Chondroitin Sulfate Glycosaminoglycans Regulate Distinct Cell Surface Receptor-Mediated Neuronal Functions

2021 ◽  
Vol 33 (191) ◽  
pp. E11-E16
Author(s):  
Tadahisa Mikami ◽  
Hiroshi Kitagawa
Keyword(s):  
Cell Surface ◽  
Chondroitin Sulfate ◽  
Cell Surface Receptor ◽  
Distinct Cell ◽  
Surface Receptor ◽  
Neuronal Functions

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 Heparan Sulfate-Independent Cell Binding and Infection with Furin-Precleaved Papillomavirus Capsids

2008 ◽  
Vol 82 (24) ◽  
pp. 12565-12568 ◽  
Author(s):  
Patricia M. Day ◽  
Douglas R. Lowy ◽  
John T. Schiller
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Cell Surface Receptor ◽  
Furin Cleavage ◽  
Human Papillomavirus Type 16 ◽  
Papillomavirus Infection ◽  
Distinct Cell ◽  
Subsequent Step ◽  
Surface Receptor ◽  
Infected Cells

ABSTRACT Papillomavirus infection normally involves virion binding to cell surface heparan sulfate proteoglycans (HSPGs). However, we found that human papillomavirus type 16 pseudovirions efficiently bound and infected cells lacking HSPGs if their L2 capsid protein was precleaved by furin, a cellular protease required for infection. The inability of pseudovirions to efficiently bind and infect cultured primary keratinocytes was also overcome by furin precleavage, suggesting that the defect involves altered HSPG modification. We conclude that the primary function of HSPG binding is to enable cell surface furin cleavage of L2 and that binding to a distinct cell surface receptor(s) is a subsequent step of papillomavirus infection.

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.

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

Inhibition of rat ventricular automaticity by adenosine

1985 ◽  
Vol 248 (6) ◽  
pp. H907-H913 ◽  
Author(s):  
L. J. Heller ◽  
R. A. Olsson
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Chronotropic Effect ◽  
Surface Receptors ◽  
Adenosine Concentration ◽  
Surface Receptor ◽  
Ventricular Automaticity ◽  
Beating Rate ◽  
Chronotropic Effects ◽  
Developed Pressure

This study was designed to characterize adenosine's negative chronotropic effect on ventricular pacemakers. The spontaneous beating rate of isolated, isovolumic rat ventricular preparations perfused with Krebs-Henseleit solution decreased as the adenosine concentration was increased [log M effective concentration 50% (EC50) = -5.22 +/- 0.17]. The lack of effect of propranolol or atropine on this adenosine response eliminates the involvement of endogenous neurotransmitters. Support for the involvement of an external cell surface receptor was provided by findings that theophylline and 8-(4-sulfophenyl)theophylline, an analogue thought to act solely at the cell surface, significantly increased the adenosine log M EC50 to -3.94 +/- 0.22 and -3.61 +/- 0.22, respectively. An increase in spontaneous beating rate induced by theophylline, but not by its analogue, was blocked by the addition of propranolol. The relative chronotropic potency of the adenosine analogues R-PIA, S-PIA, and NECA suggests that the cell surface receptors may be of the Ri type. The negative chronotropic effects of adenosine and its analogues occurred at concentrations that had no effect on the developed pressure of the paced preparation. Electrocardiographic evaluations indicate that at high agonist concentrations, there was an abrupt alteration in electrical properties of the preparation, which could be blocked by theophylline and its analogue.

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