Characterization of canine epidermal organoid cultures by immunohistochemical analysis and quantitative PCR

2020 ◽  
Author(s):  
Dominique J. Wiener ◽  
Isabelle C. Studer ◽  
Magdalena A.T. Brunner ◽  
Andreas Hermann ◽  
Simona Vincenti ◽  
...  
Keyword(s):  
Quantitative Pcr ◽  
Immunohistochemical Analysis ◽  
Organoid Cultures

scholarly journals Characterization of Neutralizing Epitopes of Varicella-Zoster Virus Glycoprotein H

2008 ◽  
Vol 83 (4) ◽  
pp. 2020-2024 ◽  
Author(s):  
Yasushi Akahori ◽  
Kazuhiro Suzuki ◽  
Tohru Daikoku ◽  
Masae Iwai ◽  
Yoshihiro Yoshida ◽  
...  
Keyword(s):  
Varicella Zoster Virus ◽  
Immunohistochemical Analysis ◽  
Human Monoclonal Antibodies ◽  
Varicella Zoster ◽  
Glycoprotein H ◽  
Spread Of Infection ◽  
Cell Spread ◽  
Independent Protein ◽  
Neutralizing Epitopes

ABSTRACT Varicella-zoster virus (VZV) glycoprotein H (gH) is the major neutralization target of VZV, and its neutralizing epitope is conformational. Ten neutralizing human monoclonal antibodies to gH were used to map the epitopes by immunohistochemical analysis and were categorized into seven epitope groups. The combinational neutralization efficacy of two epitope groups was not synergistic. Each epitope was partially or completely resistant to concanavalin A blocking of the glycomoiety of gH, and their antibodies inhibited the cell-to-cell spread of infection. The neutralization epitope comprised at least seven independent protein portions of gH that served as the target to inhibit cell-to-cell spread.

scholarly journals Prenatal Detection by Real-Time Quantitative PCR and Characterization of a New CFTR Deletion, 3600+15kbdel5.3kb (or CFTRdele19)

2000 ◽  
Vol 46 (9) ◽  
pp. 1417-1420 ◽  
Author(s):  
Bruno Costes ◽  
Emmanuelle Girodon ◽  
Dominique Vidaud ◽  
Elisabeth Flori ◽  
Azarnouche Ardalan ◽  
...  
Keyword(s):  
Real Time ◽  
Quantitative Pcr ◽  
Real Time Quantitative Pcr ◽  
Prenatal Detection

scholarly journals Development and characterization of salivary gland cancer organoid cultures

2019 ◽  
Vol 30 ◽  
pp. v472-v473
Author(s):  
W.V. Boxtel ◽  
T.M.W. Aalders ◽  
G. Lassche ◽  
I.C.H. van Engen - van Grunsven ◽  
G.W. Verhaegh ◽  
...  
Keyword(s):  
Salivary Gland ◽  
Salivary Gland Cancer ◽  
Organoid Cultures

Characterization of an antibody panel for immunohistochemical analysis of canine muscle cells

2008 ◽  
Vol 125 (3-4) ◽  
pp. 225-233 ◽  
Author(s):  
Stéphanie Gofflot ◽  
Philippe Kischel ◽  
Caroline Thielen ◽  
Vincent Radermacher ◽  
Jacques Boniver ◽  
...  
Keyword(s):  
Immunohistochemical Analysis ◽  
Muscle Cells ◽  
Antibody Panel

scholarly journals A Histopathological and Immunohistochemical Analysis of Ameloblastic Fibrodentinoma

2013 ◽  
Vol 2013 ◽  
pp. 1-7
Author(s):  
Ronell Bologna-Molina ◽  
Sirced Salazar-Rodríguez ◽  
Ana María Bedoya-Borella ◽  
Ramón Gil Carreón-Burciaga ◽  
Gabriel Tapia-Repetto ◽  
...  
Keyword(s):  
Histone H3 ◽  
Immunohistochemical Analysis ◽  
Odontogenic Tumor ◽  
Rare Entity ◽  
Ki 67 ◽  
Dental Papilla ◽  
Odontogenic Epithelium ◽  
Ameloblastic Fibroma ◽  
Large Panel

Ameloblastic fibrodentinoma (AFD) is considered a mixed odontogenic tumor that is characterized by conserved epithelial and ectomesenchymal neoplastic components. AFD is composed of long narrow cords and islands of odontogenic epithelium; the epithelial strands lie in a myxoid cell-rich ectomesenchymal tissue with stellate-shaped fibroblasts that exhibit long slender cytoplasmic extensions that resemble dental papilla. The lesions show the presence of dysplastic dentin. Although AFD is a rare entity and its very existence is not completely accepted, based on the extent of histodifferentiation, it is considered to represent a stage between ameloblastic fibroma and ameloblastic fibroodontoma. This study aimed to provide a histopathological and immunohistochemical characterization of this infrequent tumor. A large panel of antibodies including amelogenin, Ck 19, calretinin, syndecan-1, E-cadherin, MSH2, histone H3, and Ki-67 was used to illustrate the nature of the tumor.

Characterization of hepatic-organoid cultures

2009 ◽  
Vol 42 (3) ◽  
pp. 472-481 ◽  
Author(s):  
Toshihiro Mitaka ◽  
Hidekazu Ooe
Keyword(s):  
Organoid Cultures

Preparation and Characterization of Monoclonal Antibodies Specific for Lauroylated Isoform of Bovine Transducin α-Subunit: Immunohistochemical Analysis of Bovine Retinas

2002 ◽  
Vol 66 (5) ◽  
pp. 2188-2196 ◽  
Author(s):  
Osamu Shouno ◽  
Koichi Kokame ◽  
Masasuke Araki ◽  
Toshifumi Takao ◽  
Yasutsugu Shimonishi ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Immunohistochemical Analysis ◽  
Α Subunit

scholarly journals Characterization of the Gut Microbiota of Papua New Guineans Using Reverse Transcription Quantitative PCR

PLoS ONE ◽  
2015 ◽  
Vol 10 (2) ◽  
pp. e0117427 ◽  
Author(s):  
Andrew R. Greenhill ◽  
Hirokazu Tsuji ◽  
Kiyohito Ogata ◽  
Kazumi Natsuhara ◽  
Ayako Morita ◽  
...  
Keyword(s):  
Gut Microbiota ◽  
Quantitative Pcr ◽  
Reverse Transcription ◽  
Reverse Transcription Quantitative Pcr

αT-Catenin: a novel tissue-specific β-catenin-binding protein mediating strong cell-cell adhesion

2001 ◽  
Vol 114 (17) ◽  
pp. 3177-3188 ◽  
Author(s):  
Barbara Janssens ◽  
Steven Goossens ◽  
Katrien Staes ◽  
Barbara Gilbert ◽  
Jolanda van Hengel ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Immunohistochemical Analysis ◽  
Cell Types ◽  
Resistant Cell ◽  
Colon Carcinoma Cells ◽  
Intercalated Discs ◽  
Different Cell Types ◽  
Cell Adhesion Proteins ◽  
Cell Cell

Cadherins are major cell-cell adhesion proteins whose cytoplasmic domains bind to catenin proteins. Strong intercellular adhesion depends on linkage of the cadherin/catenin complex to the actin cytoskeleton via α-catenin. To date, it is not clear how different cell types achieve the variable strength of cell-cell adhesion clearly needed in a multicellular organism. Here, we report the cloning and molecular characterization of αT(testis)-catenin, a novel human cDNA encoding a protein with homology to both human αE(epithelial)-catenin and αN(neural)-catenin. Although originally discovered in testis, αT-catenin is expressed in other tissues, the highest levels being observed in heart. Immunohistochemical analysis showed human αT-catenin localization at intercalated discs of cardiomyocytes and in peritubular myoid cells of testis. In cells transfected with αT-catenin cDNA, interaction with β-catenin was demonstrated by co-immunoprecipitation. Transfection of α-catenin-deficient colon carcinoma cells recruited E-cadherin and β-catenin to cell-cell contacts and functional cadherin-mediated cell-cell adhesion was restored in this way. Moreover, compaction of these cells was at least as prominent as in the case of cells expressing endogenous αE-catenin. We propose that αT-catenin is necessary for the formation of stretch-resistant cell-cell adhesion complexes, in particular, muscle cells.

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