Jeon International Review of Cell and Molecular Biology

1. Auflage 2010
ISBN: 978-0-12-381012-0
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 279, 208 Seiten

Reihe: International Review of Cell and Molecular Biology

International Review of Cell and Molecular Biology presents current advances and comprehensive reviews in cell biology--both plant and animal. Articles address structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation and growth. Impact factor for 2008: 4.935. - Authored by some of the foremost scientists in the field - Provides up-to-date information and directions for future research - Valuable reference material for advanced undergraduates, graduate students and professional scientists

Autoren/Hrsg.

Jeon, Kwang W.

Inhaltsverzeichnis

1;Front Cover;1
2;International Review of Cell and Molecular Biology;4
3;Copyright Page;5
4;Contents;6
5;Contributors;8
6;Chapter 1: Functions of Claudin Tight Junction Proteins and Their Complex Interactions in Various Physiological Systems;10
6.1;1. Introduction;11
6.2;2. Tight Junction Membrane Integral Proteins;13
6.3;3. The Claudin Family of Tight Junction Proteins ;13
6.4;4. Claudin Interactions Within and Between TJ Strands;25
6.5;5. Is the Expression Level of Different Claudins Coregulated?;29
6.6;6. Claudin-Related Phenotypes;30
6.7;7. Concluding Remarks;35
6.8;Acknowledgment;36
6.9;References;36
7;Chapter 2: Secondary Symbiosis Between Paramecium and Chlorella Cells;42
7.1;1. Introduction;43
7.2;2. Infection Route;45
7.2.1;2.1. Classification of DVs;46
7.2.2;2.2. Timing of acidosomal and lysosomal fusion to DV;47
7.2.3;2.3. Presence of four cytological events needed to establish endosymbiosis;49
7.2.4;2.4. Initiation of algal cell division;60
7.2.5;2.5. Summary of the infection ro;61
7.3;3. Different Fates of Infection-Capable and Infection-Incapable Chlorella Species;61
7.3.1;3.1. Difference in algal attachment beneath the host cell surface;63
7.3.2;3.2. Relation between sugar residues of the algal cell wall and infectivity;66
7.3.3;3.3. Effects of WGA on the infectivity of C. sorokiniana C-212 to P. bursaria;69
7.4;4. Function of PV Membrane;70
7.4.1;4.1. Algal proteins necessary for the PV membrane;71
7.4.2;4.2. The PV membrane can provide protection from host lysosomal fusion;73
7.5;5. Host or Algal Changes Induced by Infection;77
7.6;6. Concluding Remarks;79
7.7;Acknowledgments;81
7.8;References;81
8;Chapter 3: Molecular Basis of Peroxisome Division and Proliferation in Plants;88
8.1;1. Introduction;89
8.2;2. Roles of PEROXIN11 Proteins, Dynamin-Related Proteins, and FISSION1;90
8.3;3. Other Proteins and Pathways;98
8.4;4. Environmental and Nuclear Regulation of Peroxisome Proliferation;100
8.5;5. Concluding Remarks;102
8.6;Acknowledgments;104
8.7;References;104
9;Chapter 4: New Insights into the Signal Transmission from Taste Cells to Gustatory Nerve Fibers ;110
9.1;1. Introduction;111
9.2;2. Diversity of Taste Bud Cells;112
9.3;3. Coding of Taste Information;117
9.4;4. Mechanisms for the Signal Transmission from Taste Cells to Gustatory Nerve Fibers;127
9.5;5. Concluding Remarks;134
9.6;Acknowledgments;135
9.7;References;135
10;Chapter 5: New Insights into the Regulation of Ion Channels by Integrins;144
10.1;1. Introduction;145
10.2;2. Main Structural Features of Integrins and Ion Channels ;146
10.3;3. An Outline of Integrin Signaling;152
10.4;4. Integrins and Ion Channels in Normal and Neoplastic Hematopoietic Cells;156
10.5;5. Integrins and Ion Channels in Cell Migration;172
10.6;6. Integrins and Ion Channels in the Nervous System;175
10.7;7. Concluding Remarks;185
10.8;Acknowledgments;186
10.9;References;187
11;Index;200

Leseproben

Chapter 1 Functions of Claudin Tight Junction Proteins and Their Complex Interactions in Various Physiological Systems
Liron Elkouby-Naor; Tamar Ben-Yosef    Department of Genetics, The Rappaport Family Institute for Research in the Medical Sciences, Technion-Israel Institute of Technology, Haifa, Israel Abstract
Members of the claudin family of proteins are the main components of tight junctions (TJs), the major selective barrier of the paracellular pathway between epithelial cells. As such, the claudins have the ability to generate the TJ physiological barrier and to control various physiological processes. Therefore, the importance of this family of proteins is obvious and many efforts were made to reveal different aspects of claudin TJ protein biology. In this review, we discuss recent advances in our understanding of claudin structure and function, as well as their distribution pattern in different organs and tissues. We mainly highlight the complex interactions of claudins in various physiological systems and suggest a possible role for a coregulation mechanism. Key Words Tight junctions Tight junction proteins Membrane proteins Claudin 1 Introduction
A hallmark in the development of multicellular organisms is the assembly of cellular sheets that separate compartments of different compositions. Maintenance of different compartments is performed by epithelial or endothelial cells, which adhere to each other by forming different types of intercellular junctions (Farquhar and Palade, 1963), including desmosomes (Kowalczyk et al., 1999), adherens junctions (AJs) (Nagafuchi, 2001), gap junctions (Goodenough et al., 1996), and tight junctions (TJs) (Anderson, 2001; Tsukita et al., 2001). The movement of solutes, ions, and water through epithelia occurs both across and between individual cells, and is referred to as the transcellular and the paracellular routes, respectively. Both routes display cell-specific and tissue-specific variations in permeability, and together account for the distinct transport properties of each tissue. The major barrier in the paracellular pathway is created by TJs, also known as zonula occludens (ZO; “occluding belt”). TJs can be found in various epithelial tissues, in which they form regions of intimate contact between the plasma membranes of adjacent cells (Farquhar and Palade, 1963) (Fig. 1.1A). In freeze-fracture replicas of epithelial cells TJs appear as a band-like network of branching and interconnecting thin ridges or complementary grooves, known as TJ strands (Farquhar and Palade, 1963). There is some evidence that TJs form an intramembrane diffusion barrier that restricts the lateral diffusion of apical and basolateral membrane components, thus maintaining cellular polarity (“fence function”) (Cereijido et al., 1998; Dragsten et al., 1981; van Meer and Simons, 1986; van Meer et al., 1986). TJs also close or seal the space between cells and thus set up a semipermeable barrier which prevents or reduces paracellular diffusion (“barrier function”) (Madara, 1998). Depending on the functional requirements of an epithelium, there may be small or large amounts of water and small solutes flowing passively through the TJ (Fromter and Diamond, 1972). The paracellular permeability of different epithelia was found to correlate with the number of TJ strands along the apical–basal axis (Claude and Goodenough, 1973). The morphological pattern of the strands also varies among tissues; however, the physiological correlate of these ultrastructural differences is yet unknown. The actual barrier capacity of TJs can be determined by measurements of the transepithelial electrical resistance (TER) (Fromter and Diamond, 1972). Figure 1.1 Paired TJ strands are formed by interactions between different claudins. (A) Schematic drawing of TJs that form regions of intimate contact between the plasma membranes of adjacent cells. Illustration of different claudins (B) which can interact with other homo- and heteropolymers within (C) and between (D) TJ strands. The main components of TJ strands are over 20 members of the claudin family of proteins. Claudins have various tissue distribution patterns, and many tissues express several different claudins which can interact with each other in both homotypic and heterotypic manners (Furuse et al., 1999; Morita et al., 1999) (Fig. 1.1B–D). Particular combinations and quantities of claudins modulate the charge-selective permeability of the paracellular pathway and, hence, take part in the regulation of the ionic makeup of extracellular fluids (Van Itallie and Anderson, 2006). Here, we review the functions of claudin TJ proteins and the complex interactions between them in various physiological systems. 2 Tight Junction Membrane Integral Proteins
TJ strands are composed of several types of membrane-spanning proteins: occludin (Furuse et al., 1993), members of the junction adhesion molecule (JAM) family (Mandell and Parkos, 2005), the coxsackievirus and adenovirus receptor (CAR) (Cohen et al., 2001), tricellulin (Ikenouchi et al., 2005; Riazuddin et al., 2006), and more than 20 members of the claudin family (Tsukita and Furuse, 2000; Van Itallie and Anderson, 2006). These strand-associated membrane proteins interact with the actin-based cytoskeleton (Turner, 2000), as well as with membrane-associated proteins that function as adapters and signaling proteins (Gonzalez-Mariscal et al., 2000; Mitic et al., 2000). Occludin was the first identified TJ protein. It is exclusively localized to TJs of both epithelial and endothelial cells (Furuse et al., 1993). Initially occludin was thought to be the main TJ sealing protein. However, several studies, including gene knockout analyses, revealed that TJ strands can be formed and function normally in the absence of occludin (Hirase et al., 1997; Moroi et al., 1998; Saitou et al., 1998; Wong and Gumbiner, 1997). JAMs are immunoglobulin superfamily proteins expressed at cell junctions in epithelial and endothelial cells, particularly at the apical-most part of the lateral membrane near the TJ. JAM proteins have been shown to bind to various TJ-associated cytoplasmic proteins. Despite compelling data implicating JAM proteins in formation of intercellular junctions, their direct role in the TJ has not been identified yet (Mandell and Parkos, 2005). CAR is a 46-kDa integral membrane protein with a typical transmembrane region, a long cytoplasmic domain, and an extracellular region composed of two Ig-like domains. In polarized epithelial cells CAR is expressed at the TJ, where it contributes to the barrier function (Cohen et al., 2001). Tricellulin is the most recently identified TJ integral membrane protein. It is concentrated at the vertically oriented TJ strands of tricellular contacts. Downregulation of tricellulin expression leads to compromised epithelial barrier function, and both bicellular and tricellular contacts were disorganized (Ikenouchi et al., 2005). Interestingly, in humans tricellulin mutations are associated with nonsyndromic deafness, a surprisingly limited phenotype, given the widespread tissue distribution of tricellulin in epithelial cells (Riazuddin et al., 2006). 3 The Claudin Family of Tight Junction Proteins
The claudin family includes more than 20 highly conserved TJ proteins (Table 1.1). Claudins 1 and -2 were discovered first, based on their cofractionation with occludin from isolated chicken liver junctions (Furuse et al., 1998a). Immunofluorescence and immunoelectron microscopy revealed that claudins 1 and -2 were both targeted to and incorporated into the TJ strand itself. When each of these proteins was transfected into cells that lack TJs, they were highly concentrated at cell–cell contact sites. In freeze-fracture replicas of these contact sites, well-developed networks of strands were identified that were similar to TJ strand networks in vivo (Furuse et al., 1998a). Taken together, the evidence strongly suggests that claudins are the primary proteins responsible for the physiological and structural paracellular barrier function of TJs (Tsukita and Furuse, 2000). Table 1.1 The claudin family Claudin 1 SEMP1 (senescence-associated epithelial membrane protein 1) CLDN1 3q28-29 Claudin 2 CLDN2 Xq22.3-23 Claudin 3 RVP1 (rat ventral prostate 1 protein) CLDN3 7q11.23 CPETR2 (Clostridium perfringens enterotoxin receptor 2) Claudin 4 CPE-R, CPER (Clostridium perfringens enterotoxin receptor) CLDN4 7q11.23 CPETR1 (Clostridium perfringens enterotoxin receptor 1) WBSCR8 (Williams-Beuren syndrome chromosomal region 8 protein) Claudin 5 TMVCF (transmembrane protein deleted in velo-cardio-facial...