Limits...
Thrombospondin-1 (TSP-1) Stimulates Expression of Integrin alpha6 in Human Breast Carcinoma Cells: A Downstream Modulator of TSP-1-Induced Cellular Adhesion.

John AS, Rothman VL, Tuszynski GP - J Oncol (2010)

Bottom Line: This paper reports the novel finding that TSP-1 upregulates integrin alpha6 subunit in human keratinocytes and human breast cancer cells resulting in increased cell adhesion and tumor cell invasion.The effect of TSP-1 on alpha6 subunit expression was examined in human keratinocytes and breast adenocarcinoma cell lines (MDA-MB-231) treated with TSP-1 and in TSP-1 stably transfected breast cancer cells.These data suggest that TSP-1 plays an integral role in the attachment of cells to the ECM facilitating cell motility and angiogenesis.

View Article: PubMed Central - PubMed

Affiliation: Division of Pediatric Cardiology, Children's National Medical Center, George Washington University, Washington, DC 20052, USA.

ABSTRACT
Thrombospondin-1 (TSP-1) is involved in a variety of different cellular processes including cell adhesion, tumor progression, and angiogenesis. This paper reports the novel finding that TSP-1 upregulates integrin alpha6 subunit in human keratinocytes and human breast cancer cells resulting in increased cell adhesion and tumor cell invasion. The effect of TSP-1 on alpha6 subunit expression was examined in human keratinocytes and breast adenocarcinoma cell lines (MDA-MB-231) treated with TSP-1 and in TSP-1 stably transfected breast cancer cells. TSP-1 upregulated alpha6 message and protein in these cells as revealed by differential display, Northern and Western blot analysis and immunohistochemical localization studies. The increased expression of alpha6 was shown to mediate adhesion and invasion of these cells to laminin, a major component of the basement membrane and extracellular matrix (ECM). These data suggest that TSP-1 plays an integral role in the attachment of cells to the ECM facilitating cell motility and angiogenesis.

No MeSH data available.


Related in: MedlinePlus

TSP-1 upregulates integrin α6 subunit message in human keratinocytes.  Keratinocytes were treated with either bis-tris-propane buffer or TSP-1 (60 μg/mL) in serum-free media and mRNA expression was analyzed by (a) differential display analysis and confirmed with (b) northern blot analysis.  Experiments were repeated three times and the results of a representative experiment are shown in the figure.
© Copyright Policy - open-access
Related In: Results  -  Collection


getmorefigures.php?uid=PMC2902750&req=5

fig1: TSP-1 upregulates integrin α6 subunit message in human keratinocytes. Keratinocytes were treated with either bis-tris-propane buffer or TSP-1 (60 μg/mL) in serum-free media and mRNA expression was analyzed by (a) differential display analysis and confirmed with (b) northern blot analysis. Experiments were repeated three times and the results of a representative experiment are shown in the figure.

Mentions: Differential display analysis was performed on keratinocytes treated with either 20 mM bis-tris propane buffer (vehicle for TSP-1) or TSP-1 (60 μg/mL) for twenty-four hours. The mRNA from these cells was collected and used for differential display RT-PCR. Several bands were found to be upregulated (Figure 1(a)) between buffer and TSP-1-treated samples in two separate mRNA samples collected from independent experiments. The upregulation of one band was confirmed using Northern blot analysis (Figure 1(b)). The isolated band (236 bp) was cloned and sequenced and was found to show 98% homology to the integrin α6 subunit.


Thrombospondin-1 (TSP-1) Stimulates Expression of Integrin alpha6 in Human Breast Carcinoma Cells: A Downstream Modulator of TSP-1-Induced Cellular Adhesion.

John AS, Rothman VL, Tuszynski GP - J Oncol (2010)

TSP-1 upregulates integrin α6 subunit message in human keratinocytes.  Keratinocytes were treated with either bis-tris-propane buffer or TSP-1 (60 μg/mL) in serum-free media and mRNA expression was analyzed by (a) differential display analysis and confirmed with (b) northern blot analysis.  Experiments were repeated three times and the results of a representative experiment are shown in the figure.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2902750&req=5

fig1: TSP-1 upregulates integrin α6 subunit message in human keratinocytes. Keratinocytes were treated with either bis-tris-propane buffer or TSP-1 (60 μg/mL) in serum-free media and mRNA expression was analyzed by (a) differential display analysis and confirmed with (b) northern blot analysis. Experiments were repeated three times and the results of a representative experiment are shown in the figure.
Mentions: Differential display analysis was performed on keratinocytes treated with either 20 mM bis-tris propane buffer (vehicle for TSP-1) or TSP-1 (60 μg/mL) for twenty-four hours. The mRNA from these cells was collected and used for differential display RT-PCR. Several bands were found to be upregulated (Figure 1(a)) between buffer and TSP-1-treated samples in two separate mRNA samples collected from independent experiments. The upregulation of one band was confirmed using Northern blot analysis (Figure 1(b)). The isolated band (236 bp) was cloned and sequenced and was found to show 98% homology to the integrin α6 subunit.

Bottom Line: This paper reports the novel finding that TSP-1 upregulates integrin alpha6 subunit in human keratinocytes and human breast cancer cells resulting in increased cell adhesion and tumor cell invasion.The effect of TSP-1 on alpha6 subunit expression was examined in human keratinocytes and breast adenocarcinoma cell lines (MDA-MB-231) treated with TSP-1 and in TSP-1 stably transfected breast cancer cells.These data suggest that TSP-1 plays an integral role in the attachment of cells to the ECM facilitating cell motility and angiogenesis.

View Article: PubMed Central - PubMed

Affiliation: Division of Pediatric Cardiology, Children's National Medical Center, George Washington University, Washington, DC 20052, USA.

ABSTRACT
Thrombospondin-1 (TSP-1) is involved in a variety of different cellular processes including cell adhesion, tumor progression, and angiogenesis. This paper reports the novel finding that TSP-1 upregulates integrin alpha6 subunit in human keratinocytes and human breast cancer cells resulting in increased cell adhesion and tumor cell invasion. The effect of TSP-1 on alpha6 subunit expression was examined in human keratinocytes and breast adenocarcinoma cell lines (MDA-MB-231) treated with TSP-1 and in TSP-1 stably transfected breast cancer cells. TSP-1 upregulated alpha6 message and protein in these cells as revealed by differential display, Northern and Western blot analysis and immunohistochemical localization studies. The increased expression of alpha6 was shown to mediate adhesion and invasion of these cells to laminin, a major component of the basement membrane and extracellular matrix (ECM). These data suggest that TSP-1 plays an integral role in the attachment of cells to the ECM facilitating cell motility and angiogenesis.

No MeSH data available.


Related in: MedlinePlus