scholarly journals Cellular Compartment Analysis

2020 ◽  
Author(s):  
Keyword(s):  
Compartment Analysis ◽  
Cellular Compartment

scholarly journals Cellular compartment analysis of temporal activity by fluorescent in situ hybridization (catFISH) in the transcardially perfused rat brain

2019 ◽  
Author(s):  
Ali Gheidi ◽  
Vivek Kumar ◽  
Christopher J Fitzpatrick ◽  
Rachel L Atkinson ◽  
Jonathan D Morrow
Keyword(s):  
Mammalian Brain ◽  
Compartment Analysis ◽  
Spatiotemporal Resolution ◽  
Adult Rats ◽  
Cellular Compartment ◽  
Study Gene Expression ◽  
Resolution Mapping ◽  
External Stimuli ◽  
The Brain

AbstractCellular compartment analysis of temporal activity by fluorescent in situ hybridization (catFISH) allows high spatiotemporal resolution mapping of immediate early genes in the brain in response to internal/external stimuli. One caveat of this technique and indeed other methods of in situ hybridization is the necessity of flash-freezing the brain prior to staining. Often however, the mammalian brain is transcardially perfused to use the brain tissue for immunohistochemistry, the most widely-used technique to study gene expression. The present study illustrates how the original catFISH protocol can be modified for use in adult rats that have been transcardially perfused with 4% paraformaldehyde. c-Fos activity induced by either an auditory tone or status epilepticus was visualized using the catFISH procedure. Analysis of the rat prefrontal cortex, hippocampus and amygdala shows that a clear distinction can be made between the compartmental distribution of c-Fos mRNA in the nuclei and cytoplasmic regions. Furthermore, the qualitative proportion of c-Fos compartmentalization is similar to previous reports of c-Fos expression pattern in rodents navigating novel environments. c-Fos catFISH on perfused rodent brains is an valuable addition to the traditional histological methods using fluorescently labeled riboprobes, and opens several avenues for future investigations.

Shaping and Cellular Uptake of Folic Acid Coated Gold and Magnetite Nanoparticles

2019 ◽  
Vol 9 (2) ◽  
pp. 166-172
Author(s):  
Ahmed A.G. El-Shahawy ◽  
Gamal Elghnam ◽  
Alsayed A.M. Alsherbini
Keyword(s):  
Folic Acid ◽  
Iron Oxide ◽  
Tumor Cells ◽  
Iron Oxide Nanoparticles ◽  
Individual Cell ◽  
Oxide Nanoparticles ◽  
Cellular Compartment ◽  
Specific Tumor ◽  
Uv Visible

Background:Gold and Iron Oxide nanoparticles NPs play as nanocarriers for a specific drug delivery and contrast agents. Intercellular uptake of these nanoparticles and targeting to individual cell and sub-cellular compartment is essential.Objective:The aim of the current study is to evaluate the intracellular uptake of these NPs to specific tumor cells in vitro conjugated with folic acid with a goal of enhancing the efficiency of specific targeting to tumor cells.Methods:We synthesized the nanoparticles by a chemical method and characterized by UV-Visible, FTIR, XRD, and TEM.Results & Conclusion:The results revealed the conjugation of Gold and Iron Oxide nanoparticles with folic acid increased the intercellular uptake with high percent compared to non- conjugated nanoparticles.

scholarly journals The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment.

1989 ◽  
Vol 109 (6) ◽  
pp. 3493-3501 ◽  
Author(s):  
H Ertl ◽  
R Mengele ◽  
S Wenzl ◽  
J Engel ◽  
M Sumper
Keyword(s):  
Extracellular Matrix ◽  
Chemical Structure ◽  
Chemical Nature ◽  
Sulfated Polysaccharide ◽  
Surface Glycoprotein ◽  
Amino Acid Residues ◽  
Volvox Carteri ◽  
Cellular Compartment ◽  
Cross Links ◽  
Cellular Compartments

The extracellular matrix (ECM) of Volvox contains insoluble fibrous layers that surround individual cells at a distance to form contiguous cellular compartments. Using immunological techniques, we identified a sulfated surface glycoprotein (SSG 185) as the monomeric precursor of this substructure within the ECM. The primary structure of the SSG 185 poly-peptide chain has been derived from cDNA and genomic DNA. A central domain of the protein, 80 amino acid residues long, consists almost exclusively of hydroxyproline residues. The chemical structure of the highly sulfated polysaccharide covalently attached to SSG 185 has been determined by permethylation analysis. As revealed by EM, SSG 185 is a rod-shaped molecule with a 21-nm-long polysaccharide strand protruding from its central region. The chemical nature of the cross-links between SSG 185 monomers is discussed.

scholarly journals A novel calcium-concentrating compartment drives biofilm formation and persistent infections

2020 ◽  
Author(s):  
Alona Keren-Paz ◽  
Malena Cohen-Cymberknoh ◽  
Dror Kolodkin-Gal ◽  
Iris Karunker ◽  
Simon Dersch ◽  
...  
Keyword(s):  
Biofilm Formation ◽  
Calcium Uptake ◽  
Molecular Mechanisms ◽  
Model Organism ◽  
Bacterial Cells ◽  
Mineral Layer ◽  
Cellular Compartment ◽  
Persistent Infections ◽  
Cellular Metal

AbstractBacterial biofilms produce a robust internal mineral layer, composed of calcite, which strengthens the colony and protects the residing bacteria from antibiotics. In this work, we provide evidence that the assembly of a functional mineralized macro-structure begins with mineral precipitation within a defined cellular compartment in a differentiated subpopulation of cells. Transcriptomic analysis of a model organism, Bacillus subtilis, revealed that calcium was essential for activation of the biofilm state, and highlighted the role of cellular metal homeostasis and carbon metabolism in biomineralization. The molecular mechanisms promoting calcite formation were conserved in pathogenic Pseudomonas aeruginosa biofilms, resulting in formation of calcite crystals tightly associated with bacterial cells in sputum samples collected from cystic fibrosis patients. Biomineralization inhibitors targeting calcium uptake and carbonate accumulation significantly reduced the damage inflicted by P. aeruginosa biofilms to lung tissues. Therefore, better understanding of the conserved molecular mechanisms promoting biofilm calcification can path the way to the development of novel classes of antibiotics to combat otherwise untreatable biofilm infections.

scholarly journals WDR31 is a novel ciliopathy protein displaying functional redundancy with GTPase-activating proteins ELMOD and RP2 in recruiting BBSome to cilium

2021 ◽  
Author(s):  
Sebiha Cevik ◽  
Lama Alabdi ◽  
Xiaoyu Peng ◽  
Tina Beyer ◽  
Atiyye Zorluer ◽  
...  
Keyword(s):  
Clinical Features ◽  
Renal Agenesis ◽  
Rare Disorders ◽  
Compartment Analysis ◽  
C Elegans ◽  
Gtpase Activating Proteins ◽  
Mechanistic Analysis ◽  
Evolutionarily Conserved ◽  
Null Mutants

Abstract The term “ciliopathy” refers to a group of over 35 rare disorders characterized by defective cilia and many overlapping clinical features, such as hydrocephalus, cerebellar vermis hypoplasia, polydactyly, and retinopathy. Even though many genes have been implicated in ciliopathies, the genetic pathogenesis in certain cases remains still undisclosed. Here, we identified a homozygous truncating variant in WDR31 in a patient with a typical ciliopathy phenotype encompassing congenital hydrocephalus, polydactyly, and renal agenesis. WDR31 is an evolutionarily conserved protein that localizes to the cilium and cilia-related compartment. Analysis from zebrafish supports the role of WDR31 in regulating the cilia morphology. The CRISPR/Cas9 knock-in (p.Arg261del) C. elegans model of the patient variant (p.Arg268*) reproduced several cilia-related defects observed in wdr-31 null mutants. Mechanistic analysis from C. elegans revealed that WDR-31 functions redundantly with ELDM-1 (ELMOD protein) and RPI-2 (RP2) to regulate the IFT trafficking through controlling the cilia entry of the BBSome. This work revealed WDR31 as a new ciliopathy protein that regulates IFT and BBSome trafficking.

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