Hyaluronan-binding proteins on cultured J 774 macrophages

Gustafson, Stefan; Forsberg, Nina

doi:10.1016/0167-4889(91)90218-m

Cited by 12 publications

(4 citation statements)

References 20 publications

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“…Type I collagen was extracted from rat tail tendon according to classical protocols (24). The anti-CD44 R-phycoerythrin-conjugated mouse anti-human monoclonal antibody (G44 -26) and mouse IgG2b (clone [27][28][29][30][31][32][33][34][35] were from BD Pharmingen (Franklin Lakes, NJ). The anti-MT1-MMP polyclonal antibody AB-815, the anti-caveolin-1 monoclonal antibody, the anti-ERK and anti-phospho-ERK (Thr 202 /Tyr 204 ) antibodies were from Chemicon (Temecula, CA).…”

Section: Methodsmentioning

confidence: 99%

“…Because HA uptake/degradation was shown to occur at higher temperatures, we performed the FITC-labeled HA (HA-FITC) binding assay at 4°C, at which no active internalization occurs (28,29). HA-FITC bound to the cell surface of glioma cells detached by trypsinization, as was demonstrated by the shift in fluorescence intensity (Fig.…”

Section: Ha Binding To U-87 Glioma Cells Is An Mmp-regulatedmentioning

confidence: 99%

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Hyaluronan Cell Surface Binding Is Induced by Type I Collagen and Regulated by Caveolae in Glioma Cells

Annabi

Thibeault

Moumdjian

et al. 2004

Journal of Biological Chemistry

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Hyaluronan (HA) is a component of the brain extracellular matrix environment that is synthesized and secreted by glioma cells. The primary cell surface receptor for HA is CD44, a membrane glycoprotein that is functionally regulated by a membrane type 1 matrix metalloproteinase (MT1-MMP). Both CD44 and MT1-MMP are partially located in Triton X-100-insoluble domains, but no functional link has yet been established between them. In the present study, we studied the regulation of HA cell surface binding in U-87 glioma cells. We show that an MMP-dependent mechanism regulates the intrinsic cell surface binding of HA as ilomastat, a broad MMP inhibitor, increased HA binding to glioma cells. HA binding was also rapidly and specifically up-regulated by 3-fold by type I collagen in U-87 cells, which also induced a significant morphological reorganization associated with the activation of a latent form of MMP-2 through a MT1-MMP-mediated mechanism. Interestingly, caveolae depletion with a cell surface cholesteroldepleting agent ␤-cyclodextrin triggered an additional increase (9-fold) in the binding of HA, in synergy with type I collagen. On the other hand, HA cell surface binding was diminished by the MEK inhibitor PD98059 and by the overexpression of a recombinant, wild type MT1-MMP, whereas its cytoplasmic-deleted form had no effect. Taken together, our results suggest that MT1-MMP regulates, through its cytoplasmic domain, the cell surface functions of CD44 in a collagen-rich pericellular environment. Additionally, we describe a new molecular mechanism regulating the invasive potential of glioma cells involving a MT1-MMP/CD44/caveolin interaction, which could represent a potential target for anti-cancer therapies.The principal molecules that have been identified in the normal brain extracellular matrix (ECM) 1 are hyaluronan (HA; also known as hyaluronic acid, hyaluronate) and chondroitin sulfate (1, 2). HA is an important glycosaminoglycan constituent believed to be implicated in angiogenesis, the formation of new blood vessels from preexisting vasculature. Although the serum level of HA is already used as an indicator of progressive malignant disease (3), its effects on in vivo angiogenesis and endothelial cell (EC) function are complex and have been reported to depend on HA concentration and molecular size (4, 5). Accordingly, whereas high molecular weight HA was shown to inhibit EC functions (6), low molecular weight HA stimulated EC proliferation, tubulogenesis (6, 7), and neovascularization (8). Moreover, small HA polymers efficiently regulated CD44 cell surface functional expression and promoted tumor cell migration (9). Astrocytic tumors of the central nervous system express CD44 among other cell adhesion receptors of the integrin or immunoglobulin superfamily. Although HA is the principal ligand of CD44, other CD44 ligands include the ECM components collagen, fibronectin, laminin, and chondroitin sulfate, whereas mucosal addressin, serglycin, osteopontin, and the class II invariant chain represent ECM-unrelat...

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Section: Methodsmentioning

confidence: 99%

Section: Ha Binding To U-87 Glioma Cells Is An Mmp-regulatedmentioning

confidence: 99%

Hyaluronan Cell Surface Binding Is Induced by Type I Collagen and Regulated by Caveolae in Glioma Cells

Annabi

Thibeault

Moumdjian

et al. 2004

Journal of Biological Chemistry

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“…The KC can effectively degrade HA to low-Mr products (Table 3). It has previously been shown by Gustafson & Forsberg (1991) that a murine macrophage cell line also degrades the polysaccharide. The ability of KC to degrade HA is consistent with the presence ofhyaluronidase in KC as well as in LEC (L. Roden, personal communication) and also of the enzyme Nacetylglucosamine 6-phosphate deacetylase, which is required for the formation of free acetate from the acetyl groups of HA (Campbell et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

“…Underhill (1989) observed that most macrophages react with an antibody directed towards a HA-binding protein, although the receptors were notably absent in KC. HA-binding proteins have also been identified in hamster alveolar macrophages (Green et al, 1988) and on cultured J774 macrophages (Gustafson & Forsberg, 1991). Furthermore, it has been demonstrated that HA increases the uptake of opsonized yeast particles in monocytes (Ahlgren & Jarstrand, 1984), and at relatively high concentrations inhibits phagocytosis in monocytes (Forrester & Balazs, 1980).…”

Section: Introductionmentioning

confidence: 96%

Endocytosis of hyaluronan in rat Kupffer cells

Alston-Smith

Pertoft

Laurent

1992

Biochemical Journal

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The binding, uptake and degradation of hyaluronan (HA) labelled with 3H in its acetyl group were studied in cultured rat Kupffer cells (KC). At 4 degrees C the binding increased with increasing concentrations of HA in the culture medium up to at least 1 microgram/ml, when saturation occurred. Binding could be prevented efficiently by the addition of an excess of unlabelled HA, and to a lesser extent by chondroitin sulphate and oligosaccharide fragments of HA, consisting of four sugars or more. The labelled HA bound to the cells could be removed by incubating the cells with Streptomyces hyaluronidase, or trypsin, indicating that the HA-binding sites are located on the cell surface. At 37 degrees C HA was internalized in a concentration-dependent manner, and degradation products appeared in the supernatant after 1-5 h, depending on the concentration applied. At 50 ng of free HA/ml, each KC accumulated 60 ag of the polysaccharide/min in the first 1 h, and degraded a total amount of 10 fg of HA during an 8 h period. Addition of the negatively charged polysaccharide dextran sulphate reduced binding, and to an even greater extent internalization, of HA in KC, while no effect was observed with dextran. Depletion of intracellular potassium caused a marked reduction in the rate of endocytosis of cell-membrane-associated HA into KC, without affecting binding. Addition of KCl to the culture medium returned endocytosis of [3H]HA to normal levels. There was no effect on binding and a partial effect on internalization by depletion of bivalent cations or in the presence of EDTA. The degradation of [3H]HA by KC cultures was abolished in the presence of weak bases, NH4Cl and chloroquine, supporting the idea that HA is endocytosed into lysosomes prior to degradation. The fluid-phase marker [14C]sucrose was internalized in the cells at much lower rate than was HA. Rates of binding, internalization and degradation of HA in KC point therefore to a specific endocytosis followed by an intracellular degradation to low-M(r) compounds. It was estimated that, under physiological conditions, KC only clear a minor proportion of circulating HA.

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