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Tenascin supports lymphocyte rolling.

Clark RA, Erickson HP, Springer TA - J. Cell Biol. (1997)

Bottom Line: Tenascin has been reported to have both adhesive and anti-adhesive effects in static assays.When compared to rolling of the same cell type on E-selectin, rolling on tenascin was found to be smoother at all shear stresses tested, suggesting that cells formed a larger number of bonds on the tenascin substrate than on the E-selectin substrate.When protein plating densities were adjusted to give similar profiles of cell detachment under increasing shears, the density of tenascin was 8.5-fold greater than that of E-selectin.

View Article: PubMed Central - PubMed

Affiliation: The Center for Blood Research and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.

ABSTRACT
Tenascin is a large extracellular matrix molecule expressed at specific sites in the adult, including immune system tissues such as the bone marrow, thymus, spleen, and T cell areas of lymph nodes. Tenascin has been reported to have both adhesive and anti-adhesive effects in static assays. We report here that tenascin supports the tethering and rolling of lymphocytes and lymphoblastic cell lines under flow conditions. Binding was calcium dependent and was not inhibited by treatment of lymphocytes with O-glycoprotease or a panel of glycosidases including neuraminidase and heparitinase but was inhibited by treatment of cells with proteinase K. Binding was to the fibrinogen-like terminal domain of tenascin as determined by antibody blocking studies and binding to recombinant tenascin proteins. When compared to rolling of the same cell type on E-selectin, rolling on tenascin was found to be smoother at all shear stresses tested, suggesting that cells formed a larger number of bonds on the tenascin substrate than on the E-selectin substrate. When protein plating densities were adjusted to give similar profiles of cell detachment under increasing shears, the density of tenascin was 8.5-fold greater than that of E-selectin. Binding to tenascin was not dependent on any molecules previously identified as tenascin receptors and is likely to involve a novel tenascin receptor on lymphocytes. We postulate that the ability of tenascin to support lymphocyte rolling may reflect its ability to support cell migration and that this interaction may be used by lymphocytes migrating through secondary lymphoid organs.

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The domain structure of the hexabrachion arm of human tenascin (above) and the bacterial expression proteins used  in this study (below), modified from reference 5.
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Figure 3: The domain structure of the hexabrachion arm of human tenascin (above) and the bacterial expression proteins used in this study (below), modified from reference 5.

Mentions: The cell adhesion activity of tenascin has produced some controversial results in which the whole molecule and smaller segments promote either adhesion or anti-adhesion for different cell types. Recent studies using bacterial expression proteins have identified two major cell adhesion sites in the tenascin molecule that promote adhesion of a broad range of cell types (see Fig. 3 for the domain structure of tenascin). The third FN-III domain binds three different integrins and mediates adhesion of several cell types (5, 35, 46, 52, 66). The fibrinogen domain mediates adhesion of fibroblasts via a cell surface proteoglycan (5), endothelial cells via an integrin (35), and a variety of other cells (46). In addition to these two sites, neurons can bind to FN-III domains 1–2, 7–8, and the alternatively spliced domains (22, 30, 46).


Tenascin supports lymphocyte rolling.

Clark RA, Erickson HP, Springer TA - J. Cell Biol. (1997)

The domain structure of the hexabrachion arm of human tenascin (above) and the bacterial expression proteins used  in this study (below), modified from reference 5.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2139881&req=5

Figure 3: The domain structure of the hexabrachion arm of human tenascin (above) and the bacterial expression proteins used in this study (below), modified from reference 5.
Mentions: The cell adhesion activity of tenascin has produced some controversial results in which the whole molecule and smaller segments promote either adhesion or anti-adhesion for different cell types. Recent studies using bacterial expression proteins have identified two major cell adhesion sites in the tenascin molecule that promote adhesion of a broad range of cell types (see Fig. 3 for the domain structure of tenascin). The third FN-III domain binds three different integrins and mediates adhesion of several cell types (5, 35, 46, 52, 66). The fibrinogen domain mediates adhesion of fibroblasts via a cell surface proteoglycan (5), endothelial cells via an integrin (35), and a variety of other cells (46). In addition to these two sites, neurons can bind to FN-III domains 1–2, 7–8, and the alternatively spliced domains (22, 30, 46).

Bottom Line: Tenascin has been reported to have both adhesive and anti-adhesive effects in static assays.When compared to rolling of the same cell type on E-selectin, rolling on tenascin was found to be smoother at all shear stresses tested, suggesting that cells formed a larger number of bonds on the tenascin substrate than on the E-selectin substrate.When protein plating densities were adjusted to give similar profiles of cell detachment under increasing shears, the density of tenascin was 8.5-fold greater than that of E-selectin.

View Article: PubMed Central - PubMed

Affiliation: The Center for Blood Research and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.

ABSTRACT
Tenascin is a large extracellular matrix molecule expressed at specific sites in the adult, including immune system tissues such as the bone marrow, thymus, spleen, and T cell areas of lymph nodes. Tenascin has been reported to have both adhesive and anti-adhesive effects in static assays. We report here that tenascin supports the tethering and rolling of lymphocytes and lymphoblastic cell lines under flow conditions. Binding was calcium dependent and was not inhibited by treatment of lymphocytes with O-glycoprotease or a panel of glycosidases including neuraminidase and heparitinase but was inhibited by treatment of cells with proteinase K. Binding was to the fibrinogen-like terminal domain of tenascin as determined by antibody blocking studies and binding to recombinant tenascin proteins. When compared to rolling of the same cell type on E-selectin, rolling on tenascin was found to be smoother at all shear stresses tested, suggesting that cells formed a larger number of bonds on the tenascin substrate than on the E-selectin substrate. When protein plating densities were adjusted to give similar profiles of cell detachment under increasing shears, the density of tenascin was 8.5-fold greater than that of E-selectin. Binding to tenascin was not dependent on any molecules previously identified as tenascin receptors and is likely to involve a novel tenascin receptor on lymphocytes. We postulate that the ability of tenascin to support lymphocyte rolling may reflect its ability to support cell migration and that this interaction may be used by lymphocytes migrating through secondary lymphoid organs.

Show MeSH
Related in: MedlinePlus