Integrin subunits (beta)1C-1 and (beta)1C-2 expressed in GD25T cells are retained and degraded intracellularly rather than localised to the cell surface

We have previously identified the integrin (beta)1C-2 and characterised the distribution of (beta)1C-1 and (beta)1C-2 transcripts in various cell lines and normal cells. In this study we have investigated the expression of the two (beta)1C-variants in integrin (beta)1 deficient mouse GD25T cells. After stable transfection of the GD25T cells with cDNAs coding for (beta)1A, (beta)1C-1 and (beta)1C-2, the cell surface expression of the (beta)1C-1 and (beta)1C-2 variants was found to be very low while the (beta)1A variant was expressed at high levels. Northern blot analysis showed that the level of (beta)1-transcript in the (beta)1C-1 and (beta)1C-2 clones was equal or higher than in the (beta)1A clones. Metabolic labelling and deglycosylation by endoglycosidase H treatment clearly demonstrated that the majority of the (beta)1C-1 and (beta)1C-2 chains did not become maturely glycosylated, nor did they dimerize with (alpha) subunits. After 20 hours of chase, the labelled (beta)1C-1 and (beta)1C-2 chains had been gradually degraded, whereas immature (beta)1A was converted into the maturely glycosylated form during the same period of time. Immunostaining showed intracellular (beta)1 localisation in the (beta)1C-1 and (beta)1C-2 expressing clones, while in the (beta)1A expressing clones the (beta)1 chains were mainly localised to focal adhesion sites and along fibronectin fibres. Taken together, we have shown that expression of both integrin (beta)1C-1 and (beta)1C-2 in GD25T cells result in very low cell surface expression compared with the normal (beta)1A isoform. Instead, both (beta)1C-1 and (beta)1C-2 chains remain in the endoplasmic reticulum until they are intracellularly degraded.

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Activation of Focal Adhesion Kinase in Detached Human Epidermal Cancer Cells and Their Long-term Survival Might be Associated with Cell Surface Expression of Laminin-5

Acta Dermato Venereologica ◽

10.2340/00015555-0405 ◽

2008 ◽

Vol 88 (2) ◽

pp. 100-107 ◽

Cited By ~ 2

Author(s):

H Katayama ◽

Y Yamane ◽

Y Furukawa ◽

S Kitagawa ◽

Y Nakamura ◽

...

Keyword(s):

Cell Surface ◽

Focal Adhesion Kinase ◽

Cancer Cells ◽

Focal Adhesion ◽

Surface Expression ◽

Cell Surface Expression ◽

Term Survival ◽

Long Term Survival ◽

Laminin 5

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Matrix metalloproteinase-2 activation modulates glioma cell migration

Journal of Cell Science ◽

10.1242/jcs.110.19.2473 ◽

1997 ◽

Vol 110 (19) ◽

pp. 2473-2482

Author(s):

E.I. Deryugina ◽

M.A. Bourdon ◽

G.X. Luo ◽

R.A. Reisfeld ◽

A. Strongin

Keyword(s):

Cell Migration ◽

Cell Surface ◽

Surface Expression ◽

Matrix Proteins ◽

Matrix Metalloproteinase 2 ◽

Cell Surface Expression ◽

Blocking Antibody ◽

Tumor Cell Migration ◽

Adhesion Sites ◽

Glioma Cell Migration

Stable transfection of U251.3 glioma cells with cDNA encoding MT-MMP-1 resulted in increased cell surface expression of MT-MMP-1 and TIMP-2, constitutive activation of MMP-2 proenzyme and increased collagen degradation. In tumor spheroid outgrowth assays, cell migration of MT-MMP-1 transfectants relative to control was enhanced on collagen and decreased on vitronectin and fibronectin. These effects were reversed by TIMP-2 and were not associated with any substantial changes in cell adhesion. Binding of U251.3 cells to the C-terminal domain of MMP-2 was specifically inhibited by anti-(alpha)vss3 integrin blocking antibody indicating that MMP-2 interacts with (alpha)vss3 through the enzyme's C-terminal portion at or near the integrin's matrix adhesion sites. We propose that these mechanisms could govern directed matrix degradation in the tumor cells' microenvironment by sequestration of active MMP-2 on the cell surface. Our data suggest that activation of MMP-2 and its proteolytic activity localized to the cell surface could differentially modulate tumor cell migration in response to particular matrix proteins by altering both composition of the extracellular matrix and expression of adhesion receptors on the cell surface.

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Faculty Opinions recommendation of Assembly and cell surface expression of TAP-independent, chloroquine-sensitive and interferon-gamma-inducible class I MHC complexes in transformed fibroblast cell lines are regulated by tapasin.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1009214.121258 ◽

2002 ◽

Author(s):

Tim Elliott

Keyword(s):

Cell Surface ◽

Cell Lines ◽

Interferon Gamma ◽

Fibroblast Cell ◽

Surface Expression ◽

Class I ◽

Cell Surface Expression ◽

Class I Mhc ◽

Fibroblast Cell Lines

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Faculty Opinions recommendation of Mechanism of cell surface expression of the Streptococcus mitis platelet binding proteins PblA and PblB.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1082761.535676 ◽

2007 ◽

Author(s):

Tim Mitchell

Keyword(s):

Cell Surface ◽

Binding Proteins ◽

Surface Expression ◽

Cell Surface Expression ◽

Streptococcus Mitis ◽

Platelet Binding

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Persistent HIV Transcription Induces Sialyl-Lewis-X Glyco-Antigen Cell-Surface Expression

SSRN Electronic Journal ◽

10.2139/ssrn.3565035 ◽

2020 ◽

Author(s):

Florent Colomb ◽

Leila B. Giron ◽

Leticia Kuri Cervantes ◽

Tongcui Ma ◽

Samson Adeniji ◽

...

Keyword(s):

Cell Surface ◽

Surface Expression ◽

Sialyl Lewis X ◽

Cell Surface Expression ◽

Lewis X ◽

Hiv Transcription ◽

Sialyl Lewis

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Influence of β-D-mannuronic acid, as a new member of non-steroidal anti-inflammatory drugs family, on expression pattern of chemokines and their receptors in rheumatoid arthritis

Current Drug Discovery Technologies ◽

10.2174/1570163816666191023103118 ◽

2019 ◽

Vol 16 ◽

Author(s):

Mona Aslani ◽

Arman Ahmadzadeh ◽

Zahra Aghazadeh ◽

Majid Zaki-Dizaji ◽

Laleh Sharifi ◽

...

Keyword(s):

Cell Surface ◽

Mrna Expression ◽

Surface Expression ◽

Phase Iii ◽

Cell Surface Expression ◽

Optimum Dose ◽

High Dose ◽

Mannuronic Acid ◽

Anti Inflammatory ◽

High Doses

Background: : Based on the encouraging results of phase III clinical trial of β-D-mannuronic acid (M2000) (as a new anti-inflammatory drug) in patients with RA, in this study, we aimed to evaluate the effects of this drug on the expression of chemokines and their receptors in PBMCs of RA patients. Methods:: PBMCs of RA patients and healthy controls were separated and the patients' cells were treated with low, moderate and high doses (5, 25 and 50 μg/mL) of M2000 and optimum dose (1 μg/mL) of diclofenac, as a control in RPMI-1640 medium. Real-time PCR was used for evaluating the mRNA expression of CXCR3, CXCR4, CCR2, CCR5 and CCL2/MCP-1. Cell surface expression of CCR2 was investigated using flow cytometry. Results:: CCR5 mRNA expression reduced significantly, after treatment of the patients' cells with all three doses of M2000 and optimum dose of diclofenac. CXCR3 mRNA expression down-regulated significantly followed by treatment of these cells with moderate and high doses of M2000 and optimum dose of diclofenac. CXCR4 mRNA expression declined significantly after treatment of these cells with moderate and high doses of M2000. CCL2 mRNA expression significantly reduced only followed by treatment of these cells with high dose of M2000, whereas, mRNA and cell surface expressions of CCR2 diminished significantly followed by treatment of these cells with high dose of M2000 and optimum dose of diclofenac. Conclusion:: According to our results, M2000 through the down-regulation of chemokines and their receptors may restrict the infiltration of immune cells into the synovium.

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