西藏现代藏族人颅的颅型及其特点

测量７０个西藏现代藏族人颅４０项指标；计算指数１６项；根据指数确定颅型，额型，颌型，眶型，鼻型与腭型；进行数理统计；观察性别差异，发现男发性间各测量值差显著，     

西藏拉萨、林芝地区四县人体寄生虫分布调查

按全国人体寄生虫分布调查实施细则的要求和方法对西藏自治区4县8个调查点2746人进行调查,共查见寄生虫21种。其中原虫9种、蠕虫 12种,未查见吸虫。粪检结果有结肠内阿米巴、布氏嗜碘阿米巴、微小内蜒阿米巴、哈氏内阿米巴、人毛滴虫、贾第虫、肉孢子虫、结肠小袋纤毛虫和人酵母菌,其感染率依次为23.4％、7.8％、4.4％、0.6％、0.08％、7.3％、7.1％、0.04％和0.6％。蠕虫有蛔虫、鞭虫、钩虫、蛲虫、带绦虫、微小膜壳绦虫、长膜壳绦虫和东方毛圆线虫,其感染率依次为18％、7.8％、1％、0.2％、20.4％、0.04％、0.04％和0.04％。透明胶纸肛拭法检查78人,其中烧虫感染率为13.5％;血清学检查463例,测得旋毛虫、包虫和囊虫阳性率分别为21％、16％和13％。结果表明,地理环境和人所处的经济、卫生条件,文化水平以及年龄是影响寄生虫分布和感染率的重要因素。     

1176例血培养检出真菌及细菌的耐药性分析

目的：调查2010～2013年医院常见真菌、细菌的耐药性,为临床用药提供依据。方法用 BacT／Alert 3D 全自动血培养仪进行培养,用 VITEK 鉴定系统进行细菌鉴定和药敏试验,用 WHONET5．4统计结果。结果1176例送检标本中阳性标本108例,阳性率为9．18％。分离病原菌123株,革兰阳性菌60株（48．78％）,革兰阴性菌为47株（38．21％）,真菌为16株（13．01％）。前5位病原菌依次为凝固酶阴性葡萄球菌（44株）、大肠埃希菌（18株）、肺炎克雷伯菌（15株）、白色念珠菌（10株）、金黄色葡萄球菌（7株）。耐甲氧西林凝固酶阴性葡萄球菌（MRCNS）、金黄色葡萄球菌（MRSA）检出率分别为72．73％（32／44）、57．14％（4／7）,MRSA 和 MRCNS 较 MSSA 和 MSCNS 对抗菌药物耐药率高,未发现对万古霉素及利奈唑胺耐药的葡萄球菌。酮康唑、氟康唑、咪康唑对白色念珠菌敏感率高。大肠埃希菌和肺炎克雷伯菌产超广谱β-内酰胺酶（ESBLs）率分别为50．00％、40．00％,亚胺培南和美罗培南敏感率为100．00％。头孢哌酮／舒巴坦、哌拉西林／三唑巴坦对肠杆菌科细菌、铜绿假单胞菌敏感率较高。结论血培养以凝固酶阴性葡萄球菌为主,分离菌的耐药性较强,应加强血培养,指导临床合理用药。     

AT_1R基因3′-非翻译区A1166→C变异和CA重复序列多态性与藏族EH的关联分析

目的　研究血管紧张素 的 型 (AT1 R)基因 3′-端 CA重复序列多态性和 A116 6→ C突变双等位标志是否与藏族原发性高血压 (essential hypertension,EH)的遗传易感性相关联。方法　以荧光标记 d CTP为底物 ,应用 PCR扩增和 ABI prism 377半自动测序及 PCR/ RFL P技术 ,通过病例 -对照研究、受累同胞对和家系连锁分析 ,鉴定 AT1 R基因 3′-端 CA重复序列多态性和 A116 6→ C点突变与藏族 EH的关联。结果　病例 -对照研究证明 ,AT1 R基因 3′-端 CA重复序列多态性与 EH相关联 ,χ2 =2 6 .44 ,P<0 .0 0 1,该位点杂合度为 0 .73,多态信息量为 0 .71。 AT1 R基因 3′-端 CA重复序列存在 11种等位基因 ,A7(138bp)为最常见等位基因 ,A8等位基因与 EH正相关 ,EH组和对照组中 A8等位基因频率分别为2 0 .5 %和 7.3% ,χ2 =9.6 4,P=0 .0 0 2 ,OR=3.46 ,95 % CI=1.44～ 8.5 1;受累同胞对 A8等位基因的共享连锁分析结果显示 ,χ2 =3.85 ,P=0 .0 2 5 ;家系连锁分析 L od score值为 0 .80 ,AT1 R基因 A116 6→C突变与EH无关 (P>0 .0 5 )。结论　 AT1 R基因 3′端 CA重复序列多态性与 EH相关 ,A8等位基因是藏族 EH的重要遗传标志 ,提示致病基因可能与其存在连锁不平衡     

迷信罪犯30例个性心理量表检测分析

迷信犯罪是利用迷信手段实施危害社会的行为。本文采用艾森克个性问卷、民俗信仰问卷、简易精神症状评定量表,对这类犯罪的30例(称研究组)及对照组进行检测。发现研究组有如下心理特征:个性内向(E分低)与对照组比较有显著性差异,而情绪稳定性(N)、精神病质(P)及掩饰(L)等均与对照组无显著性差异;研究组较对照组更信鬼神;而躯体化症状前者较后者多得多,但前者与癔病并无关系。     

西藏自治区精神障碍流行病学调查I:重型精神障碍

目的调查西藏精神障碍患病率,为政府制订西藏卫生工作规划提供科学依据。方法参考两次全国精神障碍流行病学调查的方法,使用美国精神障碍诊断与统计手册轴I障碍用临床定式检查执行手册/研究版(SCID-I)作为定式检查工具,并以美国精神障碍诊断与统计手册-第四版(DSM-IV)为诊断标准,对西藏具有代表性的4个地市进行精神障碍流行病学抽样调查。结果在西藏≥15岁人口中实际调查5375人,心境障碍、精神分裂症、器质性精神障碍和急性短暂精神病性障碍的时点患病率分别为0.48%,0.34%,0.17%和0.037%;终生患病率分别为0.56%,0.37%,0.17%和0.037%。结论西藏4类重型精神障碍总的终生患病率为1.14%,如何妥善解决全自治区1%人口中重型精神障碍患者的诊治问题,在政府制订卫生工作规划时有必要特别加以关注。     

拉萨市藏、汉民族血脂水平的比较

 目的 调查分析拉萨市藏、汉民族间血脂水平及其异常检出率的差异,为该地区血脂异常症的预防提供客观依据。方法 选取拉萨市藏（Tibetan,T）、汉民族（Han,H）1 228例体检人群为调查对象,其中藏族559例,汉族669例,按血脂测定标准化方法测定的血清总胆固醇（total cholesterol,TC）、三酰甘油（triglycerin,TG）、高密度脂蛋白胆固醇（high-density lipoprotein cholesterol,HDL-C）及低密度脂蛋白胆固醇（low-density lipoprotein cholesterol,LDL-C） 4项指标的血脂水平;按2007年《中国成人血脂异常防治指南》将研究对象分为4个年龄组,界定4项血脂异常标准值,比较藏、汉民族各年龄组血脂异常检出率的差异。采用协方差分析和χ2检验比较两民族间血脂存在的差异。结果 汉族TG水平高于藏族（P≤0.001）,HDL-C水平低于藏族（P<0.001）;藏族TC和LDL-C水平均高于汉族 （P<0.001、P=0.013）。藏族男性青年组、中年组、老年前期组TC异常检出率均显著高于汉族（P<0.001）,藏族男性中年组和女性青年组、中年组TG异常检出率反而比汉族高（P<0.001、P<0.05、P<0.001）;汉族男性青年组、中年组、老年前期组HDL-C异常检出率明显高于藏族（P<0.001）。结论 藏族是混合型高脂血症的高危人群,尤其藏族男性;汉族男性是低HDL-C血症的高危人群。     

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目的    了解高海拔地区藏族牧民口腔健康情况,探讨口腔疾病发病情况和规律,为采取防治措施和改善口腔医疗服务提供依据。方法    2008年10月选择西藏羊易村成年人为调查对象,共439人接受调查,其中男206人,女233人。按照年龄分为：18～24岁组（120人）、>24～34岁组（108人）、>34～44岁组（96人）、>44岁组（115人）;每个年龄组内按性别再分组。以世界卫生组织1997年口腔健康调查基本方法为标准,调查成年牧民龋齿、牙周疾病、第三磨牙萌出及口腔其他疾病患病情况,并对结果进行分析。结果    羊易村成人龋患率、龋均、平均缺牙数分别为74.94%、5.74、3.57。18～24岁和>24～34岁组女性龋均显著高于男性,且差异有统计学意义（P < 0.05）。各年龄组内男女间人均缺牙数、龋患率、有28颗牙人数、牙结石检出率、牙周炎发生率差异无统计学意义（P > 0.05）;而从总体统计,女性缺牙数、龋患率、牙周炎发生率高于男性（P < 0.05）,有28颗牙人数低于男性（P < 0.05）,男性>24～34岁组牙龈炎发生率显著高于同龄女性（P < 0.05）。>24～34岁组中女性第三磨牙萌出率高于男性（P < 0.05）,而在>44岁组中男性高于女性（P < 0.05）。在>24～34岁组、>44岁组和全体样本总计中女性萌出的第三磨牙龋齿发生率均高于男性（P < 0.05）。439名被调查者中有22人有不良固定义齿修复;38人有上颌侧切牙装饰性义齿修复。龋齿充填率为0。结论    高海拔地区缺氧环境和饮食习惯对口腔发育和疾病有一定影响。西藏牧民口腔健康状况较差,需要改善牧区口腔医疗条件,建立口腔防治体系。     

286例高原猝死尸检的临床病理分析

目的 :探讨高原猝死的病因、病理和临床特点与平原有何不同 ,以提高其诊断和治疗水平 ;方法 :对本院 1 959年 1 1月— 2 0 0 3年 1 0月 1 1 4 0例尸检进行回顾性分析研究 ;结果 :检出猝死 2 86例 ,其中呼吸系统疾病 1 73例 (60 .5% ) ,明显高于平原资料 (P <0 .0 1 ) ,心血管疾病 68例 (2 3 .8% ) ,中枢神经系统疾病 1 5例 (5.2 % ) ,均明显低于平原 (P <0 .0 1 ) ,消化系统疾病 2 2例 (7.7% ) ,泌尿生殖系统和其它疾病各 4例 (分别占 1 .4% ) ,肺炎合并肺水肿、肺出血者占 46.2 0 % ;结论 :青海高原猝死的死因呼吸系统疾病占首位 ,明显高于平原 ,心血管系统和中枢神经系统疾病相对明显低于平原 ,肺炎易并发肺水肿和肺出血     

Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28

Calcium (Ca²⁺)-dependent protein kinases (CDPKs or CPKs) are a unique family of Ca²⁺ sensor/kinase-effector proteins with diverse functions in plants. In Arabidopsis thaliana, CPK28 contributes to immune homeostasis by promoting degradation of the key immune signaling receptor-like cytoplasmic kinase BOTRYTIS-INDUCED KINASE 1 (BIK1) and additionally functions in vegetative-to-reproductive stage transition. How CPK28 controls these seemingly disparate pathways is unknown. Here, we identify a single phosphorylation site in the kinase domain of CPK28 (Ser318) that is differentially required for its function in immune homeostasis and stem elongation. We show that CPK28 undergoes intermolecular autophosphorylation on Ser318 and can additionally be transphosphorylated on this residue by BIK1. Analysis of several other phosphorylation sites demonstrates that Ser318 phosphorylation is uniquely required to prime CPK28 for Ca²⁺ activation at physiological concentrations of Ca²⁺, possibly through stabilization of the Ca²⁺-bound active state as indicated by intrinsic fluorescence experiments. Together, our data indicate that phosphorylation of Ser318 is required for the activation of CPK28 at low intracellular [Ca²⁺] to prevent initiation of an immune response in the absence of infection. By comparison, phosphorylation of Ser318 is not required for stem elongation, indicating pathway-specific requirements for phosphorylation-based Ca²⁺-sensitivity priming. We additionally provide evidence for a conserved function for Ser318 phosphorylation in related group IV CDPKs, which holds promise for biotechnological applications by generating CDPK alleles that enhance resistance to microbial pathogens without consequences to yield.

Protein kinases represent one of the largest eukaryotic protein superfamilies. While roughly 500 protein kinases have been identified in humans (1), the genomes of Arabidopsis thaliana (hereafter, Arabidopsis) (2) and Oryza sativa (3) encode more than 1,000 and 1,500 protein kinases, respectively, including several families unique to plants. Among these protein kinases are the receptor-like kinases (RLKs), receptor-like cytoplasmic kinases (RLCKs), and calcium-dependent protein kinases (CDPKs or CPKs) that have emerged as key regulators of plant immunity (4–6). Despite encompassing only 2% of most eukaryotic genomes, protein kinases phosphorylate more than 40% of cellular proteins (7, 8), reflecting their diverse roles in coordinating intracellular signaling events. Reversible phosphorylation of serine (Ser), threonine (Thr), and tyrosine (Tyr) residues can serve an array of functions including changes in protein conformation and activation state (9, 10), protein stability and degradation (11, 12), subcellular localization (13–15), and interaction with protein substrates (16–18).Calcium (Ca²⁺) is a ubiquitous secondary messenger that acts cooperatively with protein phosphorylation to propagate intracellular signals. Spatial and temporal changes in intracellular Ca²⁺ levels occur in response to environmental and developmental cues (19–23). In plants, Ca²⁺ transients are decoded by four major groups of calcium sensor proteins, which possess one or more Ca²⁺-binding EF-hand motifs (24, 25): calmodulins (CaM), CaM-like proteins, calcineurin B–like proteins, CDPKs, and Ca²⁺/CaM-dependent protein kinases.At the intersection of phosphorylation cascades and Ca²⁺ signaling are CDPKs, a unique family of Ca²⁺ sensor/kinase-effector proteins. CDPKs have been identified in all land plants and green algae, as well as certain protozoan ciliates and apicomplexan parasites (26, 27). CDPKs have a conserved domain architecture, consisting of a canonical Ser/Thr protein kinase domain and an EF-hand containing Ca²⁺-binding CaM-like domain (CLD), linked together by an autoinhibitory junction (AIJ) and flanked by variable regions on both the amino (N) and carboxyl (C) termini (28, 29). As their name implies, most CDPKs require Ca²⁺ for their activation (30). Upon Ca²⁺ binding to all EF-hands in the CaM-like domain, a dramatic conformational change occurs, freeing the AIJ from the catalytic site of the kinase, rendering the enzyme active (31–33). CDPKs vary in their sensitivity to Ca²⁺ (30), presumably allowing proteins to perceive distinct stimuli through differences in Ca²⁺-binding affinity. For example, Arabidopsis CPK4 displays half maximal kinase activity in the presence of ∼3 μM free Ca²⁺ (30) while CPK5 only requires ∼100 nM (34). Importantly, CDPKs are signaling hubs with documented roles in multiple distinct pathways (4, 24, 35–38) and are therefore likely regulated beyond Ca²⁺ activation.Subfunctionalization is at least partially mediated by protein localization and interaction with pathway-specific binding partners, as is well documented for Arabidopsis CPK3 which functions in response to biotic and abiotic stimuli in distinct cellular compartments (39). Recent attention has been drawn to site-specific phosphorylation as a mechanism to regulate the activity of multifunctional kinases. For example, phosphorylation sites on the RLK BRASSINOSTEROID INSENSITIVE 1–ASSOCIATED KINASE 1 (BAK1) are differentially required for its function as a coreceptor with a subset of leucine-rich repeat –RLKs (40). Phosphoproteomic analyses indicate that CDPKs are differentially phosphorylated following exposure to distinct stimuli (41–48); however, the biochemical mechanisms by which site-specific phosphorylation regulates multifunctional CDPKs is still poorly understood.Arabidopsis CPK28 is a plasma membrane–localized protein kinase with dual roles in plant immune homeostasis (49–51) and phytohormone-mediated reproductive growth (52, 53). In vegetative plants, CPK28 serves as a negative regulator of immune signal amplitude by phosphorylating and activating two PLANT U-BOX–type E3 ubiquitin ligases, PUB25 and PUB26, which target the key immune RLCK BOTRYTIS-INDUCED KINASE 1 (BIK1) for proteasomal degradation (50). Owing to elevated levels of BIK1, CPK28 null plants (cpk28-1) have heightened immune responses and enhanced resistance to the bacterial pathogen Pseudomonas syringae pv. tomato DC3000 (Pto DC3000) (51). Upon transition to the reproductive stage, cpk28-1 plants additionally present shorter leaf petioles, enhanced anthocyanin production, and a reduction in stem elongation (52, 53). The molecular basis for developmental phenotypes in the cpk28-1 knockout mutant, beyond hormonal imbalance (52, 53), are comparatively unknown.Our recent work demonstrated that autophosphorylation status dictates Ca²⁺-sensitivity of CPK28 peptide kinase activity in vitro (54). While dephosphorylated CPK28 is stimulated by the addition of 100 μM CaCl₂ compared to untreated protein, hyperphosphorylated CPK28 displayed similar levels of activity at basal Ca²⁺ concentrations (54). These results highlight the interesting possibility that phosphorylation status may control the activation of multifunctional kinases in distinct pathways by allowing CDPKs to respond to stimulus-specific Ca²⁺ signatures.In the present study, we identify a single autophosphorylation site, Ser318, that decouples the activity of CPK28 in immune signaling from its role in reproductive growth. We show that expression of a nonphosphorylatable Ser-to-Ala variant (CPK28^S318A) is unable to complement the immune phenotypes of cpk28-1 mutants but is able to complement defects in stem growth. Further, we uncover a functional role for phosphorylation of Ser318 in priming CPK28 for activation at low free [Ca²⁺]. Together, we demonstrate that site-specific phosphorylation can direct the activity of a multifunctional kinase in distinct pathways and provide evidence for a conserved mechanism in orthologous group IV CDPKs.