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991.
992.
Ji-Jian Chow Kamran Ahmed Zahoor Fazili Mohammed Sheikh Matin Sheriff 《Reviews in urology》2014,16(2):76-82
Renal cell carcinoma without metastasis responds well to surgical excision but is known to recur postnephrectomy. In a small but significant number of patients this recurrence is not accompanied by metastasis, which is important as these people benefit from further surgery. We examined 20 articles from the current literature to ascertain how best to treat this condition. Surgical management renders better results than conservative or medical therapies. Readily available investigations such as blood tests and computed tomography can help determine the right patients for surgery in an evidence-based fashion. Current findings have allowed us to suggest a protocol for the treatment of solitary renal fossa recurrence of postnephrectomy renal cell carcinoma. There are further opportunities for study in validating our protocol, and in novel renal cell carcinoma treatment strategies that have not been tested on solitary renal fossa recurrences.Key words: Renal cancer, Recurrence, Nephrectomy, Complications, ManagementKidney cancers represent 2% of cancers worldwide; the most common type is renal cell carcinoma. Curative treatment of localized disease is a nephrectomy. Following surgery, recurrence can happen locally with an incidence of 1.61%.1–5 A solitary renal fossa local recurrence is rare but important to distinguish from local recurrence with metastasis, which would not benefit from surgical resection. The 5-year survival postresection of local recurrence for those without metastasis compared with those with metastasis was 62% compared with 0%.4 The kidneys are bordered by the colon, spleen, liver, stomach, and associated neurovascular structures, all of which may be invaded in this form of recurrence; specific morbidity is related to the invasion and subsequent resection of these organs. General morbidity is caused by the surgery itself, with pain, infection, and hemorrhage being major contributors (Figure 1). This article explains predictive factors in recurrence, useful diagnostic modalities, and management, and provides recommendations and highlights opportunities for further study.Open in a separate windowFigure 1Computed tomography image of a patient with renal fossa recurrence of renal cancer after nephrectomy. Of note is the large mass identifiable in the spleen. 相似文献
993.
Drought is a major environmental stress threatening wheat productivity worldwide. Global climate models predict changed precipitation patterns with frequent episodes of drought. Although drought impedes wheat performance at all growth stages, it is more critical during the flowering and grain-filling phases (terminal drought) and results in substantial yield losses. The severity and duration of the stress determine the extent of the yield loss. The principal reasons for these losses are reduced rates of net photosynthesis owing to metabolic limitations—oxidative damage to chloroplasts and stomatal closure—and poor grain set and development. A comprehensive understanding of the impact of terminal drought is critical for improving drought resistance in wheat, with marker-assisted selection being increasingly employed in breeding for this resistance. The limited success of molecular breeding and physiological strategies suggests a more holistic approach, including interaction of drought with other stresses and plant morphology. Furthermore, integration of physiological traits, genetic and genomic tools, and transgenic approaches may also help to improve resistance against drought in wheat. In this review, we describe the influence of terminal drought on leaf senescence, carbon fixation, grain set and development, and explain drought resistance mechanisms. In addition, recent developments in integrated approaches such as breeding, genetics, genomics, and agronomic strategies for improving resistance against terminal drought in wheat are discussed. 相似文献
994.
Nikolaus Pfanner Martin van der Laan Paolo Amati Roderick A. Capaldi Amy A. Caudy Agnieszka Chacinska Manjula Darshi Markus Deckers Suzanne Hoppins Tateo Icho Stefan Jakobs Jianguo Ji Vera Kozjak-Pavlovic Chris Meisinger Paul R. Odgren Sang Ki Park Peter Rehling Andreas S. Reichert M. Saeed Sheikh Susan S. Taylor Nobuo Tsuchida Alexander M. van der Bliek Ida J. van der Klei Jonathan S. Weissman Benedikt Westermann Jiping Zha Walter Neupert Jodi Nunnari 《The Journal of cell biology》2014,204(7):1083-1086
The mitochondrial inner membrane contains a large protein complex that functions in inner membrane organization and formation of membrane contact sites. The complex was variably named the mitochondrial contact site complex, mitochondrial inner membrane organizing system, mitochondrial organizing structure, or Mitofilin/Fcj1 complex. To facilitate future studies, we propose to unify the nomenclature and term the complex “mitochondrial contact site and cristae organizing system” and its subunits Mic10 to Mic60.Mitochondria possess two membranes of different architecture and function (Palade, 1952; Hackenbrock, 1968). Both membranes work together for essential shared functions, such as protein import (Schatz, 1996; Neupert and Herrmann, 2007; Chacinska et al., 2009). The outer membrane harbors machinery that controls the shape of the organelle and is crucial for the communication of mitochondria with the rest of the cell. The inner membrane harbors the complexes of the respiratory chain, the F1Fo-ATP synthase, numerous metabolite carriers, and enzymes of mitochondrial metabolism. It consists of two domains: the inner boundary membrane, which is adjacent to the outer membrane, and invaginations of different shape, termed cristae (Werner and Neupert, 1972; Frey and Mannella, 2000; Hoppins et al., 2007; Pellegrini and Scorrano, 2007; Zick et al., 2009; Davies et al., 2011). Tubular openings, termed crista junctions (Perkins et al., 1997), connect inner boundary membrane and cristae membranes (Fig. 1, A and B). Respiratory chain complexes and the F1Fo-ATP synthase are preferentially located in the cristae membranes, whereas preprotein translocases are enriched in the inner boundary membrane (Vogel et al., 2006; Wurm and Jakobs, 2006; Davies et al., 2011). Contact sites between outer membrane and inner boundary membrane promote import of preproteins, metabolite channeling, lipid transport, and membrane dynamics (Frey and Mannella, 2000; Sesaki and Jensen, 2004; Hoppins et al., 2007, 2011; Neupert and Herrmann, 2007; Chacinska et al., 2009; Connerth et al., 2012; van der Laan et al., 2012).Open in a separate windowFigure 1.MICOS complex. (A) The MICOS complex (hypothetical model), previously also termed MINOS, MitOS, or Mitofilin/Fcj1 complex, is required for maintenance of the characteristic architecture of the mitochondrial inner membrane (IM) and forms contact sites with the outer membrane (OM). In budding yeast, six subunits of MICOS have been identified. All subunits are exposed to the intermembrane space (IMS), five are integral inner membrane proteins (Mic10, Mic12, Mic26, Mic27, and Mic60), and one is a peripheral inner membrane protein (Mic19). Mic26 is related to Mic27; however, mic26Δ yeast cells show considerably less severe defects of mitochondrial inner membrane architecture than mic27Δ cells (Harner et al., 2011; Hoppins et al., 2011; von der Malsburg et al., 2011). The MICOS complex of metazoa additionally contains Mic25, which is related to Mic19, yet subunits corresponding to Mic12 and Mic26 have not been identified so far. MICOS subunits that have been conserved in most organisms analyzed are indicated by bold boundary lines. (B, top) Wild-type architecture of the mitochondrial inner membrane with crista junctions and cristae. (bottom) This architecture is considerably altered in micos mutant mitochondria: most cristae membranes are detached from the inner boundary membrane and form internal membrane stacks. In some micos mutants (deficiency of mammalian Mic19 or Mic25), a loss of cristae membranes was observed (Darshi et al., 2011; An et al., 2012). Figure by M. Bohnert (Institute of Biochemistry and Molecular Biology, University of Freiburg, Freiburg, Germany).To understand the complex architecture of mitochondria, it will be crucial to identify the molecular machineries that control the interaction between mitochondrial outer and inner membranes and the characteristic organization of the inner membrane. A convergence of independent studies led to the identification of a large heterooligomeric protein complex of the mitochondrial inner membrane conserved from yeast to humans that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane (Fig. 1 A). Several names were used by different research groups to describe the complex, including mitochondrial contact site (MICOS) complex, mitochondrial inner membrane organizing system (MINOS), mitochondrial organizing structure (MitOS), Mitofilin complex, or Fcj1 (formation of crista junction protein 1) complex (Harner et al., 2011; Hoppins et al., 2011; von der Malsburg et al., 2011; Alkhaja et al., 2012). Mitofilin, also termed Fcj1, was the first component identified (Icho et al., 1994; Odgren et al., 1996; Gieffers et al., 1997; John et al., 2005) and was observed enriched at crista junctions (Rabl et al., 2009). Mutants of Mitofilin/Fcj1 as well as of other MICOS/MINOS/MitOS subunits show a strikingly altered inner membrane architecture. They lose crista junctions and contain large internal membrane stacks, the respiratory activity is reduced, and mitochondrial DNA nucleoids are altered (Fig. 1 B; John et al., 2005; Hess et al., 2009; Rabl et al., 2009; Mun et al., 2010; Harner et al., 2011; Head et al., 2011; Hoppins et al., 2011; von der Malsburg et al., 2011; Alkhaja et al., 2012; Itoh et al., 2013). It has been reported that the complex interacts with a variety of outer membrane proteins, such as channel proteins and components of the protein translocases and mitochondrial fusion machines, and defects impair the biogenesis of mitochondrial proteins (Xie et al., 2007; Darshi et al., 2011; Harner et al., 2011; Hoppins et al., 2011; von der Malsburg et al., 2011; Alkhaja et al., 2012; An et al., 2012; Bohnert et al., 2012; Körner et al., 2012; Ott et al., 2012; Zerbes et al., 2012; Jans et al., 2013; Weber et al., 2013). The MICOS/MINOS/MitOS/Mitofilin/Fcj1 complex thus plays crucial roles in mitochondrial architecture, dynamics, and biogenesis. However, communication of results in this rapidly developing field has been complicated by several different nomenclatures used for the complex as well as for its subunits (Standard name Former names Yeast ORF References Complex MICOS MINOS, MitOS, MIB, Mitofilin complex, and Fcj1 complex Xie et al., 2007; Rabl et al., 2009; Darshi et al., 2011; Harner et al., 2011; Hoppins et al., 2011; von der Malsburg et al., 2011; Alkhaja et al., 2012; An et al., 2012; Bohnert et al., 2012; Ott et al., 2012; Jans et al., 2013; Weber et al., 2013 Subunits Mic10 Mcs10, Mio10, Mos1, and MINOS1 YCL057C-A Harner et al., 2011; Hoppins et al., 2011; von der Malsburg et al., 2011; Alkhaja et al., 2012; Itoh et al., 2013; Jans et al., 2013; Varabyova et al., 2013 Mic12 Aim5, Fmp51, and Mcs12 YBR262C Hess et al., 2009; Harner et al., 2011; Hoppins et al., 2011; von der Malsburg et al., 2011; Varabyova et al., 2013 Mic19 Aim13, Mcs19, CHCH-3, CHCHD3, and MINOS3 YFR011C Xie et al., 2007; Hess et al., 2009; Darshi et al., 2011; Head et al., 2011; Alkhaja et al., 2012; Ott et al., 2012; Jans et al., 2013; Varabyova et al., 2013 Mic25 (metazoan Mic19 homologue) CHCHD6 and CHCM1 Xie et al., 2007; An et al., 2012 Mic26 Mcs29, Mio27, and Mos2 YGR235C Harner et al., 2011; Hoppins et al., 2011; von der Malsburg et al., 2011 Mic27 Aim37, Mcs27, APOOL, and MOMA-1 YNL100W Hess et al., 2009; Harner et al., 2011; Head et al., 2011; Hoppins et al., 2011; von der Malsburg et al., 2011; Weber et al., 2013 Mic60 Fcj1, Aim28, Fmp13, Mitofilin, HMP, IMMT, and MINOS2 YKR016W Icho et al., 1994; Odgren et al., 1996; Gieffers et al., 1997; John et al., 2005; Wang et al., 2008; Rabl et al., 2009; Rossi et al., 2009; Mun et al., 2010; Park et al., 2010; Körner et al., 2012; Zerbes et al., 2012; Itoh et al., 2013; Varabyova et al., 2013