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10.1242/jcs.109.2.301 http://scihub22266oqcxt.onion/10.1242/jcs.109.2.301 8838653!ä!8838653 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Cell+Sci 1996 ; 109 ( Pt 2) (ä): 301-7 Nephropedia Template TP {{tp|p=8838653|t=1996. Bone-resorbing osteoclasts reveal a dynamic division of basal plasma membrane into two different domains |pdf=|usr=}}{{8838653}} gab.com Text Bone-resorbing osteoclasts reveal a dynamic division of basal plasma membrane into two different domains JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=8838653 #FOAvip Bone-resorbing multinucleate osteoclasts exhibit a ruffled border membrane apposing the bone and a basal membrane contacting the circulation. A junctional complex called the sealing zone separates these two membrane domains, but the defined nature of these membrane domains has remained obscure. We now show, using enveloped viral glycoproteins and lectins as tools, that osteoclasts exhibit a novel membrane domain in the basal surface when they are polarized for resorption. Influenza haemagglutinin, which is apically targeted in epithelial cells, is targeted to a restricted area at the top of the basal surface, while vesicular stomatitis virus G-protein which is basolaterally targeted in epithelia, occupies the rest of the basal surface. Neither of these viral glycoproteins is gathered to the ruffled border nor sealing zone area, but they share in a specific way the basal surface. To show that the division of basal membrane into two different domains also occurs in non-infected cells, we have analyzed the distribution of receptors for these viruses and binding sites of some lectins. Both of these methods show that also some endogenous proteins are located in different domains in the basal surface in active osteoclasts. We also show that these two different membrane domains can be distinguished in scanning electron microscopy level due to the villus appearance of the central basal domain. Twit Text FOAVip Bone-resorbing osteoclasts reveal a dynamic division of basal plasma membrane into two different domains ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=8838653 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=8838653 #FOAvip English Wikipedia <ref>{{Cite pmid|8838653}}</ref> Bone-resorbing osteoclasts reveal a dynamic division of basal plasma membrane into two different domains #MMPMID8838653 Salo J; Metsikko K; Palokangas H; Lehenkari P; Vaananen HK J Cell Sci 1996[Feb]; 109 ( Pt 2) (ä): 301-7 PMID8838653show ga Bone-resorbing multinucleate osteoclasts exhibit a ruffled border membrane apposing the bone and a basal membrane contacting the circulation. A junctional complex called the sealing zone separates these two membrane domains, but the defined nature of these membrane domains has remained obscure. We now show, using enveloped viral glycoproteins and lectins as tools, that osteoclasts exhibit a novel membrane domain in the basal surface when they are polarized for resorption. Influenza haemagglutinin, which is apically targeted in epithelial cells, is targeted to a restricted area at the top of the basal surface, while vesicular stomatitis virus G-protein which is basolaterally targeted in epithelia, occupies the rest of the basal surface. Neither of these viral glycoproteins is gathered to the ruffled border nor sealing zone area, but they share in a specific way the basal surface. To show that the division of basal membrane into two different domains also occurs in non-infected cells, we have analyzed the distribution of receptors for these viruses and binding sites of some lectins. Both of these methods show that also some endogenous proteins are located in different domains in the basal surface in active osteoclasts. We also show that these two different membrane domains can be distinguished in scanning electron microscopy level due to the villus appearance of the central basal domain. |*Membrane Glycoproteins[MESH] |Animals[MESH] |Binding Sites[MESH] |Bone Resorption/*metabolism[MESH] |Cell Membrane/metabolism/ultrastructure[MESH] |Cell Polarity[MESH] |Cells, Cultured[MESH] |Hemagglutinin Glycoproteins, Influenza Virus/metabolism[MESH] |Lectins/metabolism[MESH] |Microscopy, Electron, Scanning[MESH] |Osteoclasts/cytology/*metabolism/ultrastructure[MESH] |Rats[MESH] |Receptors, Virus/metabolism[MESH]Bone-resorbing osteoclasts reveal a dynamic division of basal plasma m(epmc).pdf DeepDyve Pubget Overpricing