scholarly journals CD44H regulates tumor cell migration on hyaluronate-coated substrate.

1992 ◽  
Vol 118 (4) ◽  
pp. 971-977 ◽  
Author(s):  
L Thomas ◽  
H R Byers ◽  
J Vink ◽  
I Stamenkovic
Keyword(s):  
Cell Migration ◽  
Cell Surface ◽  
Binding Capacity ◽  
Surface Glycoprotein ◽  
Cell Surface Receptor ◽  
Cell Surface Glycoprotein ◽  
Tumor Cell Migration ◽  
Coated Substrate ◽  
Direct Demonstration ◽  
Surface Receptor

CD44 is a broadly distributed cell surface glycoprotein expressed in different isoforms in various tissues and cell lines. One of two recently characterized human isoforms, CD44H, is a cell surface receptor for hyaluronate, suggesting a role in the regulation of cell-cell and cell-substrate interactions as well as of cell migration. While CD44H has been shown to mediate cell adhesion, direct demonstration that CD44H expression promotes cell motility has been lacking. In this work we show that a human melanoma cell line, stably transfected with CD44H, displays enhanced motility on hyaluronate-coated surfaces while transfectants expressing an isoform that does not bind hyaluronate, CD44E, fail to do so. Migration of CD44H-expressing transfectants is observed to be blocked by a soluble CD44-immunoglobulin fusion protein as well as by anti-CD44 antibody, and to depend on the presence of the cytoplasmic domain of CD44. However, cells expressing CD44H cytoplasmic deletion mutants retain significant binding capacity to hyaluronate-coated substrate. Taken together, our results provide direct evidence that CD44H plays a major role in regulating cell migration on hyaluronate-coated substrate.

scholarly journals Sphingosine 1-Phosphate Stimulates Cell Migration through a Gi-coupled Cell Surface Receptor

1999 ◽  
Vol 274 (50) ◽  
pp. 35343-35350 ◽  
Author(s):  
Fang Wang ◽  
James R. Van Brocklyn ◽  
John P. Hobson ◽  
Sharareh Movafagh ◽  
Zofia Zukowska-Grojec ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cell Surface ◽  
Cell Surface Receptor ◽  
Sphingosine 1 Phosphate ◽  
Surface Receptor

scholarly journals PSGL-1 Inhibits the Incorporation of SARS-CoV and SARS-CoV-2 Spike Glycoproteins into Pseudovirions and Impairs Pseudovirus Attachment and Infectivity

Viruses ◽  
2020 ◽  
Vol 13 (1) ◽  
pp. 46
Author(s):  
Sijia He ◽  
Abdul A. Waheed ◽  
Brian Hetrick ◽  
Deemah Dabbagh ◽  
Ivan V. Akhrymuk ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cell Surface ◽  
Immune Cells ◽  
Interferon Γ ◽  
Surface Glycoprotein ◽  
Target Cells ◽  
Cell Surface Glycoprotein ◽  
A Cell ◽  
Antiviral Activities ◽  
Hiv 1

P-selectin glycoprotein ligand-1 (PSGL-1) is a cell surface glycoprotein that binds to P-, E-, and L-selectins to mediate the tethering and rolling of immune cells on the surface of the endothelium for cell migration into inflamed tissues. PSGL-1 has been identified as an interferon-γ (INF-γ)-regulated factor that restricts HIV-1 infectivity, and has recently been found to possess broad-spectrum antiviral activities. Here we report that the expression of PSGL-1 in virus-producing cells impairs the incorporation of SARS-CoV and SARS-CoV-2 spike (S) glycoproteins into pseudovirions and blocks pseudovirus attachment and infection of target cells. These findings suggest that PSGL-1 may potentially inhibit coronavirus replication in PSGL-1+ cells

Regulation of growth and dissemination of a human lymphoma by CD44 splice variants

1995 ◽  
Vol 108 (4) ◽  
pp. 1723-1733 ◽  
Author(s):  
A. Bartolazzi ◽  
D. Jackson ◽  
K. Bennett ◽  
A. Aruffo ◽  
R. Dickinson ◽  
...  
Keyword(s):  
Cell Surface ◽  
Tumor Growth ◽  
Splice Variants ◽  
Tumor Formation ◽  
Surface Glycoprotein ◽  
Cell Surface Receptor ◽  
Cell Surface Glycoprotein ◽  
Cd44 Isoforms ◽  
Coated Surfaces

CD44 is a polymorphic cell surface glycoprotein, currently proposed to be the principal cell surface receptor for hyaluronan. However, different isoforms of CD44, expressed in human lymphoid tumor cells, appear to have distinct effects on the ability of the cells to attach to hyaluronan-coated surfaces and on their capacity to form tumors in vivo. In the present study, we address the mechanisms that may regulate CD44 isoform-dependent adhesion to hyaluronan. We use a human Burkitt lymphoma, stably transfected with six different alternatively spliced human CD44 isoforms, to determine their potential hyaluronan binding and tumor growth promoting roles. We show that transfectants expressing CD44 splice variants that contain variable exons 6–10, 7–10 and 8–10 adhere to hyaluronan-coated surfaces weakly and that corresponding tumor formation in vivo is delayed with respect to CD44-negative parental cell-derived tumors. Abundant shedding of these three isoforms may play a significant role in determining the rate of tumor development. Transfectants expressing variable exon 3, on the other hand, fail to display CD44-mediated adhesion to hyaluronan, but form bone marrow tumors rapidly following intravenous injection. These observations suggest that different mechanisms regulate CD44-mediated adhesion and tumor growth, and provide evidence that expression of exon v3 may confer novel ligand-binding properties.

scholarly journals The human alpha 2-macroglobulin receptor: identification of a 420-kD cell surface glycoprotein specific for the activated conformation of alpha 2-macroglobulin.

1990 ◽  
Vol 110 (4) ◽  
pp. 1041-1048 ◽  
Author(s):  
J D Ashcom ◽  
S E Tiller ◽  
K Dickerson ◽  
J L Cravens ◽  
W S Argraves ◽  
...  
Keyword(s):  
Cell Surface ◽  
Affinity Chromatography ◽  
Anion Exchange Chromatography ◽  
Binding Activity ◽  
Exchange Chromatography ◽  
Surface Glycoprotein ◽  
Cell Surface Receptor ◽  
Affinity Matrix ◽  
Cell Surface Glycoprotein ◽  
A Cell

Ligand affinity chromatography was used to purify a cell surface alpha 2-macroglobulin (alpha 2M) receptor. Detergent extracts of human placenta were applied to an affinity matrix consisting of alpha 2M, previously reacted with methylamine, coupled to Sepharose. Elution with EDTA specifically released polypeptides with apparent molecular masses of 420 and 39 kD. In some preparations, small amounts of a 90-kD polypeptide were observed. The 420- and 39-kD polypeptides appear specific for the forms of alpha 2M activated by reaction with proteinases or methylamine and do not bind to an affinity matrix consisting of native alpha 2M coupled to Sepharose. Separation of these two polypeptides was accomplished by anion exchange chromatography, and binding activity was exclusively associated with the 420-kD polypeptide. The purified 420-kD protein binds to the conformationally altered forms of alpha 2M that are known to specifically interact with alpha 2M receptors and does not bind to native alpha 2M. Binding of the 420-kD polypeptide to immobilized wheat germ agglutinin indicates that this polypeptide is a glycoprotein. The cell surface localization of the 420-kD glycoprotein was confirmed by affinity chromatography of extracts from surface radioiodinated fibroblasts. These properties suggest that the 420-kD polypeptide is a cell surface receptor for the activated forms of alpha 2M.

scholarly journals Factors That Increase the Effective Concentration of CXCR4 Dictate Feline Immunodeficiency Virus Tropism and Kinetics of Replication

2004 ◽  
Vol 78 (17) ◽  
pp. 9132-9143 ◽  
Author(s):  
Aymeric de Parseval ◽  
Stacie Ngo ◽  
Peiqing Sun ◽  
John H. Elder
Keyword(s):  
Cell Surface ◽  
Conformational Changes ◽  
Feline Immunodeficiency Virus ◽  
Effective Concentration ◽  
Surface Glycoprotein ◽  
Cell Surface Receptor ◽  
Productive Infection ◽  
Immunodeficiency Virus ◽  
Surface Receptor ◽  
Extensive Cell

ABSTRACT The surface glycoprotein (gp95) of the feline immunodeficiency virus (FIV) binds in a strain-specific manner to several cell surface molecules, including CXCR4, heparan sulfate proteoglycans (HSPGs), DC-SIGN, and a 43-kDa cell surface receptor on T cells recently identified as CD134 by M. Shimojima et al. (Science 303:1192-1195, 2004). CXCR4 is the entry receptor in all known cases, and the other molecules act as binding receptors to help facilitate infection. In this report, we confirm and extend the findings regarding CD134 as a primary receptor for FIV. In addition, we show that temperature critically influences the binding properties of FIV gp95 to CXCR4 and HSPGs. The data show that gp95 of the field strain FIV-PPR bound to CXCR4 at 22°C, whereas binding was not detected at 4°C. In contrast, binding of the laboratory adapted FIV-34TF10 gp95 was observed at either 4°C or 22°C, albeit at increased levels at the higher temperature. The level of CXCR4 increased after the temperature was switched from 4 to 22°C, whereas the level of HSPGs decreased, resulting in higher binding of gp95 from both strains to CXCR4 and lower binding of gp95 of FIV-34TF10 to HSPGs (FIV-PPR gp95 does not bind to these molecules). The findings also show that HSPGs facilitate the CXCR4-mediated infectivity of CrFK and G355-5 cells by FIV-34TF10. These two nonlymphoid cell lines express very low levels of CXCR4 and are permissive to FIV-34TF10 but not to productive infection by FIV-PPR. However, overexpression of human CXCR4 in CrFK or G-355-5 cells resulted in extensive cell fusion and infection by FIV-PPR. Taken together, these findings indicate that factors that increase the effective concentration of CXCR4 enhance FIV infectivity and may involve (i) temperature or ligand-induced conformational changes in CXCR4 that enhance SU binding, (ii) coreceptor interactions with gp95 that either alter gp95 conformation to enhance CXCR4 binding and/or raise the localized concentration of receptor or ligand, or (iii) direct increase in CXCR4 concentration via overexpression.

scholarly journals Expression and function of a putative cell surface receptor for fibronectin in hamster and human cell lines.

1986 ◽  
Vol 103 (4) ◽  
pp. 1595-1603 ◽  
Author(s):  
P J Brown ◽  
R L Juliano
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Lines ◽  
Human Cell ◽  
Mammalian Cells ◽  
Surface Glycoprotein ◽  
Cell Surface Receptor ◽  
Human Cell Lines ◽  
Cell Surface Glycoprotein ◽  
Fibronectin Receptor

We have previously reported the use of monoclonal antibodies to identify a 140-kD cell surface glycoprotein in mammalian cells that is specifically involved in fibronectin-mediated cell adhesion. We now report the purification of this molecule using immunoaffinity chromatography and the subsequent generation of polyclonal antibodies that selectively immunoprecipitate 140-kD putative fibronectin receptor glycoprotein (gp140) extracted from rodent or human cells; these antibodies also specifically block fibronectin-mediated cell adhesion but not adhesion mediated by other factors in serum. Expression of gp140-like molecules was detected on the surfaces of several adherent human cell lines (HDF, WISH, and EFC) but not on erythrocytes; however, gp140 was also detected on a nonadherent human lymphoid line (DAUDI). Analysis of gp140 on nonreducing SDS gels revealed two closely migrating bands. Protease digestion and peptide mapping suggests that the two bands are closely related polypeptides.

scholarly journals Mitogenesis, cell migration, and loss of focal adhesions induced by tenascin-C interacting with its cell surface receptor, annexin II.

1996 ◽  
Vol 7 (6) ◽  
pp. 883-892 ◽  
Author(s):  
C Y Chung ◽  
J E Murphy-Ullrich ◽  
H P Erickson
Keyword(s):  
Endothelial Cells ◽  
Cell Migration ◽  
Cell Surface ◽  
Focal Adhesions ◽  
Cell Surface Receptor ◽  
Annexin Ii ◽  
Tenascin C ◽  
Subsequent Response ◽  
Surface Receptor ◽  
A Cell

In a previous study we demonstrated that the alternatively spliced region of tenascin-C, TNfnA-D, bound with high affinity to a cell surface receptor, annexin II. In the present study we demonstrate three changes in cellular activity that are produced by adding intact tenascin-C or TNfnA-D to cells, and we show that all three activities are blocked by antibodies against annexin II. 1) TNfnA-D added to confluent endothelial cells induced loss of focal adhesions. 2) TNfnA-D produced a mitogenic response of confluent, growth-arrested endothelial cells in 1% serum. TNfnA-D stimulated mitogenesis only when it was added to cells before or during exposure to other mitogens, such as basic fibroblast growth factor or serum. Thus the effect of TNfnA-D seems to be to facilitate the subsequent response to growth factors. 3) TNfnA-D enhanced cell migration in a cell culture wound assay. Antibodies to annexin II blocked all three cellular responses to TNfnA-D. These data show that annexin II receptors on endothelial cells mediate several cell regulatory functions attributed to tenascin-C, potentially through modulation of intracellular signalling pathways.

Expression, function, and localization of the REG cell surface receptor

2001 ◽  
Vol 120 (5) ◽  
pp. A18-A19
Author(s):  
B DIECKGRAEFE ◽  
C HOUCHEN ◽  
H ZHANG
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Surface Receptor
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