绒山蝠生态的初步调查

绒山蝠(Nyctalus noctula velutinus)是芜湖市周围地区常见的食虫蝙蝠,国内仅见于南方。关于翼手类的生态资料,国内报道不多,绒山蝠的生态尚未见系统报告。从1980年起,我们连续3年对绒山蝠进行了定点观察和测定,现将初步调查报道如下。     

绒山蝠肝细胞电镜观察和乳酸脱氢酮同工酶的研究

本文用光镜和电镜观察了绒山蝠肝细胞的超微结构,用聚内烯酰胺凝胶电泳,对肝细胞ＬＤＨ同工酶进行了研究,肝细胞有丰富的线粒体,内质网,核糖体,发达的高尔基体,溶酶体等,在线粒体的周围有一层粗面内质网包绕,二者的密切关系,不仅在绒山蝠其他组织中,且在大部分哺乳动物细胞中均未观察到。该种肝细胞的ＬＤＨ同工酶以Ｍ型基为主,主要催化丙酮酸还原成乳酸。     

蝙蝠寄生吸虫中孔属一新种(复殖目:中孔科)

中国蝙蝠寄生吸虫的研究,国内仅见陈心陶(1954)曾有报告。我们于1987年2—3月,在杭州的绒菊头蝠(Rhinolopbus lanosus)与皮氏菊头蝠(Rhinolophus pearsonii)的小肠中采得一些标本,经鉴定为中孔科(Mesotritidae)中孔属(Mesotretes)的一新种东方中孔吸虫新种Mesotretes rientalisp.nov.(见图)。模式标本(正模1个,副模9个)保存在杭州师范学院生物系动物教研室,新种器官的量度均以mm为单位。寄主:绒菊头蝠Rhinolophus lanosus皮氏菊头蝠Rhinolophus pearsonii寄生部位:小肠分布地点:杭州种的描述:根据10个标本,结合活体观察。体呈柳叶形,1.91…     

绒山蝠肝细胞电镜观察和乳酸脱氢酶同工酶的研究

本文用光镜和电镜观察了绒山蝠肝细胞的超微结构,用聚内烯酰胺凝胶电泳,对肝组织ＬＤＨ同工酶进行了研究。肝细胞有丰富的线粒体、内质网、核糖体,发达的高尔基体、溶酶体等。在线粒体的周围有一层粗面内质网包绕,二者的密切关系,不仅在绒山蝠其他组织中,且在大部分哺乳动物细胞中均未观察到。该种肝细胞的ＬＤＨ同工酶以Ｍ亚基为主,主要催化丙酮酸还原成乳酸。     

回声定位蝙蝠耳蜗毛细胞静纤毛的长度特征

描电子显微镜下观察爪哇大足鼠耳蝠(Myotis adversus)、白腹管鼻蝠(Murina leucogaster)、山蝠(Nyctalus plancyi)和马铁菊头蝠(Rhinolophus ferrumequinum)耳蜗毛细胞静纤毛, 测量其长度, 并与五种非回声定位哺乳动物耳蜗静纤毛长度进行比较. 研究发现: 回声定位蝙蝠耳蜗外毛细胞静纤毛较非回声定位哺乳动物相应位置的短; 回声定位蝙蝠耳蜗内毛细胞静纤毛长于其外毛细胞静纤毛, 而非回声定位哺乳动物内毛细胞静纤毛长度并无此规律. 我们认为, 回声定位蝙蝠耳蜗听毛细胞静纤毛长度的特点可能是对高频声波和回声定位适应的结果.     

中华山蝠的研究进展及保护对策

中华山蝠(Ｎｙｃｔａｌｕｓｖｅｌｕｔｉｎｕｓ)(或称绒山蝠),属翼手目(Ｃｈｉｒｏｐｔｅｒａ),蝙蝠科(Ｖｅｓｐｅｒｔｉｌｉｏｎｉｄａｅ),山蝠属(Ｎｙｃｔａｌｕｓ),是我国特有的种类。广泛分布于中国南部,喜栖于建筑物的天花板、梁柱、瓦缝等处。有关中华山蝠的研究80年代才开始,迄今为止发表有关论文仅6篇。其中分类方面2篇,细胞遗传方面3篇,生态方面1篇,研究的深度及广度远远不够。中华山蝠捕食大量的蚊虫,为人类的健康作出了极大的贡献。然而,随着城市建设步伐的加快,大量旧的建筑物被装修或折迁,中华山蝠的栖息环境遭到极大的破坏,数…     

三峡工程重庆库区民翼手类研究

1996年至1997年,通过对三峡工程重庆库区13个县（区）68个洞穴的考察和标本采集,结合历史资料记述,确认重庆库区共有翼手目动物4科26种。其中8种为重庆市新记录,分别是绒菊头蝠、皮菊头蝠、西南鼠耳蝠、水鼠耳蝠、尖耳鼠耳蝠、大足鼠耳蝠、长折翼蝠和皱唇蝠。研究发现冀手类更喜欢潮湿、低海拔、人类干扰少、洞深在50m以上、周围是农田－草灌的洞穴。     

蝙蝠和鲸都是种名吗

初中《动物学》课本在讲哺乳纲的翼手目和鲸目时,介绍了蝙蝠和鲸。我们查阅了《辞海》(生物分册)553页,书中写到:“蝙蝠,哺乳纲、翼手目动物的通称,是具有飞翔能力的哺乳动物……分大蝙蝠和小蝙蝠两大类。前者体型大,第一和第二指均有爪,以果实为食,如狐蝠、果蝠、犬蝠。后者体型较小,仅第一指具爪,种类较多,一般以昆虫为食,如菊头蝠、蹄蝠、伏翼(家蝠)、山蝠、大耳蝠等。可见,     

动物细胞的多功能细胞器——鞭毛、纤毛和微绒毛(3)

动物是从单细胞生物中带鞭毛的领鞭毛虫演化而来的,但是在过去的很长一段时期中,人们普遍认为动物身体内的多数细胞是不带鞭毛的,只有精子、呼吸道和输卵管的上皮细胞有能够摆动的鞭毛(称动纤毛)。在20世纪60年代,人们就发现动物细胞上不能摆动的鞭毛(称静纤毛),但是由于不知其生理功能而不被重视。在21世纪初,科学家发现,多囊肾其实是与纤毛有关的疾病,随后对纤毛的研究才进入热潮。近年来的研究表明,在脑脊液的流动和动物内脏位置左右不对称分布上动纤毛发挥关键作用。而静纤毛存在于动物的许多细胞上,含有各种感觉受体,成为动物细胞接收信号的"天线"。它们能够感知动物体内多种液体的流动情况,被动物用于监测血压、眼压、胆汁流动、尿液流动和感知骨骼负荷;动物的视觉、听觉、嗅觉、味觉、触觉、自体感觉、细胞运动也是通过静纤毛接收信号的。在动物胚胎的发育过程中,静纤毛也负责细胞的信息接收,是Hedgehog(刺猬蛋白)信号通路、Wnt信号通路、Notch信号通路等的起始处。由于纤毛在动物体内的多种功能,纤毛功能障碍会导致全身性疾病,统称纤毛病(ciliopathy),包括嗅觉丧失、听觉丧失、视网膜退化、雄性不育、脑室积水、脑发育障碍、骨骼畸形、多指、多囊肾、多囊肝、内脏位置左右颠倒等多种症状。领鞭毛虫的另一个线状结构——领毛,演变成为动物细胞上的微绒毛,像静纤毛一样,成为细胞接收信号的"天线",在视觉、听觉、嗅觉、味觉、触觉和自体感觉中发挥作用。因此鞭毛、纤毛和微绒毛一起,被认为是动物细胞上的多功能细胞器。     

动物细胞的多功能细胞器——鞭毛、纤毛和微绒毛(2)

动物是从单细胞生物中带鞭毛的领鞭毛虫演化而来的,但是在过去的很长一段时期中,人们普遍认为动物身体内的多数细胞是不带鞭毛的,只有精子、呼吸道和输卵管的上皮细胞有能够摆动的鞭毛(称动纤毛)。在20世纪60年代,人们就发现动物细胞上不能摆动的鞭毛(称静纤毛),但是由于不知其生理功能而不被重视。在21世纪初,科学家发现,多囊肾其实是与纤毛有关的疾病,随后对纤毛的研究才进入热潮。近年来的研究表明,在脑脊液的流动和动物内脏位置左右不对称分布上动纤毛发挥关键作用。而静纤毛存在于动物的许多细胞上,含有各种感觉受体,成为动物细胞接收信号的"天线"。它们能够感知动物体内多种液体的流动情况,被动物用于监测血压、眼压、胆汁流动、尿液流动和感知骨骼负荷;动物的视觉、听觉、嗅觉、味觉、触觉、自体感觉、细胞运动也是通过静纤毛接收信号的。在动物胚胎的发育过程中,静纤毛也负责细胞的信息接收,是Hedgehog(刺猬蛋白)信号通路、Wnt信号通路、Notch信号通路等的起始处。由于纤毛在动物体内的多种功能,纤毛功能障碍会导致全身性疾病,统称纤毛病(ciliopathy),包括嗅觉丧失、听觉丧失、视网膜退化、雄性不育、脑室积水、脑发育障碍、骨骼畸形、多指、多囊肾、多囊肝、内脏位置左右颠倒等多种症状。领鞭毛虫的另一个线状结构——领毛,演变成为动物细胞上的微绒毛,像静纤毛一样,成为细胞接收信号的"天线",在视觉、听觉、嗅觉、味觉、触觉和自体感觉中发挥作用。因此鞭毛、纤毛和微绒毛一起,被认为是动物细胞上的多功能细胞器。     

Analyses of 22S Dynein Binding to Tetrahymena Axonemes Lacking Outer Dynein Arms

ABSTRACT. Tetrahymena thermophila mutants homozygous for the oad mutation become nonmotile when grown at the restrictive temperature of 39° C. Axonemes isolated from nonmotile oad mutants ( oad 39° C axonemes) lack approximately 90% of their outer dynein arms and are deficient in 22S dynein. Here we report that oad 39° C axonemes contain 40% of the 22S dynein heavy chains that wild-type axonemes contain and that oad axonemes do not undergo ATP-induced microtubule sliding in vitro. Wild-type 22S dynein will bind to the outer arm position in oad axonemes and restore ATP-induced microtubule sliding in those axonemes. Unlike wild-type 22S dynein, oad 22S dynein does not bind to the outer arm position in oad axonemes. These data indicate that the oad mutation affects some component of the outer arm dynein itself rather than the outer arm dynein binding site. These data also indicate that oad axonemes can be used to assay outer dynein arm function.     

A Temperature-Sensitive Mutation Affecting Synthesis of Outer Arm Dyneins in Tetrahymena thermophila

ABSTRACT. We have characterized a novel, temperature-sensitive mutation affecting motility in Tetrahymena thermophila . Mutants grew and divided normally at the restrictive temperature (38°C), but became nonmotile. Scanning electron microscopic analysis indicated that nonmotile mutants contained the normal number of cilia and that the cilia were of normal length. Transmission electron microscopic analysis indicated that axonemes isolated from nonmotile mutants lacked outer dynein arms, so the mutation was named oad I ( outer arm defficient ). Motile mutants shifted to 38° C under conditions that prevent cell growth and division (starvation) remained motile suggesting that once assembled into axonemes at the permissive temperature (28° C) the outer arm dyneins remain functional at 38° C. Starved, deciliated mutants regenerated a full complement of functional cilia at 38° C, indicating that the mechanism that incorporates the outer arm dynein into developing axonemes is not affected by the oad I mutation. Starved, nonmotile mutants regained motility when shifted back to 28° C, but not when incubated with cycloheximide. We interpret these results to rule out the hypothesis that the oad I mutation affects the site on the microtubules to which the outer arm dyneins bind. Axonemes isolated from mutants grown for one generation at 38° C had a mean of 6.0 outer arm dyneins, and axonemes isolated from mutants grown for two generations at 38° C had a mean of 3.2 outer arm dyneins. Taken together, these results indicate that the oad I mutation affects the synthesis of outer arm dyneins in Tetrahymena .     

Substructure of solitary cilia in mouse kidney

Summary Recent scanning electron microscopic studies confirm the presence of solitary cilia on most epithelial cells along the mammalian nephron and collecting ducts.By transmission electron microscopy we have found that the axonemata of such cilia consist of a maximal number of 9 doublet and no singlet filaments. 10% of the cross-sectioned cilia contain 9 doublets arranged in a peripheral ring (9+0 pattern). 30 % of the cross-sections contain 8 or 7 doublets in peripheral ring and 1 or 2 doublets in the central region (8+1 and 7+2 patterns). Serial sections and goniometer tilt reveal the central doublets to originate as dislodged peripheral doublets. 60% of the sectioned cilia contain filament numbers between 8 and 4. In patterns of 5 and 4 filaments single microtubules predominate.The functional significance of these atypical cilia is discussed.We are indebted to Prof. B. Afzelius and Prof. Th. Brun for valuable information and discussions during this work. The technical assistance of Miss K. Weltzin, Mr. E. Erichsen, Mr. R. Jensen and Mr. J. Røli is greatly appreciated     

The exocyst localizes to the primary cilium in MDCK cells

Primary cilia play a role in the maintenance of tubular epithelial differentiation and ciliary dysfunction can result in abnormal cyst formation, such as occurs in autosomal dominant polycystic kidney disease (ADPKD). We previously showed that the exocyst, an eight-protein complex involved in the biogenesis of polarity from yeast to mammals, is centrally involved in cyst formation [Mol. Biol. Cell. 11 (2000) 4259]. Here we show that the exocyst complex localizes to the primary cilium in Madin-Darby canine kidney (MDCK) tubular epithelial cells. We further show that the exocyst is overexpressed in both cell lines and primary cell cultures of ADPKD origin, suggesting that the exocyst may be involved in the pathogenesis of ADPKD.     

Regulation of outer-arm-dynein activity by phosphorylation and control of ciliary beat frequency

Summary Ciliary beating is empowered by a mechanochemical enzyme, dynein, which appears as two rows of projections on doublet microtubules. While inner-arm dyneins modulate beat form, outer-arm dynein empowers ciliary beat and sets beat frequency. Beat frequency is controlled via phosphorylation of outer-arm dynein. UsingParamecium tetraurelia as model system, we have previously identified a regulatory light chain of outer-arm dynein (22S dynein), M_r29 (p29), whose phosphorylation is cAMP-dependent. The phosphorylation state of the p29 in 22 S dynein determines in vitro microtubule translocation velocity. Although in vitro phosphorylation of p29 takes place in a short time, the percent change ist significantly less than the percent change in dynein activation, or in ciliary beat frequency. A potential mechanism that explains how a few activated dyneins can change ciliary beating is discussed.     

The structure of the tips of mammalian respiratory cilia

Summary The ciliary crown and the relationship of the ciliary crown to the underlying axoneme were studied by electron microscopy in cilia from hamster and rat trachea and bronchioles, and rabbit trachea. The ciliary crown is a cluster of 4 to 6 fibrils 35 nm long protruding beyond the plasma membrane at the tips of the cilia. The fibrils are well preserved after tannic acidglutaraldehyde-osmium tetroxide fixation and have high contrast with a periodic density of 4.5 nm. They stain relatively weakly with phosphotungstic acid. The surface of the fibrils stains with ruthenium red.The microtubules of the axoneme end in a plate of electron dense amorphous material. A five layered disc occupies the space between the membrane and the amorphous plate at the tip of the axoneme. The plasma membrane can be dissolved with the detergent triton X-100 without loss of the ciliary crown. This indicates that the ciliary crown is composed of transmembranous filaments which are bound to the disc at the tip of the axoneme.Supported by U.S.P.H.S. Research Grant number HL-12650     

Elektronenmikroskopische Untersuchungen zum Problem der Sekretion der bindegewebigen Interzellularsubstanz

Zusammenfassung Die Sinnesorgane des Vorderendes von Linens ruber werden elektronen-mikroskopisch vor allem im Hinblick auf die rezeptorischen Strukturen untersucht. Am Kopfvorderrand liegen zwei Rezeptortypen: Typ 1 ist mit 20–40, Typ 2 nur mit einer Zilie besetzt. Die Seitenwurzeln der Zilien von Typ 1 sind parallel angeordnet. Die Perikarya beider Rezeptoren liegen unterhalb des Epithelverbandes, dessen Großteil von Typ 1 eingenommen wird. In den Kopfspalten finden sich primäre Sinneszellen mit eingesenkten Zilien, deren Membran regelmäßig aufgeschwollen ist. Im Cerebralorgan dominiert ebenfalls eine primäre Sinneszelle, die reichlich efferent innerviert wird. In den Lichtrezeptoren findet sich eine Zilie unter dem distalen Mikrovillisaum.Alle beschriebenen Zilien sind deutlich voneinander und von den Wimpern der Epidermis unterschieden. Sie werden mit den Zilien der Rezeptoren anderer Tiergruppen verglichen.

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The fine structure of the sensory organs of Lineus ruber O. F. Müller (Nemertini, Heteronemertini)

Summary The sensory organs located in the head reagion of the ribbon worm Lineus ruber have been investigated with the electron microscope. Attention has been focussed on the apical cell-structures, which are assumed to be related to sensory functions. At the anterior edge of the head two receptor-types occur: type 1 bears 20–40 apical cilia, type 2 only 1 cilium per cell. The lateral ciliary rootlets of type 1 are oriented strictly parallel. The pericarya of both receptor types of which type 1 is particularly dominant, are situated below the basement lamina of the epithelium. In the cephalic clefts primary sensory cells occur, the cilia of which are invaginated into the apical cytoplasm. Their ciliary membrane exhibits regular inflations. In the cerebral organ also primary sensory cells dominate which receive an abundant efferent nerve supply. In the light receptors only one cilium is to be found below the distal villi. The cilia of the sensory cells and also of the ordinary epidermis cells show individual characteristics not shared by the other types. Their structural peculiarities are compared with those of sensory organs of other groups of animals.

Herrn Prof. Dr. Drs. h. c. W. Bargmann zum 65. Geburtstag gewidmet.     

Cilia in the accessory hyperstriatum of the domestic fowl

Summary Numerous neurons and glia in the accessory hyperstriatum of the domestic fowl contain a cilium that is attached to a basal body. The accessory centriole is in the vicinity of the basal body and in some instances a connection between the two centrioles is noted. Cross-striated rootlets are associated with the basal body and the accessory centriole, however, some rootlets are found distant to centrioles. Cross sections of cilia show that most accessory hyperstriatal cilia have an 8+1 fiber pattern. Several proposed functional roles of neuronal cilia are discussed.This investigation was supported by a research grant from the National Institute of Neurological Diseases and Stroke (5 RO 1 NSO 7557-02) awarded to Norma Jean Adamo.     

Cohesin protein SMC1 is a centrosomal protein

Structural maintenance of chromosome protein 1 (SMC1) is well known for its roles in sister chromatid cohesion and DNA repair. In this study, we report a novel centrosomal localization of SMC1 within the cytoplasm in a variety of mammalian cell lines. We showed that SMC1 localized to centrosomes throughout the cell cycle in a microtubule-independent manner. Biochemically, SMC1 was cofractionated with the centrosomal protein γ-tubulin in centrosomal preparation. Immunohistochemistry and immunoelectron microscopy performed on mouse tissue sections revealed that SMC1 antibody strongly labeled the base of cilia in ciliated epithelia, where basal bodies were located. Furthermore, we showed that SMC1 was associated with both centrioles of a centrosome at G0/G1 stage of the cell cycle. These results demonstrate that SMC1 is a centrosomal protein, suggesting possible involvement of SMC1 in centrosome/basal body-related functions, such as organization of dynamic arrays of microtubules and ciliary formation.