{"title":"Syndrome of aluminum toxicity and diversity of aluminum resistance in higher plants.","authors":"Jian Feng Ma","doi":"10.1016/S0074-7696(07)64005-4","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)64005-4","url":null,"abstract":"<p><p>Aluminum (Al) is the most abundant metal in the earth's crust, while its soluble ionic form (Al(3+)) shows phytotoxicity, which is characterized by a rapid inhibition of root elongation. Aluminum targets multiple cellular sites by binding, resulting in disrupted structure and/or functions of the cell wall, plasma membrane, signal transduction pathway, and Ca homeostasis. On the other hand, some plant species have evolved mechanisms to cope with Al toxicity both externally and internally. The well-documented mechanisms for external detoxification of Al include the release of organic acid anions from roots and alkalination of the rhizosphere. Genes encoding transporters for Al-induced secretion of organic acid anions have been identified and characterized. Recent studies show that ABC transporters are involved in Al resistance. The internal detoxification of Al in Al-accumulating plants is achieved by the formation of nontoxic Al complexes with organic acids or other chelators and sequestration of these complexes in the vacuoles. In some plant species, Al shows beneficial effects on plant growth under particular conditions, although the exact mechanisms for these effects are unknown.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"264 ","pages":"225-52"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)64005-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27073174","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Neurogenesis in the fish retina.","authors":"Deborah L Stenkamp","doi":"10.1016/S0074-7696(06)59005-9","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)59005-9","url":null,"abstract":"<p><p>The retinas of teleost fish have long been of interest to developmental neurobiologists for their persistent plasticity during growth, life history changes, and response to injury. Because the vertebrate retina is a highly conserved tissue, the study of persistent plasticity in teleosts has provided insights into mechanisms for postembryonic retinal neurogenesis in mammals. In addition, in the past 10 years there has been an explosion in the use of teleost fish-zebrafish (Danio rerio) in particular-to understand the mechanisms of embryonic retinal neurogenesis in a model vertebrate with genetic resources. This review summarizes the key features of teleost retinal neurogenesis that make it a productive and interesting experimental system, and focuses on the contributions to our knowledge of retinal neurogenesis that uniquely required or significantly benefited from the use of a fish model system.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"259 ","pages":"173-224"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)59005-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26658865","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cell and molecular biology of the spindle matrix.","authors":"Kristen M Johansen, Jørgen Johansen","doi":"10.1016/S0074-7696(07)63004-6","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)63004-6","url":null,"abstract":"<p><p>The concept of a spindle matrix has long been proposed to account for incompletely understood features of microtubule spindle dynamics and force production during mitosis. In its simplest formulation, the spindle matrix is hypothesized to provide a stationary or elastic molecular matrix that can provide a substrate for motor molecules to interact with during microtubule sliding and which can stabilize the spindle during force production. Although this is an attractive concept with the potential to greatly simplify current models of microtubule spindle behavior, definitive evidence for the molecular nature of a spindle matrix or for its direct role in microtubule spindle function has been lagging. However, as reviewed here multiple studies spanning the evolutionary spectrum from lower eukaryotes to vertebrates have provided new and intriguing evidence that a spindle matrix may be a general feature of mitosis.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"263 ","pages":"155-206"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)63004-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26911419","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"LEM-Domain proteins: new insights into lamin-interacting proteins.","authors":"Nicole Wagner, Georg Krohne","doi":"10.1016/S0074-7696(07)61001-8","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)61001-8","url":null,"abstract":"<p><p>LEM-domain proteins present a growing family of nonrelated inner nuclear membrane and intranuclear proteins, including emerin, MAN1, LEM2, several alternatively spliced isoforms of LAP2, and various uncharacterized proteins in higher eukaryotes as well as the Drosophila-specific proteins otefin and Bocksbeutel. LEM-domain proteins are involved in diverse cellular processes including replication and cell cycle control, chromatin organization and nuclear assembly, the regulation of gene expression and signaling pathways, as well as retroviral infection. Genetic analyses in different model organisms reveal new insights into the various functions of LEM-domain proteins, lamins, and their involvement in laminopathic diseases. All these findings as well as previously proposed ideas and models have been summarized to broaden our view of this exciting protein family.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"261 ","pages":"1-46"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)61001-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26769758","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cell and molecular biology of transthyretin and thyroid hormones.","authors":"Samantha J Richardson","doi":"10.1016/S0074-7696(07)58003-4","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)58003-4","url":null,"abstract":"<p><p>Advances in four areas of transthyretin (TTR) research result in this being a timely review. Developmental studies have revealed that TTR is synthesized in all classes of vertebrates during development. This leads to a new hypothesis on selection pressure for hepatic TTR synthesis during development only, changing the previous hypotheses from \"onset\" of hepatic TTR synthesis in adulthood to \"maintaining\" hepatic TTR synthesis into adulthood. Evolutionary studies have revealed the existence of TTR-like proteins (TLPs) in nonvertebrate species and elucidated some of their functions. Consequently, TTR is an excellent model for the study of the evolution of protein structure, function, and localization. Studies of human diseases have demonstrated that TTR in the cerebrospinal fluid can form amyloid, but more recently there has been recognition of the roles of TTR in depression and Alzheimer's disease. Furthermore, amyloid mutations in human TTR that are the normal residues in other species result in cardiac deposition of TTR amyloid in humans. Finally, a revised model for TTR-thyroxine entry into the cerebrospinal fluid via the choroid plexus, based on data from studies in TTR null mice, is presented. This review concentrates on TTR and its thyroid hormone binding, in development and during evolution, and summarizes what is currently known about TLPs and the role of TTR in diseases affecting the brain.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"258 ","pages":"137-93"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)58003-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26586503","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Daylength measurements by rice plants in photoperiodic short-day flowering.","authors":"Takeshi Izawa","doi":"10.1016/S0074-7696(07)56006-7","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)56006-7","url":null,"abstract":"<p><p>Plants set seed at appropriate seasons. One major mechanism responsible for this adaptation involves photoperiodic flowering. Most plants are classified as either long-day plants, which flower under a longer photoperiod, or short-day plants, which flower under a shorter photoperiod. A third group, day-neutral plants, is not responsive to changes in photoperiod. During the past decade, molecular analysis has revealed at the molecular level how the long-day plant Arabidopsis thaliana measures daylength in photoperiodic flowering. In contrast, the molecular mechanisms underlying the responses of short-day plants are still under investigation. Progress in understanding photoperiodic flowering in rice (Oryza sativa), a short-day plant, revealed unique, evolutionarily conserved pathways involved in photoperiodic flowering at the molecular level. Furthermore, the conserved pathways promote flowering under short-day conditions and suppress flowering under long-day conditions in rice, but promote flowering under long-day conditions in Arabidopsis. In this chapter, we discuss the molecular mechanisms responsible for short-day flowering in rice in comparison with long-day flowering in Arabidopsis.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"256 ","pages":"191-222"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)56006-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26504694","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Role of CCN2/CTGF/Hcs24 in bone growth.","authors":"Satoshi Kubota, Masaharu Takigawa","doi":"10.1016/S0074-7696(07)57001-4","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)57001-4","url":null,"abstract":"<p><p>Our bones mostly develop through a process called endochondral ossification. This process is initiated in the cartilage prototype of each bone and continues through embryonic and postnatal development until the end of skeletal growth. Therefore, the central regulator of endochondral ossification is the director of body construction, which is, in other words, the determinant of skeletal size and shape. We suggest that CCN2/CTGF/Hcs24 (CCN2) is a molecule that conducts all of the procedures of endochondral ossification. CCN2, a member of the CCN family of novel modulator proteins, displays multiple functions by manipulating the local information network, using its conserved modules as an interface with a variety of other biomolecules. Under a precisely designed four-dimensional genetic program, CCN2 is produced from a limited population of chondrocytes and acts on all of the mesenchymal cells inside the bone callus to promote the integrated growth of the bone. Furthermore, the utility of CCN2 as regenerative therapeutics against connective tissue disorders, such as bone and cartilage defects and osteoarthritis, has been suggested. Over the years, the pathological action of CCN2 has been suggested. Nevertheless, it can also be regarded as another aspect of the physiological and regenerative function of CCN2, which is discussed as well.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"257 ","pages":"1-41"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)57001-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26536358","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Fibroblast differentiation in wound healing and fibrosis.","authors":"Ian A Darby, Tim D Hewitson","doi":"10.1016/S0074-7696(07)57004-X","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)57004-X","url":null,"abstract":"<p><p>The contraction of granulation tissue from skin wounds was first described in the 1960s. Later it was discovered that during tissue repair, fibroblasts undergo a change in phenotype from their normal relatively quiescent state in which they are involved in slow turnover of the extracellular matrix, to a proliferative and contractile phenotype termed myofibroblasts. These cells show some of the phenotypic characteristics of smooth muscle cells and have been shown to contract in vitro. In the 1990s, a number of researchers in different fields showed that myofibroblasts are present during tissue repair or response to injury in a variety of other tissues, including the liver, kidney, and lung. During normal repair processes, the myofibroblastic cells are lost as repair resolves to form a scar. This cell loss is via apoptosis. In pathological fibroses, myofibroblasts persist in the tissue and are responsible for fibrosis via increased matrix synthesis and for contraction of the tissue. In many cases this expansion of the extracellular matrix impedes normal function of the organ. For this reason much interest has centered on the derivation of myofibroblasts and the factors that influence their differentiation, proliferation, extracellular matrix synthesis, and survival. Further understanding of how fibroblast differentiation and myofibroblast phenotype is controlled may provide valuable insights into future therapies that can control fibrosis and scarring.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"257 ","pages":"143-79"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)57004-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26536787","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Mitotic spindle dynamics in Drosophila.","authors":"Ingrid Brust-Mascher, Jonathan M Scholey","doi":"10.1016/S0074-7696(06)59004-7","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)59004-7","url":null,"abstract":"<p><p>Mitosis, the process by which the replicated chromosomes are segregated equally into daughter cells, has been studied for over a century. Drosophila melanogaster is an ideal organism for this research. Drosophila embryos are well suited to image mitosis, because during cycles 10-13 nuclei divide rapidly at the surface of the embryo, but mitotic cells during larval stages and spermatocytes are also used for the study of mitosis. Drosophila can be easily maintained, many mutant stocks exist, and transgenic flies expressing mutated or fluorescently labeled proteins can be made. In addition, the genome has been completed and RNA interference can be used in Drosophila tissue culture cells. Here, we review our current understanding of spindle dynamics, looking at the experiments and quantitative modeling on which it is based. Many molecular players in the Drosophila mitotic spindle are similar to those in mammalian spindles, so findings in Drosophila can be extended to other organisms.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"259 ","pages":"139-72"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)59004-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26658862","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"YidC as an essential and multifunctional component in membrane protein assembly.","authors":"Dorothee Kiefer, Andreas Kuhn","doi":"10.1016/S0074-7696(06)59003-5","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)59003-5","url":null,"abstract":"<p><p>Membrane proteins fulfill a number of vital functions in prokaryotic and eukaryotic cells. They are often organized in multicomponent complexes, folded within the membrane bilayer and interacting with the cytoplasmic and periplasmic or external soluble compartments. For the biogenesis of integral membrane proteins, the essential biochemical steps are (1) the insertion and topogenesis of the transmembrane protein segments into the lipid bilayer, (2) the three-dimensional folding of the translocated hydrophilic domains, and (3) the assembly into multimeric complexes. Intensive research has elucidated the basic mechanisms of membrane protein insertion in the homologous translocation machineries of different cellular systems. Whereas the Sec translocation system is found in the endoplasmic reticulum of eukaryotic cells and in the prokaryotic plasma membrane, the YidC-Oxa1 membrane insertase is present in prokaryotic and organellar membranes. This review focuses on the discoveries of the YidC system in bacterial as well as the Oxa1/Alb3 protein family of eukaryotic cells and will particularly emphasize evolutionary aspects.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"259 ","pages":"113-38"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)59003-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26658929","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}