Journal of cytology & histology最新文献

{"title":"Arsenic-induced Histological Alterations in Various Organs of Mice","authors":"A. S. Noman, S. Dilruba, N. C. Mohanto, Lutfur Rahman, Z. Khatun, W. Riad, A. Al Mamun, S. Alam, Sharmin Aktar, S. Chowdhury, Z. Saud, Z. Rahman, Khaled Hossain, A. Haque","doi":"10.4172/2157-7099.1000323","DOIUrl":"https://doi.org/10.4172/2157-7099.1000323","url":null,"abstract":"Deposition of arsenic in mice through groundwater is well documented but little is known about the histological changes of organs by the metalloid. Present study was designed to evaluate arsenic-induced histological alterations in kidney, liver, thoracic artery and brain of mice which are not well documented yet. Swiss albino male mice were divided into 2 groups and treated as follows: Group 1: control, 2: arsenic (sodium arsenite at 10 mg/kg b.w. orally for 8 wks). Group 2 showed marked degenerative changes in kidney, liver, thoracic artery, and brain whereas Group 1 did not reveal any abnormalities on histopathology. We therefore concluded that arsenic induces histological alterations in the tested organs.","PeriodicalId":91112,"journal":{"name":"Journal of cytology & histology","volume":"6 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2015-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2157-7099.1000323","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70344291","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":"Fiber Composition of the Grasscutter (<i>Thryonomys swinderianus</i>, Temminck 1827) Thigh Muscle: An Enzyme-histochemical Study.","authors":"Serge Niangoran Bakou, Gualbert Simon Nteme Ella, Serge Aoussi, Lydie Guiguand, Yannick Cherel, Agathe Fantodji","doi":"10.4172/2157-7099.1000311","DOIUrl":"10.4172/2157-7099.1000311","url":null,"abstract":"<p><p>The aim of this study was to describe de fiber composition in the thigh muscles of grass cutter (<i>Thryonomys swinderianus</i>, Temminck 1827). Ten 4 to 6-month-old (3 to 4 kg) male grasscutter were used in this study. Eleven skeletal muscles of the thigh [M. biceps femoris (BF), M. rectus femoris (RF), M. vastus lateralis (VL), M. vastus medialis (VM), M. tensor fasciae latae (TFL), M. semitendinosus (ST), M. semimembranosus (SM), M. semimembranosus accessorius (SMA), M. Sartorius (SRT), M. pectineus (PCT), M. adductor magnus (AM)] were collected after animals euthanasia and examined by light microscopy. Three muscle fiber types (I, IIB and IIA) were found in these muscles using enzyme histochemical techniques [myosine adenosine triphosphatase (ATPase) and nicotinamide adenine dinucleotide tetrazolium reductase (NADH-TR)]. Ten of these eleven muscles are composed by 89% to 100% of fast contracting fibers (types IIA and IIB), while the SMA was almost exclusively formed by slow contracting fibers.</p>","PeriodicalId":91112,"journal":{"name":"Journal of cytology & histology","volume":"6 2","pages":"311"},"PeriodicalIF":0.0,"publicationDate":"2015-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4496929/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33898355","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":"Loss of Sarcomere-associated Formins Disrupts Z-line Organization, but does not Prevent Thin Filament Assembly in <i>Caenorhabditis elegans</i> Muscle.","authors":"Lei Mi-Mi,&nbsp;David Pruyne","doi":"10.4172/2157-7099.1000318","DOIUrl":"https://doi.org/10.4172/2157-7099.1000318","url":null,"abstract":"<p><p>Members of the formin family of actin filament nucleation factors have been implicated in sarcomere formation, but precisely how these proteins affect sarcomere structure remains poorly understood. Of six formins in the simple nematode <i>Caenorhabditis elegans</i>, only FHOD-1 and CYK-1 contribute to sarcomere assembly in the worm's obliquely striated body-wall muscles. We analyze here the ultrastructure of body-wall muscle sarcomeres in worms with putative null <i>fhod-1</i> and <i>cyk-1</i> gene mutations. Contrary to a simple model that formins nucleate actin for thin filament assembly, formin mutant sarcomeres contain thin filaments. Rather, formin mutant sarcomeres are narrower and have deformed thin filament-anchoring Z-line structures. Thus, formins affect multiple aspects of sarcomere structure.</p>","PeriodicalId":91112,"journal":{"name":"Journal of cytology & histology","volume":"6 2","pages":""},"PeriodicalIF":0.0,"publicationDate":"2015-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2157-7099.1000318","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33995299","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":"<i>In situ</i> Detection of MicroRNAs: The Art of MicroRNA Research in Human Diseases.","authors":"Duo Zhang,&nbsp;Lixin Xie,&nbsp;Yang Jin","doi":"10.4172/2157-7099.S3-013","DOIUrl":"https://doi.org/10.4172/2157-7099.S3-013","url":null,"abstract":"Duo Zhang1, Lixin Xie2 and Yang Jin1* 1Division of Pulmonary and Critical Care Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA, USA 02115 2Department of Respiratory Medicine, Chinese PLA General Hospital, 28th Fuxing Road, Beijing 100853, PR China *Corresponding author: Yang Jin, Division of Pulmonary and Critical Care, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, 75 Francis St., Boston, MA 02115, USA, Tel: 6177324334; E-mail: yjin@rics.bwh.harvard.edu","PeriodicalId":91112,"journal":{"name":"Journal of cytology & histology","volume":"Suppl 3 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2157-7099.S3-013","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35017328","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":"Single Cell Multiplex Protein Measurements through Rare Earth Element Immunolabeling, Laser Capture Microdissection and Inductively Coupled Mass Spectrometry.","authors":"Amir Liba,&nbsp;Jonathan Wanagat","doi":"10.4172/2157-7099.1000290","DOIUrl":"https://doi.org/10.4172/2157-7099.1000290","url":null,"abstract":"<p><p>Complex diseases such as heart disease, stroke, cancer, and aging are the primary causes of death in the US. These diseases cause heterogeneous conditions among cells, conditions that cannot be measured in tissue homogenates and require single cell approaches. Understanding protein levels within tissues is currently assayed using various molecular biology techniques (e.g., Western blots) that rely on milligram to gram quantities of tissue homogenates or immunofluorescent (IF) techniques that are limited by spectral overlap. Tissue homogenate studies lack references to tissue structure and mask signals from individual or rare cellular events. Novel techniques are required to bring protein measurement sensitivity to the single cell level and offer spatiotemporal resolution and scalability. We are developing a novel approach to protein quantification by exploiting the inherently low concentration of rare earth elements (REE) in biological systems. By coupling REE-antibody immunolabeling of cells with laser capture microdissection (LCM) and ICP-QQQ, we are achieving multiplexed protein measurement in histological sections of single cells. This approach will add to evolving single cell techniques and our ability to understand cellular heterogeneity in complex biological systems and diseases.</p>","PeriodicalId":91112,"journal":{"name":"Journal of cytology & histology","volume":"5 6","pages":""},"PeriodicalIF":0.0,"publicationDate":"2014-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2157-7099.1000290","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34594448","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":"Does Nebulin Make Tropomyosin Less Dynamic in Mature Myofibrils in Cross-Striated Myocytes?","authors":"D. Dube, J. Wang, Y. Fan, JM Sanger, JW Sanger","doi":"10.4172/2157-7099/1000239","DOIUrl":"https://doi.org/10.4172/2157-7099/1000239","url":null,"abstract":"Myofibrils in vertebrate cardiac and skeletal muscles are characterized by groups of proteins arranged in contractile units or sarcomeres, which consist of four major components – thin filaments, thick filaments, titin and Z-bands. The thin actin/tropomyosin-containing filaments are embedded in the Z-bands and interdigitate with the myosin-containing thick filaments aligned in A-bands. Titin is attached to the Z-band and extends upto the middle of the A-Band. In this mini review, we have addressed the mechanism of myofibril assembly as well as the dynamics and maintenance of the myofibrils in cardiac and skeletal muscle cells. Evidence from our research as well as from other laboratories favors the premyofibril model of myofibrillogenesis. This three-step model (premyofibril to nascent myofibril to mature myofibril) not only provides a reasonable mechanism for sequential interaction of various proteins during assembly of myofibrils, but also suggests why the dynamics of a thin filament protein like tropomyosin is higher in cardiac muscle than in skeletal muscles. The dynamics of tropomyosin not only varies in different muscle types (cardiac vs. skeletal), but also varies during myofibrillogenesis, for example, premyofibril versus mature myofibrils in skeletal muscle. One of the major differences in protein composition between cardiac and skeletal muscle is nebulin localized along the thin filaments (two nebulins/thin filament) of mature myofibrils in skeletal muscle cells, but which is expressed in a minimal quantity (one nebulin/50 actin filaments) in ventricular cardiomyocytes. Interestingly, nebulin is not associated with premyofibrils in skeletal muscle. Our FRAP(Fluorescence Recovery After Photobleaching) results suggest that tropomyosin is more dynamic in premyofibrils than in mature myofibrils in skeletal muscle, and also, the dynamics of tropomyosin in mature myofibrils is significantly higher in cardiac muscle compared to skeletal muscle. Our working hypothesis is that the association of nebulin in mature myofibrils renders tropomyosin less dynamic in skeletal muscle.","PeriodicalId":91112,"journal":{"name":"Journal of cytology & histology","volume":"5 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2014-04-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2157-7099/1000239","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70344500","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}