Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1098/rsob.150046 http://scihub22266oqcxt.onion/10.1098/rsob.150046 C4554917!4554917 !26269427     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26269427 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Open+Biol 2015 ; 5 (8 ): ä Nephropedia Template TP {{tp|p=26269427 |t=2015. Cytokines and growth factors cross-link heparan sulfate |pdf=|usr=}}{{26269427 }} gab.com Text Cytokines and growth factors cross-link heparan sulfate JO: Open Biol http://www.kidney.de/pget.php?&tw=1&pmid=26269427 #FOAvip The glycosaminoglycan heparan sulfate (HS), present at the surface of most cells and ubiquitous in extracellular matrix, binds many soluble extracellular signalling molecules such as chemokines and growth factors, and regulates their transport and effector functions. It is, however, unknown whether upon binding HS these proteins can affect the long-range structure of HS. To test this idea, we interrogated a supramolecular model system, in which HS chains grafted to streptavidin-functionalized oligoethylene glycol monolayers or supported lipid bilayers mimic the HS-rich pericellular or extracellular matrix, with the biophysical techniques quartz crystal microbalance (QCM-D) and fluorescence recovery after photobleaching (FRAP). We were able to control and characterize the supramolecular presentation of HS chains--their local density, orientation, conformation and lateral mobility--and their interaction with proteins. The chemokine CXCL12? (or SDF-1?) rigidified the HS film, and this effect was due to protein-mediated cross-linking of HS chains. Complementary measurements with CXCL12? mutants and the CXCL12? isoform provided insight into the molecular mechanism underlying cross-linking. Fibroblast growth factor 2 (FGF-2), which has three HS binding sites, was also found to cross-link HS, but FGF-9, which has just one binding site, did not. Based on these data, we propose that the ability to cross-link HS is a generic feature of many cytokines and growth factors, which depends on the architecture of their HS binding sites. The ability to change matrix organization and physico-chemical properties (e.g. permeability and rigidification) implies that the functions of cytokines and growth factors may not simply be confined to the activation of cognate cellular receptors. Twit Text FOAVip Cytokines and growth factors cross-link heparan sulfate ????Open Biol http://www.kidney.de/pget.php?&tw=1&pmid=26269427 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26269427 #FOAvip English Wikipedia <ref>{{Cite pmid|26269427 }}</ref> Cytokines and growth factors cross-link heparan sulfate #MMPMID26269427 Migliorini E ; Thakar D ; Kühnle J ; Sadir R ; Dyer DP ; Li Y ; Sun C ; Volkman BF ; Handel TM ; Coche-Guerente L ; Fernig DG ; Lortat-Jacob H ; Richter RP Open Biol 2015[Aug]; 5 (8 ): ä PMID26269427 show ga The glycosaminoglycan heparan sulfate (HS), present at the surface of most cells and ubiquitous in extracellular matrix, binds many soluble extracellular signalling molecules such as chemokines and growth factors, and regulates their transport and effector functions. It is, however, unknown whether upon binding HS these proteins can affect the long-range structure of HS. To test this idea, we interrogated a supramolecular model system, in which HS chains grafted to streptavidin-functionalized oligoethylene glycol monolayers or supported lipid bilayers mimic the HS-rich pericellular or extracellular matrix, with the biophysical techniques quartz crystal microbalance (QCM-D) and fluorescence recovery after photobleaching (FRAP). We were able to control and characterize the supramolecular presentation of HS chains--their local density, orientation, conformation and lateral mobility--and their interaction with proteins. The chemokine CXCL12? (or SDF-1?) rigidified the HS film, and this effect was due to protein-mediated cross-linking of HS chains. Complementary measurements with CXCL12? mutants and the CXCL12? isoform provided insight into the molecular mechanism underlying cross-linking. Fibroblast growth factor 2 (FGF-2), which has three HS binding sites, was also found to cross-link HS, but FGF-9, which has just one binding site, did not. Based on these data, we propose that the ability to cross-link HS is a generic feature of many cytokines and growth factors, which depends on the architecture of their HS binding sites. The ability to change matrix organization and physico-chemical properties (e.g. permeability and rigidification) implies that the functions of cytokines and growth factors may not simply be confined to the activation of cognate cellular receptors. |Chemokine CXCL12/chemistry/metabolism [MESH] |Cytokines/chemistry/*metabolism [MESH] |Extracellular Matrix/chemistry/metabolism [MESH] |Glycosaminoglycans/chemistry/metabolism [MESH] |Heparitin Sulfate/*chemistry/metabolism [MESH] |Humans [MESH] |Intercellular Signaling Peptides and Proteins/*chemistry/metabolism [MESH] |Models, Molecular [MESH] |Molecular Conformation [MESH]Cytokines and growth factors cross-link heparan sulfate (epmc).pdf DeepDyve Pubget Overpricing