the donor, providing evidence that greater than 90% of the apoE in the plasma is synthesized by the liver. In contrast, the cerebrospinal fluid apoE phenotype did not change to the donor's phenotype after liver transplantation, indicating that most of the apoE in CSF cannot be derived from the plasma pool and therefore must be synthesized locally. The apoB100 phenotype (assessed with immunoassays using monoclonal antibody MB19, an antibody that detects a two-allele polymorphism in apoB) invariably converted to the phenotype of the donor. In four normolipidemic patients, we determined the MB19 phenotype of both the apoB100 and apoB48 in the "chylomicron fraction" isolated from plasma 3 h after a fat-rich meal. Interestingly, the apoB100 in the chylomicron fraction invariably had the phenotype of the donor, indicating that the vast majority of the large, triglyceride-rich apoB100-containing lipoproteins that appear in the plasma after a fat-rich meal are actually VLDL of hepatic origin. The MB19 phenotype of the apoB48 in the plasma chylomicron fraction did not change after liver transplantation, indicating that almost all of the apoB48 in plasma chylomicrons is derived from the intestine. These results were consistent with our immunocytochemical studies on intestinal biopsy specimens of organ donors; using apoB-specific monoclonal antibodies, we found evidence for apoB48, but not apoB100, in donor intestinal biopsy specimens.     

Low diurnal variability of apolipoprotein A1, apolipoprotein B and apolipoprotein B/apolipoprotein A1 ratio during normal sleep and after an acute shift of sleep

ObjectiveThe aim of this study was to study the diurnal variation of the cardiovascular risk markers apolipoprotein A1 and B and apo B/apo A1 ratio.Design and methodsWe have studied the diurnal variation of apolipoprotein A1, apolipoprotein B and apo B/apo A1 ratio during night sleep and the day sleep conditions in seven healthy volunteers (age 22–32 yr). Samples were collected every hour to evaluate the effect of different sampling times on the test results.ResultsThe lowest diurnal coefficient of variation (CV) was observed for the apo B/apo A1 ratio, which usually was below 2% but also apolipoprotein A1, apolipoprotein B showed low CV. There were no significant differences between nightsleep and daysleep for any of the studied markers.ConclusionEven if there was a diurnal variation for these markers, the variation was very low. Thus, sampling does not have to be restricted to certain times of the day.     

Structural relationship of human apolipoprotein B48 to apolipoprotein B100.

Although the complete amino acid sequence of human apolipoprotein (apo) B100 is known (4536 amino acids), the structure of apo B48 has not been defined. The objective of our study was to define the structure of apo B48 and its relationship to apo B100. Antibodies were produced against 22 synthetic peptides corresponding to sequences in human apo B100. The levels of immunoreactivity of the antipeptides to apo B100 and apo B48 were used to define the structural relationship between these two species of apo B. Six antibodies from sequences in the amino-terminal half of apo B100, including antipeptide 2110-2129, bound to both apo B100 and apo B48. 15 other apo B-specific antipeptides from sequences carboxyl-terminal to residue 2152 bound to apo B100, but not to apo B48. Immunoblots of cyanogen bromide digests of apo B100 and apo B48 with antipeptides 2068-2091 and 2110-2129 detected a 16-KD fragment (residues 2016-2151) in the apo B100 digest and a fragment of identical size in the apo B48 digest. Because apo B48 appears to contain the apo B100 cyanogen bromide fragment 2016-2151 and because an antiserum specific for the peptide 2152-2168 does not bind to apo B48, we conclude that apo B48 represents the amino-terminal 47% of apo B100 and that the carboxyl terminus of apo B48 is in the vicinity of residue 2151 of apo B100.     

Estimation of LDL-associated apolipoprotein B from measurements of triglycerides and total apolipoprotein B

BACKGROUND: VLDL and chylomicrons may interfere with measurements of apolipoprotein B (apo B) on LDL particles. Ultracentrifugation of samples enriched in chylomicrons and VLDL and subsequent measurement of apo B in the infranate fraction [density (d) = 1.006] removes this interference. This apo B fraction is called "LDL-apo B." METHODS: We retrospectively analyzed 64 895 measurements of triglycerides, total apo B, and LDL-apo B. Samples were ultracentrifuged, and 3 commercially available immunoassays that use different antibodies were used to measure LDL-apo B in the 1.006 infranate fraction. RESULTS: After adjusting for triglyceride concentration, we found total apo B and LDL-apo B measurements to be strongly correlated. We derived a simple linear equation for calculating LDL-apo B concentration (in milligrams per deciliter) from measurements of total apo B and triglycerides: LDL-apo B = apo B - 10 mg/dL - triglycerides/32. This equation accurately predicts LDL-apo B values within +/- 12% of the measured value in 75% of cases. CONCLUSIONS: Our equation provides a convenient means of estimating LDL-apo B from commonly available measurements of total apo B and triglycerides without the need for ultracentrifugation. LDL-apo B measurements were also independent of the different apo B antibodies in the 3 assays used in this study. An equation that predicts LDL-apo B particle number may be useful, regardless of the apo B assay used.     

Turbidimetric assay of apolipoprotein A-II

A turbidimetric assay for the quantification of apolipoprotein A-II in serum is described. Its adaptation for the Cobas Bio Analyser (Hoffmann La Roche) is reported. Regression analysis of apolipoprotein A-II values measured by turbidimetry revealed a good measure of agreement with the data obtained by radial immunodiffusion (RID) (r = 0.90, y = 0.97x + 0.021, n = 100) as well as with data obtained by immunonephelometry (r = 0.838, y = 0.925x + 0.029, n = 34). A variation coefficient of 3.2% (n = 18) was found in relation to the precision in the series and a variation coefficient of 3.5% (n = 36) in relation to day to day precision.     

Macrophage-specific expression of human apolipoprotein E reduces atherosclerosis in hypercholesterolemic apolipoprotein E-null mice.

apoE deficiency causes hyperlipidemia and premature atherosclerosis. To determine if macrophage-specific expression of apoE would decrease the extent of atherosclerosis, we expressed human apoE in macrophages of apoE-null mice (apoE-/-) and assessed the effect on lipid accumulation in cells of the arterial wall. Macrophage-specific expression of human apoE in normal mice was obtained by use of the visna virus LTR. These animals were bred with apoE-/- mice to produce animals hemizygous for expression of human apoE in macrophages in the absence of murine apoE (apoE-/-,hTgE+/0). Low levels of human apoE mRNA were present in liver and spleen and high levels in lung and peritoneal macrophages. Human apoE was secreted by peritoneal macrophages and was detected in Kupffer cells of the liver. Human apoE in the plasma of apoE-/-,hTgE+/0 mice (n = 30) was inversely correlated (P < 0.005) with the plasma cholesterol concentration. After 15 wk on a normal chow diet, atherosclerosis was assessed in apoE-/-,hTgE+/0 animals and in apoE-/-,hTgE0/0 littermates matched for plasma cholesterol level (approximately 450 mg/dl) and lipoprotein profile. There was significantly less atherosclerosis in both the aortic sinus and in the proximal aorta (P < 0.0001) in the animals expressing the human apoE transgene. In apo-E-/-,hTgE+/0 animals, which had detectable atherosclerotic lesions, human apoE was detected in the secretory apparatus of macrophage-derived foam cells in the arterial wall. The data demonstrate that expression of apoE by macrophages is antiatherogenic even in the presence of high levels of atherogenic lipoproteins. The data suggest that apoE prevents atherosclerosis by promoting cholesterol efflux from cells of the arterial wall.     

Familial apolipoprotein A-I variants

Apolipoprotein (apo) A-I is the major apolipoprotein of HDL and is a single polypeptide chain with 243 amino acid residues. Familial apo A-I deficiency is a rare metabolic disorder of which 13 cases have been characterized at the molecular level. However, in subjects with apo A-I deficiency, coronary artery disease is not always present. To date, more than 40 genetically determined structural variants of apo A-I have been identified. Seven apo A-I mutations have been identified to cause hereditary amyloidosis. In our laboratory, we characterized ten apo A-I variants, including apo A-I(Vall56Glu) Oita. A minority of structural variants were associated with altered HDL cholesterol levels or increased risk for cardiovascular disease.     

In vivo metabolism of apolipoprotein S in humans. Comparison with apolipoprotein A-I metabolism

¹²⁵I-labelled apolipoprotein (Apo) S and ¹³¹I-labelled apolipoprotein A-I were injected i.v. into healthy volunteers. Blood samples and daily urine collections were drawn periodically for 15 days. Ninety-eight percent of ¹³¹I radioactivity and > 95% of ¹²⁵I radioactivity were found in HDL after Superose gel chromatography of plasma. About 10% of each radioactivity was recovered in the d 1.250 infranate after one ultracentrifugation. Affinity chromatography on monoclonal anti-Apo A-I Sepharose column separates two lipoprotein particles containing Apo S, one retained with Apo A-I (42.5%) and the other eluting without Apo A-I (57.5%).

Kinetic parameters were calculated according to exponential curve fitting. Mean transit time was about 7.0 days for both Apo A-I and Apo S. FCR of Apo S was 50% higher than FCR of Apo A-I. Synthetic rate of Apo S was about 150 times smaller than for Apo A-I.

As heterogeneity of HDL-S was suggested by both the results of affinity chromatography and the urinary data, a compartmental model was built which fitted adequately all data. Part of the model is common to HDL-A-I and HDL-S.