高龄髋部骨折的治疗

目的研究高龄髋部骨折手术治疗的特点。方法回顾52例高龄(80岁以上)髋部骨折的手术选择及术前、术后的注意事项。结果除3例患者疗效欠佳外,其余取得较好效果。结论高龄髋部骨折患者,应慎重、认真对待,手术治疗可取得较好的结果,提高生活质量。     

The monoclonal antibody Alz-50, used to reveal cytoskeletal changes in Alzheimer's disease, also reacts with a large subpopulation of somatostatin neurons in the normal human hypothalamus and adjoining areas

The monoclonal antibody Alz-50 is directed against Alzheimer's disease-related modified tau proteins and reveals cytoskeletal changes, i.e. neurofibrillary tangles and dystrophic neurites. The present study shows that, in the hypothalamus of non-demented control subjects, this same antibody gives a distinctive staining pattern of a subpopulation of somatostatin neurons and beaded fibers. Furthermore, Alz-50 occasionally recognizes somatostatin-containing cell bodies and dystrophic neurite-like fibers in the (neuritic) senile plaques of AD patients. These observations have direct consequences for the interpretation of Alz-50 staining in diagnostic usage and for the assessment of Alzheimer's disease-like changes induced by β-amyloid in experimental animal brains. On dot spotting, Alz-50 was found to bind to a number of fragments from the somatostatin precursor, of which somatostatin_15–28 stained best. Preadsorption of Alz-50 by somatostatin_15–28, as well as other specificity tests, failed, however, to provide any clue to the nature of the unknown compound(s) stained in the control hypothalamus.     

老年性白内障手术心电监护

目的：评价老年性白内障超声乳化伴人工晶体植入术心电监护的临床意义。方法：随机选择老年性白内障超声乳化伴人工晶体植入术行心电监护244例（287只眼）。结果：手术中出现血压明显升高，心肌缺血及心律失常者114例，经及时处理后恢复。结论：老年性白内障患者，术中行心电监护对提高手术安全性十分重要。     

误诊为脑梗塞的老年人脑肿瘤

目的 探讨将中老年人脑肿瘤误诊为脑血管病的原因及二者之间的一些内在联系。方法 回顾性分析18例老年中脑肿瘤患者的临床表现,诊断与治疗结果。结果 18例患者神经手术、化疗、放疗及对症处理,全组无严重并发症,好转出院。结论老年中脑肿瘤病史、症状及体征不典型。常呈卒中样发病,临床上极易误疹,应高度重视。     

Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease

Antibodies to the lysosomal hydrolases, cathepsins B and D and β-hexosaminidase A, revealed alterations of the endosomal-lysosomal system in neurons of the Alzheimer disease brain, which preceded evident degenerative changes and became marked as atrophy, neurofibrillary pathology, or chromatolysis developed. At the earliest stages of cell atrophy, hydrolase-positive lysosomas accumulated at the basal pole and then massively throughout the perikarya and proximal dendrites of affected pyramidal neurons in Alzheimer prefrontal cortex and hippocampus, far exceeding the changes of normal aging. Secondary lysosomes as well as tertiary residual bodies (lysosomes/lipofuscin) increased implying stimulated, autophagocytosis and lysosomal system activation. Less affected brain regions, such as the thalamus, displayed similar though less extensive alterations. Certain thalamic neurons exhibited a distinctive lysosome-related abnormality characterized by the presence of cell surface blebs of varying size and number filled with intense hydrolase immunoreactivity. At more advanced stages of degeneration in still intact neurons, hydrolase-positive lipofuscin, particularly in the form of abnormal large aggregates, nearly filled the cytoplasm. Similar lipofuscin aggregates were oberved in abundance in the extracellular space following cell lysis and were usually associated with deposits of the β-amyloid protein. Degenerating neurons and their processes were the major source of these aggregates within senile plaques which contained high concentrations of acid hydrolases. We have shown in previous studies that these lysosomal hydrolases in plaques are enzymatically-active. The persistence of lysosomal structures in the brain parenchyma after neurons hyve degenerated is a striking and potentially diagnostic feature of Alzheimer disease which has not been observed, to our knowledge, in other degenerative diseases. The lysosomal response in degerating Alzheimer neurons represents a probable link between an early activation of the lysosomal system in at-risk, normal-appearing neurons and the end-stage contribution of lysosomes to senile plaque formation of emphasizes a slowly progressive disturbance of the lysosomal system throughout the development of Alzheimer disease.     

老年患者尿路感染菌群分布及其耐药性分析

目的 :了解老年患者尿路感染致病菌的菌群分布及其对抗生素的耐药情况 ,为临床合理使用抗生素提供依据。方法 :收集湖北省 15所三级甲等医院 2 0 0 2年尿路感染老年患者清洁中段尿细菌培养分离的 5 34株致病菌 ,对其进行耐药性监测。药敏采用K B法 ,用WHONET 5软件进行数据分析。结果 :共收集致病菌 5 34株 ,其中革兰阴性菌 4 0 9株 (76 .6 % ) ,革兰阳性菌 12 5株(2 3.4 % )。革兰阴性菌中大肠埃希菌检出率最高 (2 6 4株 ,4 9.4 % ) ,其次为克雷白杆菌 (44株 ,8.2 % )。 16 .7%的大肠埃希菌和 2 2 .7%的克雷白杆菌产超广谱 β 内酰胺酶。亚胺培南、阿米卡星、头孢他啶对革兰阴性菌的抗菌活性最强 ,而革兰阴性菌对环丙沙星、庆大霉素、哌拉西林的耐药率均在 5 0 %以上。革兰阳性菌以肠球菌最多见 (6 4株 ,12 % ) ,其次为葡萄球菌属 (43株 ,8.1% )。革兰阳性菌对SMZco、红霉素等的耐药率均在 4 0 %以上 ,但对万古霉素均敏感。结论 :老年患者尿路感染以革兰阴性菌为优势菌株 ,且耐药性日益严重 ,对亚胺培南、阿米卡星、头孢他啶最为敏感。革兰阳性菌宜以万古霉素为首选。     

Immunohistochemical localization of tissue factor pathway inhibitor-1 (TFPI-1), a Kunitz proteinase inhibitor, in Alzheimer''s disease

Senile plaques in Alzheimer's disease (AD) are composed principally of Aβ, a 4 kDa fragment of the amyloid precursor protein (APP). Longer forms of APP which contain a Kunitz proteinase inhibitor (KPI) domain are elevated in aged and in AD brains. Tissue factor pathway inhibitor-1 (TFPI) contains three tandem KPI domains and has been well characterized for its role as a natural anticoagulant in the extrinsic coagulation pathway. Functionally, the first two KPI domains of TFPI bind and inhibit the activity of factor Xa and VIIa respectively. In addition, TFPI and APP-KPI share a common clearance mechanism through the low density lipoprotein receptor-related protein (LRP). As part of an ongoing study of the role of KPI-containing proteins in AD, the current study examines TFPI localization in the brain. We report here that TFPI is immunohistochemically localized to microglia in both AD and non-AD individuals and is localized to some senile plaques in AD. Western blot analyses indicate that the amount of TFPI is elevated in frontal cortex samples from AD brains. We propose that TFPI may play a cell specific role in proteinase regulation in the brain.     

Comparison of silver stainings and immunohistology for the detection of neurofibrillary tangles and extracellular cerebral amyloid in paraffin sections

Summary The sensitivities of six silver-staining methods and immunohistology for beta and tau protein were compared for their ability to demonstrate neurofibrillary tangles (NFT) and senile plaques (SP) in paraffin sections. Serial sections of the hippocampal area of 35 brains showing these neuropathological findings were cut and stained by the methods of Cross, Campbell, Bielschowsky, Gallyas, Yamaguchi, our variant (method of Reusche) and immunohistology. In the detection of NFT, the techniques of Gallyas, Bielschowsky, our method and tau protein immunostaining were the most sensitive methods. The procedure of Campbell and again our method were proven to be superior to the other stainings in demonstrating SP as well as diffuse and subpial amyloid. Moreover, our method reliably stained vascular and perivascular amyloid which can be identified in brains with congophilic angiopathy. Due to a lack of control in certain steps of the procedures most of the silver-staining methods are complicated and to not present reliable results. Our variant is easy to perform and, thus, may be used as a sensitive, simple and reliable alternative for the impregnation of the main lesions (NFT and SP) occurring in senile dementia of Alzheimer type and brains with normal aging for screening, retrospective and quantitative studies and for routine purposes.Parts of this paper were presented at the IV. European Meeting of Neuropathology, Berlin Germany, 1992     

Diffuse type of senile plaques in the cerebellum of Alzheimer-type dementia demonstrated byβ protein immunostain

Summary We studied senile plaques (SP) in the cerebella of six autopsied subjects with Alzheimer-type dementia (ATD) and ten non-ATD autopsied subjects between the ages of 78 and 90. Neither SP nor amyloid angiopathy (AA) was observed in any of the non-ATD subjects. In the four of the six ATD subjects, diffuse plaques in the molecular layer were seen as ill-defined areas of fine fibrillar materials by protein immunostaining with formic acid pretreatment, the modified Bielschowsky stain, and periodic acid-methenamine silver (PAM) stain. The plaques were not visible with Bodian, Congo red, or periodic acid-Schiff stains. Compact plaques in the Purkinje cell or in the granular cell layers were found in three of the six subjects. Their amyloid core was often surrounded by areolar amyloid deposits. AA was observed in three of the six subjects. The argyrophilia of the diffuse and compact plaques, demonstrated by the modified Bielschowsky and PAM stains, became undetectable when the sections were first treated with formic acid. Such treatment made the plaques immunoreactive with protein antiserum. The findings suggested that cerebellar diffuse plaques and compact plaques consist mainly of an amyloid component, and are characteristic of ATD.     

Demonstration of microglial cells in and around senile (neuritic) plaques in the Alzheimer brain

Summary A monoclonal antibody, termed AD11/8, reactive to microglial cells, was produced by immunization of mice with partially purified amyloid fibrils of senile (neuritic) plaques. With immunoperoxidase staining on human tissues, AD11/8 also recognized macrophages in the red pulp of the spleen, Kupffer cells in the liver, and macrophages in the bone marrow. The results show that AD11/8 recognizes the antigens associated with mononuclear phagocytes lineage. In normal brains a few resting microglial cells were stained in gray matter, and less frequently in white matter. In senile dementia of the Alzheimer type numerous microglial cells were stained intensively and they often formed clusters in gray matter. By double immunostaining with AD11/8 and a polyclonal antibody against synthetic amyloid -protein, clustered microglial cells were observed in and around senile plaques with amyloid deposits. Some amyloid plaque cores were surrounded by microglial cell processes. These results indicate that microglial cells may play an important role in senile plaque formation.Supported in part by the Grant-in Aid for Scientific Research from the Ministry of Education, Science and Culture, the grants for Research of Dementia and for Primary Amyloidosis from the Ministry of Health and Welfare, Japan