Influence of surface modification on vitality and differentiation of Caco-2 cells

Piana, Claudia; Güll, Iris; Gerbes, Stefan; Gerdes, Ralf; Mills, Christopher A.; Samitier, J.; Wirth, Michael; Gabor, Franz

doi:10.1111/j.1432-0436.2006.00141.x

Cited by 12 publications

(9 citation statements)

References 17 publications

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“…Primary chondrocytes of 2 donors were seeded into 96-well microplates (Iwaki, Japan) and cultured for 48 h. Then, cells were treated in quadruplet with 10 ng/ml IL-1β or 40 ng/ml TNF-α for 24 h. The total number of cells was determined using the CyQuant assay kit (Molecular Probes, USA) pursuing a modified protocol [30]. Moreover, the rate of proliferation of cells was assessed by incorporation of 2-bromodeoxyuridine into the DNA of dividing cells using the colorimetric BrdU assay (Roche, Germany), according to the manufacturer’s instructions.…”

Section: Methodsmentioning

confidence: 99%

Phenotype-related differential α-2,6- or α-2,3-sialylation of glycoprotein N-glycans in human chondrocytes

Toegel

Pabst

et al. 2010

Osteoarthritis and Cartilage

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Objective Sialic acids frequently occur at the terminal positions of glycoprotein N-glycans present at chondrocyte surfaces or in the cartilage matrix. Sialic acids are transferred to glycoproteins in either α-2,3 or α-2,6 linkage by specific sialyltransferases (SiaTs) and can potentially affect cell functions and cell-matrix interactions. The present study aimed to assess the relationship between the expression of the human chondrocyte phenotype and the sialylation of chondrocyte glycoprotein N-glycans. Methods The transcription of 5 SiaT was quantified using real-time RT-PCR assays. N-glycan analysis was performed using LC-ESI-MS. Primary human chondrocytes were cultured in monolayer or alginate beads and compared to the chondrocyte cell lines C-28/I2 and SW1353. In addition, effects of interleukin-1β or tumor necrosis factor-α on primary cells were assessed. Results Primary human chondrocytes predominantly express α-2,6-specific SiaTs and accordingly, α-2,6-linked sialic acid residues in glycoprotein N-glycans. In contrast, the preponderance of α-2,3-linked sialyl residues and, correspondingly, reduced levels of α-2,6-specific SiaTs are associated with the altered chondrocyte phenotype of C-28/I2 and SW1353 cells. Importantly, a considerable shift towards α-2,3-linked sialic acids and α-2,3-specific SiaT mRNA levels occurred in primary chondrocytes treated with IL-1β or TNF-α. Conclusion The expression of the differentiated chondrocyte phenotype is linked to the ratio of α-2,6- to α-2,3-linked sialic acids in chondrocyte glycoprotein N-glycans. A shift towards altered sialylation might contribute to impaired cell-matrix interactions in disease conditions.

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Section: Methodsmentioning

confidence: 99%

Phenotype-related differential α-2,6- or α-2,3-sialylation of glycoprotein N-glycans in human chondrocytes

Toegel

Pabst

et al. 2010

Osteoarthritis and Cartilage

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“…Absorbance was measured in triplicate at 650 nm using a Tecan Infinite M200 microplate reader (SLT). Finally, absorbance values were normalized to equal DNA contents as evaluated using the CyQuant assay (Piana et al 2007). …”

Section: Methodsmentioning

confidence: 99%

Lectin binding patterns reflect the phenotypic status of in vitro chondrocyte models

Toegel

Plattner

et al. 2009

In Vitro Cell.Dev.Biol.-Animal

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In vitro studies using chondrocyte cell cultures have increased our understanding of cartilage physiology and the altered chondrocytic cell phenotype in joint diseases. Beside the use of primary cells isolated from cartilage specimens of donors, immortalized chondrocyte cell lines such as C-28/I2 and T/C-28a2 have facilitated reproducible and standardized experiments. Although carbohydrate structures appear of significance for cartilage function, the contribution of the chondrocyte glycocalyx to matrix assembly and alterations of the chondrocyte phenotype is poorly understood. Therefore, the present study aimed to evaluate the glycoprofile of primary human chondrocytes as well as of C-28/I2 and T/C-28a2 cells in culture. First, the chondrocytic phenotype of primary and immortalized cells was assessed using real-time reverse transcriptase polymerase chain reaction, immunofluorescence, and glycosaminoglycans staining. Then, a panel of lectins was selected to probe for a range of oligosaccharide sequences determining specific products of the O-glycosylation and N-glycosylation pathways. We found that differences in the molecular phenotype between primary chondrocytes and the immortalized chondrocyte cell models C-28/I2 and T/C-28a2 are reflected in the glycoprofile of the cells. In this regard, the glycocalyx of immortalized chondrocytes was characterized by reduced levels of high-mannose type and sialic acid-capped N-glycans as well as increased fucosylated O-glycosylation products. In summary, the present report emphasizes the glycophenotype as an integral part of the chondrocyte phenotype and points at a significant role of the glycophenotype in chondrocyte differentiation.

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“…A study using Caco-2 cells showed that there was a relationship between perfluoronated functional coating and degree of cell differentiation [127]. A study using Caco-2 cells showed that there was a relationship between perfluoronated functional coating and degree of cell differentiation [127].…”

Section: Role Of Surface Chemistry In Tissue Engineeringmentioning

confidence: 99%

Surface Chemistry Influences Implant Biocompatibility

Thevenot

Tang³

2008

CTMC

695

224

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Implantable medical devices are increasingly important in the practice of modern medicine. Unfortunately, almost all medical devices suffer to a different extent from adverse reactions, including inflammation, fibrosis, thrombosis and infection. To improve the safety and function of many types of medical implants, a major need exists for development of materials that evoked desired tissue responses. Because implant-associated protein adsorption and conformational changes thereafter have been shown to promote immune reactions, rigorous research efforts have been emphasized on the engineering of surface property (physical and chemical characteristics) to reduce protein adsorption and cell interactions and subsequently improve implant biocompatibility. This brief review is aimed to summarize the past efforts and our recent knowledge about the influence of surface functionality on protein:cell:biomaterial interactions. It is our belief that detailed understandings of bioactivity of surface functionality provide an easy, economic, and specific approach for the future rational design of implantable medical devices with desired tissue reactivity and, hopefully, wound healing capability.

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Influence of surface modification on vitality and differentiation of Caco-2 cells

Cited by 12 publications

References 17 publications

Phenotype-related differential α-2,6- or α-2,3-sialylation of glycoprotein N-glycans in human chondrocytes

Phenotype-related differential α-2,6- or α-2,3-sialylation of glycoprotein N-glycans in human chondrocytes

Lectin binding patterns reflect the phenotypic status of in vitro chondrocyte models

Surface Chemistry Influences Implant Biocompatibility

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