H. Lodish - Molecular Cell Biology (5ed, Freeman, 2003) (796244), страница 102
Текст из файла (страница 102)
Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 84:345–357.Hynes, R. O. 1999. Cell adhesion: old and new questions. TrendsCell Biol. 9(12):M33–M337. Millennium issue.Hynes, R. O. 2002. Integrins: bidirectional, allosteric signalingmachines. Cell 110:673–687.Jamora, C., and E. Fuchs. 2002. Intercellular adhesion, signallingand the cytoskeleton. Nature Cell Biol.
4(4):E101–E108.Juliano, R. L. 2002. Signal transduction by cell adhesion receptors and the cytoskeleton: functions of integrins, cadherins, selectins,and immunoglobulin-superfamily members. Ann. Rev. Pharmacol.Toxicol. 42:283–323.−200204060Time (min)Leahy, D. J. 1997. Implications of atomic resolution structuresfor cell adhesion. Ann. Rev. Cell Devel. Biol. 13:363–393.Sheetlike Epithelial Tissues: Junctions and Cell-AdhesionMoleculesBoggon, T. J., et al.
2002. C-cadherin ectodomain structure andimplications for cell adhesion mechanisms. Science 296:1308–1313.Clandinin, T. R., and S. L. Zipursky. 2002. Making connectionsin the fly visual system. Neuron 35:827–841.Conacci-Sorrell, M., J. Zhurinsky, and A. Ben-Ze’ev.
2002. Thecadherin-catenin adhesion system in signaling and cancer. J. Clin.Invest. 109:987–991.Fuchs, E., and S. Raghavan. 2002. Getting under the skin of epidermal morphogenesis. Nature Rev. Genet. 3(3):199–209.Leckband, D. 2002. The structure of the C-cadherin ectodomainresolved. Structure (Camb). 10:739–740.Pierschbacher, M. D., and E. Ruoslahti. 1984. Cell attachmentactivity of fibronectin can be duplicated by small synthetic fragmentsof the molecule. Nature 309(5963):30–33.Schöck, F., and N. Perrimon. 2002. Molecular mechanisms ofepithelial morphogenesis.
Ann. Rev. Cell Devel. Biol. 18:463–493.Shimaoka, M., J. Takagi, and T. A. Springer. 2002. Conformational regulation of integrin structure and function. Ann. Rev. Biophys. Biomol. Struc. 31:485–516.Tsukita, S., M. Furuse, and M. Itoh. 2001. Multifunctionalstrands in tight junctions. Nature Rev. Mol. Cell Biol. 2:285–293.ReferencesXiong, J. P., et al. 2001.
Crystal structure of the extracellularsegment of integrin V3. Science 294:339–345.The Extracellular Matrix of Epithelial SheetsBoutaud, A., et al. 2000. Type IV collagen of the glomerularbasement membrane: evidence that the chain specificity of networkassembly is encoded by the noncollagenous NC1 domains. J. Biol.Chem.
275:30716–30724.Esko, J. D., and U. Lindahl. 2001. Molecular diversity of heparan sulfate. J. Clin. Invest. 108:169–173.Hohenester, E., and J. Engel. 2002. Domain structure and organisation in extracellular matrix proteins. Matrix Biol. 21(2):115–128.Nakato, H., and K. Kimata. 2002. Heparan sulfate fine structure and specificity of proteoglycan functions.
Biochim. Biophys.Acta 1573:312–318.Perrimon, N., and M. Bernfield. 2001. Cellular functions of proteoglycans: an overview. Semin. Cell Devel. Biol. 12(2):65–67.Rosenberg, R. D., et al. 1997. Heparan sulfate proteoglycans ofthe cardiovascular system: specific structures emerge but how is synthesis regulated? J. Clin. Invest. 99:2062–2070.The Extracellular Matrix of Nonepithelial TissuesKramer, R. Z., J. Bella, B. Brodsky, and H. M. Berman.
2001.The crystal and molecular structure of a collagen-like peptide witha biologically relevant sequence. J. Mol. Biol. 311:131–147.Mao, J. R., and J. Bristow. 2001. The Ehlers-Danlos syndrome:on beyond collagens. J. Clin. Invest. 107:1063–1069.Shaw, L. M., and B. R. Olsen. 1991. FACIT collagens: diversemolecular bridges in extracellular matrices. Trends Biochem. Sci.16(5):191–194.Weiner, S., W. Traub, and H. D. Wagner. 1999. Lamellar bone:structure–function relations. J. Struc. Biol.
126:241–255.Adhesive Interactions Involving Nonepithelial CellsBartsch, U. 2003. Neural CAMs and their role in thedevelopment and organization of myelin sheaths. Front. Biosci.8:D477–D490.Brummendorf, T., and V. Lemmon. 2001. Immunoglobulin superfamily receptors: cis-interactions, intracellular adapters and alternative splicing regulate adhesion. Curr. Opin. Cell Biol. 13:611–618.Cukierman, E., R. Pankov, and K.
M. Yamada. 2002. Cell interactions with three-dimensional matrices. Curr. Opin. Cell Biol.14:633–639.Durbeej, M., and K. P. Campbell. 2002. Muscular dystrophiesinvolving the dystrophin-glycoprotein complex: an overview of current mouse models. Curr. Opin. Genet. Devel. 12:349–361.Geiger, B., A. Bershadsky, R.
Pankov, and K. M. Yamada. 2001.Transmembrane crosstalk between the extracellular matrix and thecytoskeleton. Nature Rev. Mol. Cell Biol. 2:793–805.Hobbie, L., et al. 1987. Restoration of LDL receptor activity inmutant cells by intercellular junctional communication. Science235:69–73.243Lawrence, M. B., and T. A. Springer. 1991. Leukocytes roll ona selectin at physiologic flow rates: distinction from and prerequisitefor adhesion through integrins. Cell 65:859–873.Lo, C.
Gap junctions in development and disease. Ann. Rev. Cell.Devel. Biol. 10.1146/annurev.cellbio.19.111301.144309. (Expectedto be published in 2003.)Reizes, O., et al. 2001. Transgenic expression of syndecan-1 uncovers a physiological control of feeding behavior by syndecan-3.Cell 106:105–116.Somers, W. S., J.
Tang, G. D. Shaw, and R. T. Camphausen.2000. Insights into the molecular basis of leukocyte tethering androlling revealed by structures of P- and E-selectin bound to SLe(X)and PSGL-1. Cell 103:467–479.Stein, E., and M. Tessier-Lavigne. 2001. Hierarchical organization of guidance receptors: silencing of netrin attraction by Slitthrough a Robo/DCC receptor complex. Science 291:1928–1938.Plant TissuesDelmer, D. P., and C.
H. Haigler. 2002. The regulation of metabolic flux to cellulose, a major sink for carbon in plants. Metab. Eng.4:22–28.Iwai, H., N. Masaoka, T. Ishii, and S. Satoh. 2000. A pectin glucuronyltransferase gene is essential for intercellular attachment in theplant meristem. Proc. Nat’l. Acad. Sci. USA 99:16319–16324.Lord, E. M. 2003. Adhesion and guidance in compatible pollination. J. Exp. Bot. 54(380):47–54.Lord, E. M., and J. C. Mollet.
2002. Plant cell adhesion: a bioassay facilitates discovery of the first pectin biosynthetic gene. Proc.Nat’l. Acad. Sci. USA 99:15843–15845.Lord, E. M., and S. D. Russell. 2002. The mechanisms of pollination and fertilization in plants. Ann. Rev. Cell Devel. Biol.18:81–105.Pennell, R. 1998. Cell walls: structures and signals.
Curr. Opin.Plant Biol. 1:504–510.Ross, W. Whetten, J. J. MacKay, and R. R. Sederoff. 1998. Recent advances in understanding lignin biosynthesis. Ann. Rev. PlantPhysiol. Plant Mol. Biol. 49:585–609.Zambryski, P., and K. Crawford. 2000. Plasmodesmata: gatekeepers for cell-to-cell transport of developmental signals in plants.Ann. Rev. Cell Devel. Biol. 16:393–421.Growth and Use of Cultured CellsDavis, J. M., ed. 1994. Basic Cell Culture: A Practical Approach.IRL Press.Goding, J. W. 1996.
Monoclonal Antibodies: Principles and Practice. Production and Application of Monoclonal Antibodies in CellBiology, Biochemistry, and Immunology, 3d ed. Academic Press.Kohler, G., and C. Milstein. 1975. Continuous cultures of fusedcells secreting antibody of predefined specificity. Nature256:495–497.Shaw, A. J., ed. 1996. Epithelial Cell Culture. IRL Press.Tyson, C. A., and J. A.
Frazier, eds. 1993. Methods in Toxicology. Vol. I (Part A): In Vitro Biological Systems. Academic Press. Describes methods for growing many types of primary cells in culture.7TRANSPORT OFIONS AND SMALLMOLECULES ACROSSCELL MEMBRANESAquaporin, the water channel, consists of four identical transmembrane polypeptides.The plasma membrane is a selectively permeable barrier between the cell and the extracellular environment. Its permeability properties ensure thatessential molecules such as ions, glucose, amino acids, andlipids readily enter the cell, metabolic intermediates remain in the cell, and waste compounds leave the cell.
Inshort, the selective permeability of the plasma membraneallows the cell to maintain a constant internal environment. In Chapter 5, we learned about the components andstructural organization of cell membranes. Movement ofvirtually all molecules and ions across cellular membranesis mediated by selective membrane transport proteins embedded in the phospholipid bilayer. Because different celltypes require different mixtures of low-molecular-weightcompounds, the plasma membrane of each cell type contains a specific set of transport proteins that allow onlycertain ions and molecules to cross.