出版時間:2009-4 出版社:科學出版社 作者:Constance Hammond 頁數(shù):398
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前言
人腦或神經(jīng)系統(tǒng)是我們已知的宇宙中最復(fù)雜的物質(zhì)結(jié)構(gòu),神經(jīng)科學是探索腦的奧秘的科學,是21世紀迅猛發(fā)展的生命科學中最為突出的領(lǐng)域之一。過去的十多年中,分子生物學和計算機科學技術(shù)的快速發(fā)展,極大地推動了神經(jīng)科學的發(fā)展,人類基因組DNA序列的闡明及其對神經(jīng)科學的推動、腦功能成像技術(shù)研究人腦和心理活動的巨大進展便是最突出的代表。對許多神經(jīng)元活動的基本過程,神經(jīng)科學家已經(jīng)可以通過基因操作,在基因及其編碼的蛋白分子的結(jié)構(gòu)和功能水平上進行描述和分析,從而精細地研究其復(fù)雜的細胞膜上和胞內(nèi)信號的調(diào)控分子機制。腦功能成像技術(shù)使得過去只能停留在人腦這個“黑箱”外、對心理現(xiàn)象的腦機制進行各種猜測和假說的時代成為過去,人腦的認知和思維活動變得“看得見”了。神經(jīng)科學不僅吸引著各類神經(jīng)生物學家、化學家和物理學家,而且吸引分子生物學家、計算機科學家和心理學家紛紛加入其中,成為真正意義上的多種學科交叉的科學。
內(nèi)容概要
這本《細胞分子神經(jīng)生理學》描述了神經(jīng)細胞生理活動過程的基本概念、基本原理和主要的實驗依據(jù),包括神經(jīng)細胞和膠質(zhì)細胞的結(jié)構(gòu)與功能、電壓門控性離子通道與神經(jīng)元的興奮性、受體門控性離子通道與突觸傳遞、神經(jīng)電信號在樹突一胞體的整合、神經(jīng)元發(fā)放模式、突觸可塑性以及神經(jīng)網(wǎng)絡(luò)等。盡管該書沒有探討多突觸信號的匯聚整合原理、整合信號驅(qū)動神經(jīng)細胞編程的機理、神經(jīng)信號編程的內(nèi)涵、神經(jīng)信號編程的穩(wěn)態(tài)以及網(wǎng)絡(luò)內(nèi)神經(jīng)元的時空編程等神經(jīng)科學的基本問題,但對于神經(jīng)生理學領(lǐng)域教學研究人員仍然是一本應(yīng)選用的好教科書,尤其是對于神經(jīng)科學的初學者來說,這本書是建立神經(jīng)生理學基本概念和知識的精品讀物。為了使初學者能夠盡快地把握該書的內(nèi)容,導讀作者用中文給出了各個章節(jié)的核心要點。
作者簡介
作者:(美國)Constance HammondLarry R. Squire is Distinguished Professor of Psy-chiatry, Neurosciences, and Psychology at the Univer-sity of California School of Medicine, San Diego, andResearch Career Scientist at the Veterans AffairsMedical Center, San Diego. He investigates the organi-zation and neurological foundations of memory. He isa former President of the Society for Neuroscience andis a member of the National Academy of Sciences andthe Institute of Medicine.Darwin K. Berg is Distinguished Professor in theDivision of Biological Sciences at the University ofCalifornia, San Diego. He has been chairman of theBiology Department and currently serves as Councilorof the Society for Neuroscience and as a Board memberof the Kavli Institute for Brain and Mind. His researchis focused on the roles of nicotinic cholinergic signal-ing in the vertebrate nervous system.Floyd Bloom is Professor Emeritus in the Molecularand Integrative Neuroscience Department (MIND) at The Scripps Research Institute. His recent awardsinclude the Sarnat Award from the Institute of Medi-cine and the Salmon Medal of the New York Academyof Medicine. He is a former President of the Society forNeuroscience and is a member of the NationalAcademy of Sciences and the Institute of Medicine. Sascha du Lac is an Investigator of the HowardHughes Medical Institute and an Associate Professorof Systems Neurobiology at the Salk Institute for Bio-logical Studies. Her research interests are in the neu-robiology of resilience and learning, and her laboratoryinvestigates behavioral, circuit, cellular, and molecularmechanisms in the sense of balance. Anirvan Ghosh is Stephen Kuffler Professor in theDivision of Biological Sciences at the University of California, San Diego and Director of the graduateprogram in Neurosciences. His research interestsinclude the development of synaptic connections inthe central nervous system and the role of activity-dependent gene expression in the cortical develop-ment. He is recipient of the Presidential Early CareerAward for Scientists and Engineers and the Society forNeuroscience Young Investigator Award. Nicholas C. Spitzer is Distinguished Professor inthe Division of Biological Sciences at the University of California, San Diego. His research is focusedon neuronal differentiation and the role of electricalactivity and calcium signaling in the assembly ofthe nervous system. He has been chairman ofthe Biology Department and the Neurobiology Section,a trustee of the Grass Foundation, and served as Councilor of the Society for Neuroscience. He is amember of the American Academy of Arts and Sci-ences and Co-Director of the Kavli Institute for Brainand Mind.
書籍目錄
前言致謝第1章 神經(jīng)元第2章 神經(jīng)元-膠質(zhì)細胞第3章 離子梯度、離子電流和膜電位第4章 電壓門控性鈉離子通道與動作電位第5章 電壓依賴式鈣離子通道與動作電位第6章 化學性突觸第7章 神經(jīng)遞質(zhì)釋放第8章 離子型乙酰膽堿受體(AChR)第9章 離子型GABAA受體第10章 離子型谷氨酸受體第11章 代謝型GABAB受體第12章 代謝型谷氨酸受體第13章 胞體一樹突對突觸后電位的編輯處理:生物膜的被動特性第14章 胞體-樹突膜上閾下電壓門控電流第15章 低閾值電壓門控電流在胞體-樹突對突觸后電位的編輯處理中的作用第16章 高電壓激活的去極化電流在胞體一樹突對突觸后電位的編輯處理中的作用第17章 神經(jīng)元放電模式第18章 突觸可塑性第19章 成體海馬網(wǎng)絡(luò)第20章 海馬神經(jīng)網(wǎng)絡(luò)的成熟索引
章節(jié)摘錄
插圖:Acetylcholinesterases are glycoproteins synthesizedin the soma and carried to the terminals via antero-grade axonal transport. They are inserted into thepresynaptic membrane and the basal lamina. They dis-play an important structural polymorphism (Figure6.12b): they have a globular form (G) or an asymmetricform (A). These different forms have distinct localiza-tions. Globular forms (G) are anchored in the pre- orpostsynaptic membrane (these are ectoenzymes) andare secreted as a soluble protein into the synaptic cleft.Asymmetric forms (A) are anchored in the basal lam-ina (Figure 6.12c). The molecules of acetylcholine,released in the synaptic cleft when the neuromuscularjunction is activated, cross the basal lamina through itsloose stitches. But a part of the acetylcholine moleculesis also degraded before being fixed to postsynapticreceptors, by the acetylcholinesterase inserted in thebasal lamina. The other part is quickly degraded afterits fixation. Acetylcholinesterases hydrolyze acetyl-choline into acetic acid and choline. Choline is takenup by presynaptic terminals for the synthesis of newmolecules of acetylcholine. This degradation system ofacetylcholine is a very efficient system for inactivationof a neurotransmitter.6.3.3 Nicotinic receptors for acetylcholine are abundant in the crests of the folds in the postsynaptic membrane The plasma membrane of muscle cells, the sar-colemma, presents numerous folds in mammalian neu-romuscular junctions. By using a radioactive ligand for atype of acetylcholine nicotinic receptor, c-bungarotoxinlabelled with a radioactive isotope or a fluorescent mole-cule, it has been shown that the radioactive materialaccumulates predominantly in the crests of the folds inthe sarcolemma. Immunocytochemical techniques pro-duce similar results. Other studies have shown that theyare anchored to the underlying cytoskeleton (see thefollowing section). The nicotinic receptor is a transmembrane glycopro-tein comprising four homologous subunits assembledinto a heterologous 2B8 pentamer. It is a receptorchannel permeable to cations whose activation resultsin the net entry of positively charged ions and in depolar-ization of the postsynaptic membrane. The structureand functional characteristics of the muscular icotinicreceptors are given in Chapter 8.6.3.4 Mechanisms involved in the accumulation of postsynaptic receptorsin the folds of the postsynaptic muscular membrane The acetylcholine nicotinic receptors are, in theadult neuromuscular junction, present in high density(about 10,000 molecules per itm) in the postsynapticregions and occur in a much lower density in thenonsynaptic membrane (extrajunctional membrane).Under the nerve terminal, the muscle cell is free of themyofimanents actin and myosin. At this level, four toeight cell nuclei are found, the fundamental nuclei(Ranvier 1875). The myonuclei located outside the post-synaptic region (extrasynaptic) are the sarcoplasmicnuclei. The formation of this well organized subsynapticdomain - which concerns not only the nicotinic recep-tors but also the Golgi apparatus and the cytoskeleton(it also comprises the organization of the basal laminaand the distribution of the asymmetric form of acetyl-cholinesterase in the synaptic cleft) - occurs in numer-ous steps during maturation of the neuromuscularjunction (Figure 6.13a): There is an increase in the number of nicotinicreceptors (1 and 2) during fusion of the myoblasts to form myotubes, owing to the neosynthesis of these receptors. They have an even distribution over the membrane surface. This phenomenon is independent of the neuromuscular activity since it is not affected by the injection in ovo of nicotinic antagonists such as curare.~ There is formation of aggregates of nicotinic receptors under the nerve terminal (3-5) and disappearance of extrajunctional receptors (5).
編輯推薦
《細胞和分子神經(jīng)生理學(第3版)(導讀版·原版引進)》是建立神經(jīng)生理學基本概念和知識的精品讀物。為了使初學者能夠盡快地把握該書的內(nèi)容,導讀作者用中文給出了各個章節(jié)的核心要點。
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