scholarly journals A localized molecular automaton for in situ visualization of proteins with specific chemical modifications

2020 ◽  
Vol 11 (6) ◽  
pp. 1665-1671
Author(s):  
Lu Liu ◽  
Siqiao Li ◽  
Anwen Mao ◽  
Guyu Wang ◽  
Yiran Liu ◽  
...  
Keyword(s):  
Cell Surface ◽  
Specific Protein ◽  
Chemical Modifications ◽  
Specific Chemical ◽  
Propagation Algorithm ◽  
In Situ Visualization

A localized DNA automaton is reported for in situ visualization of a specific protein subtype with dual chemical modifications on the cell surface, which executes protein-confined computation according to an anticoding–coding propagation algorithm.

The cell surface of Propionibacterium acnes: effect of specific chemical modifications on the ability of vaccines to produce splenomegaly in mice

1982 ◽  
Vol 28 (4) ◽  
pp. 375-382 ◽  
Author(s):  
Alastair T. Pringle ◽  
Cecil S. Cummins
Keyword(s):  
Cell Surface ◽  
Propionibacterium Acnes ◽  
Reticuloendothelial System ◽  
Chemical Modifications ◽  
Specific Chemical ◽  
Sodium Metaperiodate ◽  
Chemical Treatments ◽  
Strong Acids ◽  
Ionizable Groups ◽  
Phosphate Groups

The surface of Propionibacterium acnes, VPI 0009, was studied using microelectrophoresis following chemical treatments intended to modify specific charged groups. The effect of these specific chemical modifications on ability of cells to induce splenomegaly, an indicator of stimulation of the reticuloendothelial system, was also determined. There was little difference between pH mobility curves of P. acnes VPI 0009 and other strains of propionibacteria which were not able to stimulate the reticuloendothelial system. Amino and carboxyl groups were found to be the sole ionizable groups at the cell surface and modification of these groups caused a substantial decrease in the ability of cells to stimulate the reticuloendothelial system. No phosphate groups were detected. Evidence for two types of amino groups was found: one type was present on protein moieties and their modification did not affect ability to stimulate the reticuloendothelial system, whereas modification of the other type, which was present on carbohydrate moieties, caused a loss of ability to stimulate the reticuloendothelial system. Mild oxidation with sodium metaperiodate caused abolition of reticuloendothelial system stimulation, but had no effect on surface charged groups, indicating it was acting on the unsubstituted linkages of sugar residues. Treatments with strong acids caused abolition of ability to stimulate the reticuloendothelial system and this was accompanied by release of polysaccharide material.

scholarly journals Identification of potential autoantigens in anti-CCP-positive and anti-CCP-negative rheumatoid arthritis using citrulline-specific protein arrays

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Thomas B. G. Poulsen ◽  
Dres Damgaard ◽  
Malene M. Jørgensen ◽  
Ladislav Senolt ◽  
Jonathan M. Blackburn ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Protein Microarray ◽  
Specific Protein ◽  
Immune Reactivity ◽  
Igg Antibodies ◽  
Native Proteins ◽  
Array Technology ◽  
Citrullinated Proteins ◽  
Folded Proteins

AbstractThe presence or absence of autoantibodies against citrullinated proteins (ACPAs) distinguishes two main groups of rheumatoid arthritis (RA) patients with different etiologies, prognoses, disease severities, and, presumably, disease pathogenesis. The heterogeneous responses of RA patients to various biologics, even among ACPA-positive patients, emphasize the need for further stratification of the patients. We used high-density protein array technology for fingerprinting of ACPA reactivity. Identification of the proteome recognized by ACPAs may be a step to stratify RA patients according to immune reactivity. Pooled plasma samples from 10 anti-CCP-negative and 15 anti-CCP-positive RA patients were assessed for ACPA content using a modified protein microarray containing 1631 different natively folded proteins citrullinated in situ by protein arginine deiminases (PADs) 2 and PAD4. IgG antibodies from anti-CCP-positive RA plasma showed high-intensity binding to 87 proteins citrullinated by PAD2 and 99 proteins citrullinated by PAD4 without binding significantly to the corresponding native proteins. Curiously, the binding of IgG antibodies in anti-CCP-negative plasma was also enhanced by PAD2- and PAD4-mediated citrullination of 29 and 26 proteins, respectively. For only four proteins, significantly more ACPA binding occurred after citrullination with PAD2 compared to citrullination with PAD4, while the opposite was true for one protein. We demonstrate that PAD2 and PAD4 are equally efficient in generating citrullinated autoantigens recognized by ACPAs. Patterns of proteins recognized by ACPAs may serve as a future diagnostic tool for further subtyping of RA patients.

scholarly journals Trace Amine-Associated Receptor 1 Trafficking to Cilia of Thyroid Epithelial Cells

Cells ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1518
Author(s):  
Maria Qatato ◽  
Vaishnavi Venugopalan ◽  
Alaa Al-Hashimi ◽  
Maren Rehders ◽  
Aaron D. Valentine ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Lines ◽  
Human Thyroid ◽  
Apical Plasma Membrane ◽  
Thyroid Cell ◽  
Thyroid Cells ◽  
Trace Amine ◽  
Rat Thyroid

Trace amine-associated receptor 1 (rodent Taar1/human TAAR1) is a G protein-coupled receptor that is mainly recognized for its functions in neuromodulation. Previous in vitro studies suggested that Taar1 may signal from intracellular compartments. However, we have shown Taar1 to localize apically and on ciliary extensions in rodent thyrocytes, suggesting that at least in the thyroid, Taar1 may signal from the cilia at the apical plasma membrane domain of thyrocytes in situ, where it is exposed to the content of the follicle lumen containing putative Taar1 ligands. This study was designed to explore mouse Taar1 (mTaar1) trafficking, heterologously expressed in human and rat thyroid cell lines in order to establish an in vitro system in which Taar1 signaling from the cell surface can be studied in future. The results showed that chimeric mTaar1-EGFP traffics to the apical cell surface and localizes particularly to spherical structures of polarized thyroid cells, procilia, and primary cilia upon serum-starvation. Moreover, mTaar1-EGFP appears to form high molecular mass forms, possibly homodimers and tetramers, in stably expressing human thyroid cell lines. However, only monomeric mTaar1-EGFP was cell surface biotinylated in polarized human thyrocytes. In polarized rat thyrocytes, mTaar1-EGFP is retained in the endoplasmic reticulum, while cilia were reached by mTaar1-EGFP transiently co-expressed in combination with an HA-tagged construct of the related mTaar5. We conclude that Taar1 trafficking to cilia depends on their integrity. The results further suggest that an in vitro cell model was established that recapitulates Taar1 trafficking in thyrocytes in situ, in principle, and will enable studying Taar1 signaling in future, thus extending our general understanding of its potential significance for thyroid autoregulation.

In-situ visualization of polypropylene crystallization during extrusion

2014 ◽  
Vol 33 ◽  
pp. 57-63 ◽  
Author(s):  
Alireza Tabatabaei ◽  
M. Reza Barzegari ◽  
Mohammadreza Nofar ◽  
Chul B. Park
Keyword(s):  
In Situ Visualization

In situ visualization of zinc plating in gel polymer electrolyte

2021 ◽  
pp. 138877
Author(s):  
Yuju Jeon ◽  
Yutong Wu ◽  
Yamin Zhang ◽  
Chihyun Hwang ◽  
Hyun-Wook Lee ◽  
...  
Keyword(s):  
Polymer Electrolyte ◽  
Gel Polymer Electrolyte ◽  
Zinc Plating ◽  
In Situ Visualization
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