International Review of Cytology-A Survey of Cell Biology最新文献

{"title":"New insights into fatty acid modulation of pancreatic beta-cell function.","authors":"Esther P Haber,&nbsp;Joaquim Procópio,&nbsp;Carla R O Carvalho,&nbsp;Angelo R Carpinelli,&nbsp;Philip Newsholme,&nbsp;Rui Curi","doi":"10.1016/S0074-7696(06)48001-3","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)48001-3","url":null,"abstract":"<p><p>Insulin resistance states as found in type 2 diabetes and obesity are frequently associated with hyperlipidemia. Both stimulatory and detrimental effects of free fatty acids (FFA) on pancreatic beta cells have long been recognized. Acute exposure of the pancreatic beta cell to both high glucose concentrations and saturated FFA results in a substantial increase of insulin release, whereas a chronic exposure results in desensitization and suppression of secretion. Reduction of plasma FFA levels in fasted rats or humans severely impairs glucose-induced insulin release but palmitate can augment insulin release in the presence of nonstimulatory concentrations of glucose. These results imply that changes in physiological plasma levels of FFA are important for regulation of beta-cell function. Although it is widely accepted that fatty acid (FA) metabolism (notably FA synthesis and/or formation of LC-acyl-CoA) is necessary for stimulation of insulin secretion, the key regulatory molecular mechanisms controlling the interplay between glucose and fatty acid metabolism and thus insulin secretion are not well understood but are now described in detail in this review. Indeed the correct control of switching between FA synthesis or oxidation may have critical implications for beta-cell function and integrity both in vivo and in vitro. LC-acyl-CoA (formed from either endogenously synthesized or exogenous FA) controls several aspects of beta-cell function including activation of certain types of PKC, modulation of ion channels, protein acylation, ceramide- and/or NO-mediated apoptosis, and binding to and activating nuclear transcriptional factors. The present review also describes the possible effects of FAs on insulin signaling. We have previously reported that acute exposure of islets to palmitate up-regulates some key components of the intracellular insulin signaling pathway in pancreatic islets. Another aspect considered in this review is the potential source of fatty acids for pancreatic islets in addition to supply in the blood. Lipids can be transferred from leukocytes (macrophages) to pancreatic islets in coculture. This latter process may provide an additional source of FAs that may play a significant role in the regulation of insulin secretion.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"248 ","pages":"1-41"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)48001-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25863832","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":"Endogenous ligands of PACAP/VIP receptors in the autocrine-paracrine regulation of the adrenal gland.","authors":"Maria Teresa Conconi,&nbsp;Raffaella Spinazzi,&nbsp;Gastone G Nussdorfer","doi":"10.1016/S0074-7696(06)49001-X","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)49001-X","url":null,"abstract":"<p><p>Vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (PACAP) are the main endogenous ligands of a class of G protein-coupled receptors (Rs). Three subtypes of PACAP/VIP Rs have been identified and named PAC(1)-Rs, VPAC(1)-Rs, and VPAC(2)-Rs. The PAC(1)-R almost exclusively binds PACAP, while the other two subtypes bind with about equal efficiency VIP and PACAP. VIP, PACAP, and their receptors are widely distributed in the body tissues, including the adrenal gland. VIP and PACAP are synthesized in adrenomedullary chromaffin cells, and are released in the adrenal cortex and medulla by VIPergic and PACAPergic nerve fibers. PAC(1)-Rs are almost exclusively present in the adrenal medulla, while VPAC(1)-Rs and VPAC(2)-Rs are expressed in both the adrenal cortex and medulla. Evidence indicates that VIP and PACAP, acting via VPAC(1)-Rs and VPAC(2)-Rs coupled to adenylate cyclase (AC)- and phospholipase C (PLC)-dependent cascades, stimulate aldosterone secretion from zona glomerulosa (ZG) cells. There is also proof that they can also enhance aldosterone secretion indirectly, by eliciting the release from medullary chromaffin cells of catecholamines and adrenocorticotropic hormone (ACTH), which in turn may act on the cortical cells in a paracrine manner. The involvement of VIP and PACAP in the regulation of glucocorticoid secretion from inner adrenocortical cells is doubtful and surely of minor relevance. VIP and PACAP stimulate the synthesis and release of adrenomedullary catecholamines, and all three subtypes of PACAP/VIP Rs mediate this effect, PAC(1)-Rs being coupled to AC, VPAC(1)-Rs to both AC and PLC, and VPAC(2)-Rs only to PLC. A privotal role in the catecholamine secretagogue action of VIP and PACAP is played by Ca(2+). VIP and PACAP may also modulate the growth of the adrenal cortex and medulla. The concentrations attained by VIP and PACAP in the blood rule out the possibility that they act as true circulating hormones. Conversely, their adrenal content is consistent with a local autocrine-paracrine mechanism of action.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"249 ","pages":"1-51"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)49001-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26022786","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":"Current strategies in overcoming resistance of cancer cells to apoptosis melanoma as a model.","authors":"Peter Hersey,&nbsp;L Zhuang,&nbsp;X D Zhang","doi":"10.1016/S0074-7696(06)51004-6","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)51004-6","url":null,"abstract":"<p><p>Most anticancer agents mediate their effects through common pathways which induce apoptosis or in some cases necrosis of cancer cells. The apoptotic pathways are regulated by Bcl-2 family proteins, which include both pro- and anti-apoptotic members. Much is known about the interactions of these proteins involved in apoptosis and this information is being utilized in the development of new reagents that may be used to treat patients with cancers. The inhibitor of apoptosis family of proteins constitute a second group of proteins which inhibit the effector caspases. Reagents that inhibit their activity are also under development. Resistance of cancer cells to treatment can in many instances be attributed to activation of intracellular signal pathways involved in survival, such as the Ras-Raf-MEK-ERK1/2 or the P13K-Akt pathway. Again, much has been learned about the control of these pathways and their activation of resistance mechanisms. Inhibitors of such pathways are being evaluated in preclinical and clinical studies and are showing promise as a new class of anticancer agents. Much of the progress in future studies will likely depend on the ability to target these new treatments to particular subgroups of patients with tumor characteristics that make them responsive to the agents in question.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"251 ","pages":"131-58"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)51004-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26227329","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 human lacrimal gland and nasolacrimal duct mucins.","authors":"Friedrich Paulsen","doi":"10.1016/S0074-7696(06)49005-7","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)49005-7","url":null,"abstract":"<p><p>The old concept that the lacrimal gland is only a serous gland has been superseded by the finding that lacrimal acinar cells are able to produce mucins--high-molecular-weight proteins--the major mass being carbohydrates with the common feature of tandem repeats of amino acids rich in serine, threonine, and proline in the central domain of the mucin core peptide. At the ocular surface, maintenance of the tear film, lubrication, and provision of a pathogen barrier on the epithelia, conjunctiva, and cornea have been shown to be facilitated by mucins that are present in membrane-anchored (lining epithelial cells) or secreted (goblet cells) form. Also in the lacrimal gland, both membrane-anchored (MUCs 1, 4, and 16) and secreted (MUCs 5B and 7) mucins have been identified. The lacrimal gland is the main contributor to the aqueous portion of the tear film. It is part of the lacrimal apparatus that comprises, together with the lacrimal gland, the paired lacrimal canaliculi, the lacrimal sac, and the nasolacrimal duct, which collects the tear fluid and conveys it into the nasal cavity. In this review, the latest information regarding mucin function in the human lacrimal gland and the human efferent tear ducts is summarized with regard to mucous epithelia integrity, rheological and antimicrobial properties of the tear film and tear outflow, age-related changes, and certain disease states such as the pathogenesis of dry eye, dacryostenosis, and dacryolith formation.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"249 ","pages":"229-79"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)49005-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26019980","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":"Cellular and molecular biology of orphan G protein-coupled receptors.","authors":"Da Young Oh,&nbsp;Kyungjin Kim,&nbsp;Hyuk Bang Kwon,&nbsp;Jae Young Seong","doi":"10.1016/S0074-7696(06)52003-0","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)52003-0","url":null,"abstract":"<p><p>The superfamily of G protein-coupled receptors (GPCRs) is the largest and most diverse group of membrane-spanning proteins. It plays a variety of roles in pathophysiological processes by transmitting extracellular signals to cells via heterotrimeric G proteins. Completion of the human genome project revealed the presence of approximately 168 genes encoding established nonsensory GPCRs, as well as 207 genes predicted to encode novel GPCRs for which the natural ligands remained to be identified, the so-called orphan GPCRs. Eighty-six of these orphans have now been paired to novel or previously known molecules, and 121 remain to be deorphaned. A better understanding of the GPCR structures and classification; knowledge of the receptor activation mechanism, either dependent on or independent of an agonist; increased understanding of the control of GPCR-mediated signal transduction; and development of appropriate ligand screening systems may improve the probability of discovering novel ligands for the remaining orphan GPCRs.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"252 ","pages":"163-218"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)52003-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26260882","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":"Hsp70 chaperone as a survival factor in cell pathology.","authors":"Irina Guzhova,&nbsp;Boris Margulis","doi":"10.1016/S0074-7696(06)54003-3","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)54003-3","url":null,"abstract":"<p><p>Heat shock protein Hsp70 is implicated in the mechanism of cell reaction to a variety of cytotoxic factors. The protective function of Hsp70 is related to its ability to promote folding of nascent polypeptides and to remove denatured proteins. Many types of cancer cells contain high amounts of Hsp70, whose protective capacity may pose a problem for therapy in oncology. Hsp70 was shown to be expressed on the surface of cancer cells and to participate in the presentation of tumor antigens to immune cells. Therefore, the chaperone activity of Hsp70 is an important factor that should be taken into consideration in cancer therapy. The protective role of Hsp70 is also evident in neuropathology. Many neurodegenerative processes are associated with the accumulation of insoluble aggregates of misfolded proteins in neural cells. These aggregates hamper intracellular transport, inhibit metabolism, and activate apoptosis through diverse pathways. The increase of Hsp70 content results in the reduction of aggregate size and number and ultimately enhances cell viability.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"254 ","pages":"101-49"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)54003-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26425498","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":"Growth and division of peroxisomes.","authors":"Michael Schrader,&nbsp;H Dariush Fahimi","doi":"10.1016/S0074-7696(06)55005-3","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)55005-3","url":null,"abstract":"<p><p>Peroxisomes are ubiquitous subcellular organelles, which are highly dynamic and display large plasticity in response to cellular and environmental conditions. Novel proteins and pathways that mediate and control peroxisome formation, growth, and division continue to be discovered, and the cellular machineries that act together to regulate peroxisome number and size are under active investigation. Here, advances in the field of peroxisomal dynamics and proliferation in mammals and yeast are reviewed. The authors address the signals, conditions, and proteins that affect, regulate, and control the number and size of this essential organelle, especially the components involved in the division of peroxisomes. Special emphasis is on the function of dynamin-related proteins (DRPs), on Fis1, a putative adaptor for DRPs, on the role of the Pex11 family of peroxisomal membrane proteins, and the cytoskeleton.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"255 ","pages":"237-90"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)55005-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26508864","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":"Vomeronasal versus olfactory epithelium: is there a cellular basis for human vomeronasal perception?","authors":"Martin Witt,&nbsp;Thomas Hummel","doi":"10.1016/S0074-7696(06)48004-9","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)48004-9","url":null,"abstract":"<p><p>The vomeronasal organ (VNO) constitutes an accessory olfactory organ that receives chemical stimuli, pheromones, which elicit behavioral, reproductive, or neuroendocrine responses among individuals of the same species. In many macrosmatic animals, the morphological substrate constitutes a separate organ system consisting of a vomeronasal duct (ductus vomeronasalis, VND), equipped with chemosensory cells, and a vomeronasal nerve (nervus vomeronasalis, VNN) conducting information into the accessory olfactory bulb (AOB) in the central nervous system (CNS). Recent data require that the long-accepted dual functionality of a main olfactory system and the VNO be reexamined, since all species without a VNO are nevertheless sexually active, and species possessing a VNO also can sense other than \"vomeronasal\" stimuli via the vomeronasal epithelium (VNE). The human case constitutes a borderline situation, as its embryonic VNO anlage exerts a developmental track common to most macrosmatics, but later typical structures such as the VNN, AOB, and probably most of the chemoreceptor cells within the still existent VND are lost. This review also presents recent information on the VND including immunohistochemical expression of neuronal markers, intermediate filaments, lectins, integrins, caveolin, CD44, and aquaporins. Further, we will address the issue of human pheromone candidates.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"248 ","pages":"209-59"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)48004-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25863835","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":"Bacterial cell division: the mechanism and its precison.","authors":"Elizabeth Harry,&nbsp;Leigh Monahan,&nbsp;Lyndal Thompson","doi":"10.1016/S0074-7696(06)53002-5","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)53002-5","url":null,"abstract":"<p><p>The recent development of cell biology techniques for bacteria to allow visualization of fundamental processes in time and space, and their use in synchronous populations of cells, has resulted in a dramatic increase in our understanding of cell division and its regulation in these tiny cells. The first stage of cell division is the formation of a Z ring, composed of a polymerized tubulin-like protein, FtsZ, at the division site precisely at midcell. Several membrane-associated division proteins are then recruited to this ring to form a complex, the divisome, which causes invagination of the cell envelope layers to form a division septum. The Z ring marks the future division site, and the timing of assembly and positioning of this structure are important in determining where and when division will take place in the cell. Z ring assembly is controlled by many factors including negative regulatory mechanisms such as Min and nucleoid occlusion that influence Z ring positioning and FtsZ accessory proteins that bind to FtsZ directly and modulate its polymerization behavior. The replication status of the cell also influences the positioning of the Z ring, which may allow the tight coordination between DNA replication and cell division required to produce two identical newborn cells.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"253 ","pages":"27-94"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)53002-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26358133","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":"Roles of PACAP-containing retinal ganglion cells in circadian timing.","authors":"Jens Hannibal","doi":"10.1016/S0074-7696(06)51001-0","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)51001-0","url":null,"abstract":"<p><p>The brain's biological clock located in the suprachiasmatic nucleus (SCN) generates circadian rhythms in physiology and behavior. The clock-driven rhythms need daily adjustment (entrainment) to be synchronized with the astronomical day of 24 h. The most important stimulus for entrainment of the clock is the light-dark (LD) cycle. In this review functional elements of the light entrainment pathway will be considered with special focus on the neurotransmitter pituitary adenylate cyclase-activating polypeptide (PACAP), which is found exclusively in the monosynaptic neuronal pathway mediating light information to the SCN, the retinohypothalamic tract (RHT). The retinal ganglion cells of the RHT are intrinsically photosensitive due to the expression of melanopsin and seem to constitute a non-image forming photosensitive system in the mammalian eye regulating circadian timing, masking behavior, light-regulated melatonin secretion, and the pupillary light reflex. Evidence from in vitro and in vivo studies and studies of mice lacking PACAP and the specific PACAP receptor (PAC1) indicate that PACAP and glutamate are neurotransmitters in the RHT which in a clock and concentration-dependent manner interact during light entrainment of the clock.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"251 ","pages":"1-39"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)51001-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26227326","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}