Immunocytochemistry of Intermediate Filament Proteins Present in Pleomorphic Adenomas of the Human Parotid Gland: Characterization of Different Cell Types in the Same Tumor

Of all the significant researches that have taken place in isolation, culture and characterization of mesenchymal stem cells (MSCs), the field of kidney-derived mesenchymal stem cells (KMSCs) in Tibetan mastiff is still a blank. Therefore, the purpose of this study is to isolate, culture and characterize the Tibetan mastiff KMSCs. The KMSCs were successfully isolated from one-day year old Tibetan mastiff kidney, cultured for 16 passages and distinguished by two methods: immunofluorescence staining and RT-PCR. The Tibetan mastiff KMSCs expressed specific surface marker genes (VIM, CD44, FN1, CD90, CD109, CD73, FN1) and kidney marker gene PAX2. The proliferation ability of Tibetan mastiff KMSCs was measured through cell count and clonality. Furthermore, cells differentiated into different cell types (hepatocellular cells, osteogenic cells, adipogenic cells and chondrogenic cells) under special induced medium, and the marker genes of induced cells were identified with Immunofluorescence staining and RT-PCR. All of these results indicated that the Tibetan mastiff KMSCs were obtained successfully, which possessed certain characteristics of multipotent stem cells. Therefore, MSCs in Tibetan mastiff kidney hold potential for clinical applications for regenerative therapy and their further studies are waiting to be required to investigate their functions.

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Poster 32 Characterization of Novel Cell Lines from Pleomorphic Adenomas of the Parotid Gland Established in a Collagen Gel System

Otolaryngology ◽

10.1016/s0194-5998(05)80667-9 ◽

1995 ◽

Vol 113 (2) ◽

pp. P85-P85

Author(s):

William I. Kuhel ◽

Melissa G. Steiner ◽

John F. Carew ◽

Jerry Huo

Keyword(s):

Parotid Gland ◽

Cell Lines ◽

Collagen Gel ◽

Pleomorphic Adenomas ◽

Gel System

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

Journal of Cell Science ◽

10.1242/jcs.114.17.3177 ◽

2001 ◽

Vol 114 (17) ◽

pp. 3177-3188 ◽

Cited By ~ 1

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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Biochemical and immunological characterization of pea nuclear intermediate filament proteins

Planta ◽

10.1007/s00425-003-1182-5 ◽

2004 ◽

Vol 218 (6) ◽

pp. 965-975 ◽

Cited By ~ 29

Author(s):

Gregory B. Clark ◽

Stanley J. Roux ◽

Sonal S. D. Blumenthal

Keyword(s):

Intermediate Filament ◽

Intermediate Filament Proteins ◽

Immunological Characterization

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Cell penetrating peptides can exert biological activity: a review

BioMolecular Concepts ◽

10.1515/bmc.2010.016 ◽

2010 ◽

Vol 1 (2) ◽

pp. 109-116 ◽

Cited By ~ 11

Author(s):

Jamie Brugnano ◽

Brian C. Ward ◽

Alyssa Panitch

Keyword(s):

Gene Expression ◽

Biological Activity ◽

Cell Membrane ◽

Recent Literature ◽

Cell Types ◽

Cell Penetrating Peptides ◽

Cell Penetrating ◽

Different Cell Types ◽

Traditional Understanding

AbstractCell penetrating peptides (CPPs) have been successful in delivering cargo into many different cell types and are an important alternative to other methods of permeation that might damage the integrity of the cell membrane. The traditional view of CPPs is that they are inert molecules that can be successfully used to deliver many cargos intracellularly. The goal of this review is to challenge this traditional understanding of CPPs. Recent literature has demonstrated that CPPs themselves can convey biological activity, including the alteration of gene expression and inhibition of protein kinases and proteolytic activity. Further characterization of CPPs is required to determine the extent of this activity. Research into the use of CPPs for intracellular delivery should continue with investigators being aware of these recent results.

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Partial characterization of different cell types found in the Xenopuslaevis lymphoreticular tumor based on the presence or absence of surface immunoglobulins and Fc receptor molecules

Developmental & Comparative Immunology ◽

10.1016/0145-305x(86)90176-x ◽

1986 ◽

Vol 10 (4) ◽

pp. 547-559 ◽

Cited By ~ 3

Author(s):

Véronique Coosemans ◽

Irandokht Hadji-Azimi

Keyword(s):

Cell Types ◽

Fc Receptor ◽

Partial Characterization ◽

Surface Immunoglobulins ◽

Different Cell Types

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The characterization of an acidic calmodulin-binding protein in brain cytoskeleton and membrane fractions

Biochemical Journal ◽

10.1042/bj2400593 ◽

1986 ◽

Vol 240 (2) ◽

pp. 593-596

Author(s):

P Strocchi ◽

J M Gilbert

Keyword(s):

Intermediate Filament ◽

Gel Electrophoresis ◽

Binding Protein ◽

Two Dimensional ◽

Proteolytic Digestion ◽

Two Dimensional Gel Electrophoresis ◽

Intermediate Filament Proteins ◽

Calmodulin Binding ◽

Acidic Proteins

One of the most abundant acidic proteins in rat brain has an Mr of 68,000 and a pI of 5.6 (68K 5.6 protein) when analysed by two-dimensional gel electrophoresis. The 68K 5.6 protein was found in large relative amounts in brain cytoskeleton preparations and in membrane and supernatant fractions. High-salt washing and proteolytic digestion did not remove this protein from the membrane elements. The 68K 5.6 protein was also found in the microtubule-associated protein fraction of purified microtubules and was present in large relative amounts in preparations of intermediate-filament proteins. The 68K 5.6 protein binds to calmodulin in the presence of Ca2+ ions, and we found it to be an abundant acidic calmodulin-binding protein in brain tissue.

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