Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains

2002 ◽  
Vol 115 (16) ◽  
pp. 3309-3318 ◽  
Author(s):  
Hidekazu Takagi ◽  
Yasushi Asano ◽  
Naomi Yamakawa ◽  
Isamu Matsumoto ◽  
Koji Kimata
Keyword(s):  
Cell Surface ◽  
Chondroitin Sulfate ◽  
Cell Sorting ◽  
Cell Attachment ◽  
Chondroitin Sulfate Proteoglycans ◽  
Cell Surface Receptor ◽  
A431 Cells ◽  
Stable Transfectants ◽  
Surface Receptor ◽  
35 Kda Protein

Chondroitin sulfate proteoglycans, including PG-M/versican, inhibit cell-substratum adhesion. They achieve this through their chondroitin sulfate chains. In order to define the molecular mechanism for this inhibition, we investigated the influence of these chains on cell attachment to substratum,the first step in cell adhesion. Chondroitin sulfate chains did not prevent cell attachment. In fact, a variety of cells attached to chondroitin sulfate,implying the existence of putative receptors and/or binding proteins for this extracellular matrix glycosaminoglycan. Detergent-extracted human fibroblast membrane protein extracts were examined by affinity chromatography in the presence of Ca2+ on chondroitin sulfate immobilized on agarose CL-6B. A 68 kDa and a 35 kDa protein were isolated, sequenced and demonstrated to be annexin 6 and annexin 4, respectively. Next we used A431 cells devoid of annexin 6 expression to verify that annexin 6 is the receptor for this glycosaminoglycan. We confirmed that A431 cells were unable to attach to the chondroitin sulfate substratum and that the stable transfectants expressing annexin 6 conferred the ability to attach to chondroitin sulfate chains. Further, the presence of annexin 6 on the cell surface was confirmed by fluorescence-activated cell sorting analysis using the annexin 6 antibody;annexin 4 is not present on the cell surface. In summary, annexin 6 is a candidate receptor for chondroitin sulfate chains.

scholarly journals Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes

1995 ◽  
Vol 11 (9) ◽  
pp. 319
Author(s):  
S.J. Rogerson ◽  
S.C. Chaiyaroj ◽  
K. Ng ◽  
J.C. Reeder ◽  
G.V. Brown
Keyword(s):  
Plasmodium Falciparum ◽  
Cell Surface ◽  
Chondroitin Sulfate ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
A Cell ◽  
Chondroitin Sulfate A

scholarly journals Cell surface heparan sulfate mediates some adhesive responses to glycosaminoglycan-binding matrices, including fibronectin.

1983 ◽  
Vol 96 (1) ◽  
pp. 112-123 ◽  
Author(s):  
J Laterra ◽  
J E Silbert ◽  
L A Culp
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Cell Attachment ◽  
Heparan Sulfate Proteoglycans ◽  
Cell Surface Receptor ◽  
Platelet Factor ◽  
Microfilament Bundles ◽  
Surface Receptor ◽  
Mediate Cell ◽  
3T3 Cell Lines

Proteins with affinities for specific glycosaminoglycans (GAC's) were used as probes for testing the potential of cell surface GAG's to mediate cell adhesive responses to extracellular matrices (ECM). Plasma fibronectin (FN) and proteins that bind hyaluronate (cartilage proteo-glycan core and link proteins) or heparan sulfate (platelet factor 4 [PF4]) were adsorbed to inert substrata to evaluate attachment and spreading of several 3T3 cell lines. Cells failed to attach to hyaluronate-binding substrata. The rates of attachment on PF4 were identical to those on FN; however, PF4 stimulated formation of broad convex lamellae but not tapered cell processes fibers during the spreading response. PF4-mediated responses were blocked by treating the PF4-adsorbed substratum with heparin (but not chondroitin sulfate), or alternatively the cells with Flavobacter heparinum heparinase (but not chondroitinase ABC). Heparinase treatment did not inhibit cell attachment to FN but did inhibit spreading. Cells spread on PF4 or FN contained similar Ca2+-independent cell-substratum adhesions, as revealed by EGTA-mediated retraction of their substratum-bound processes. Microtubular networks reorganized in cells on PF4 but failed to extend into the broadly spread lamellae, where fine microfilament bundles had developed. Stress fibers, common on FN, failed to develop on PF4. These experiments indicate that (a) heparan sulfate proteoglycans are critical mediators of cell adhesion and heparan sulfate-dependent adhesion via PF4 is comparable in some, but not all, ways to FN-mediated adhesion, (b) the uncharacterized and heparan sulfate-independent "cell surface" receptor for FN permits some but not all aspects of adhesion, and (c) physiologically compatible and complete adhesion of fibroblasts requires binding of extracellular matrix FN to both the unidentified "cell surface" receptor and heparan sulfate proteoglycans.

scholarly journals Enhancing activity and phospholipase A2 activity: two independent activities present in the enhancing factor molecule

1999 ◽  
Vol 340 (1) ◽  
pp. 237-243 ◽  
Author(s):  
Shilpa KADAM ◽  
Rita MULHERKAR
Keyword(s):  
Cell Surface ◽  
Phospholipase A2 ◽  
Cell Surface Receptor ◽  
Egf Receptors ◽  
Pla2 Activity ◽  
Phospholipase Activity ◽  
A431 Cells ◽  
Enhancing Factor ◽  
293 Cells ◽  
Surface Receptor

Enhancing factor (EF), a molecule that increases the binding of epidermal growth factor (EGF) to A431 cells, was first isolated in our laboratory from mouse intestines, and subsequently shown to be a secretory form of phospholipase A2 (PLA2) [Mulherkar, Rao, Wagle, Patki and Deo (1993) Biochem. Biophys. Res. Commun. 195, 1254-1263]. We had proposed earlier that EF increases the binding of EGF by first binding to its own cell-surface receptor [identified as a 100 kDa molecule; Mulherkar and Deo (1986) J. Cell. Physiol. 127, 183-188], and then by creating a binding site for EGF. However, due to its PLA2 activity, there was a possibility that EF, by its phospholipase activity could be unmasking cryptic EGF receptors on the cell surface, thereby increasing the number of binding sites for EGF. To test whether enhancing activity and phospholipase activity are independent of each other, a series of mutations were created using the full-length EF cDNA as a template, expressed in 293 cells and the mutant recombinant proteins checked for EF as well as PLA2 activities. Our studies have shown that one of the mutant EF proteins, lacking PLA2 activity, retains EF activity. This demonstrates unambiguously that EF and PLA2 activities are two independent activities in the same molecule. Mutation in the Ca2+-binding loop resulted in loss of EF activity, thereby demonstrating that EF activity is Ca2+-dependent. The N-terminal region of the EF molecule appears to be crucial for the enhancing activity.

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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