This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Isacke, C M
Right arrow Articles by Trowbridge, I S
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Isacke, C M
Right arrow Articles by Trowbridge, I S

 Previous Article  |  Next Article 

Mol Cell Biol. 1990 June; 10(6): 2606-2618

p180, a novel recycling transmembrane glycoprotein with restricted cell type expression.

C M Isacke, P van der Geer, T Hunter and I S Trowbridge

Department of Biochemistry, Imperial College of Science and Technology, University of London, England.

ABSTRACT

A 180-kilodalton (kDa) protein (p180) was identified among the antigens for a panel of monoclonal antibodies raised against human fibroblast cell surface proteins. Binding studies with 125I-Fab' fragments of an anti-p180 monoclonal antibody demonstrated that 10 to 30% of p180 was located on the plasma membrane and that the remaining 70 to 90% was on intracellular membranes. p180 was rapidly internalized from the cell surface at 37 degrees C, and kinetic analyses indicated that this was a constitutive process followed by the recycling of p180 back to the plasma membrane. Morphological studies demonstrated that on the cell surface p180 was concentrated in coated pits, whereas inside the cell it was found in endosomes as suggested by its colocalization with the transferrin receptor. Immunoblot analysis with a polyclonal antiserum raised against purified human protein showed that p180 has a restricted distribution with expression at high levels in fibroblast cultures and in tissues containing cells of mesodermal origin. A biochemical characterization of p180 showed it to be a transmembrane glycoprotein with an extracellular domain, which consists of approximately 30 kDa of complex oligosaccharides attached to at least 45 kDa of the protein core. The cytoplasmic domain of p180 was found to contain a serine residue(s) that was phosphorylated both in vivo and in vitro by activated protein kinase C. p180 was purified by subjecting solubilized membrane proteins from a human osteosarcoma cell line to immunoaffinity chromatography and gel filtration. The N-terminal sequence information obtained from the purified protein showed no homology to other known proteins. It was concluded that p180 may be a novel recycling receptor which is highly restricted in its expression to fibroblastlike cells.

Mol Cell Biol. 1990 June; 10(6): 2606-2618




This article has been cited by other articles:

  • Wienke, D., Davies, G. C., Johnson, D. A., Sturge, J., Lambros, M. B.K., Savage, K., Elsheikh, S. E., Green, A. R., Ellis, I. O., Robertson, D., Reis-Filho, J. S., Isacke, C. M. (2007). The Collagen Receptor Endo180 (CD280) Is Expressed on Basal-like Breast Tumor Cells and Promotes Tumor Growth In vivo. Cancer Res. 67: 10230-10240 [Abstract] [Full Text]  
  • Madsen, D. H., Engelholm, L. H., Ingvarsen, S., Hillig, T., Wagenaar-Miller, R. A., Kjoller, L., Gardsvoll, H., Hoyer-Hansen, G., Holmbeck, K., Bugge, T. H., Behrendt, N. (2007). Extracellular Collagenases and the Endocytic Receptor, Urokinase Plasminogen Activator Receptor-associated Protein/Endo180, Cooperate in Fibroblast-mediated Collagen Degradation. J. Biol. Chem. 282: 27037-27045 [Abstract] [Full Text]  
  • Sturge, J., Todd, S. K., Kogianni, G., McCarthy, A., Isacke, C. M. (2007). Mannose receptor regulation of macrophage cell migration. J. Leukoc. Biol. 82: 585-593 [Abstract] [Full Text]  
  • Sturge, J., Wienke, D., Isacke, C. M. (2006). Endosomes generate localized Rho-ROCK-MLC2-based contractile signals via Endo180 to promote adhesion disassembly. JCB 175: 337-347 [Abstract] [Full Text]  
  • Sly, W. S., Vogler, C., Grubb, J. H., Levy, B., Galvin, N., Tan, Y., Nishioka, T., Tomatsu, S. (2006). Enzyme therapy in mannose receptor-null mucopolysaccharidosis VII mice defines roles for the mannose 6-phosphate and mannose receptors. Proc. Natl. Acad. Sci. USA 103: 15172-15177 [Abstract] [Full Text]  
  • Thomas, E. K., Nakamura, M., Wienke, D., Isacke, C. M., Pozzi, A., Liang, P. (2005). Endo180 Binds to the C-terminal Region of Type I Collagen. J. Biol. Chem. 280: 22596-22605 [Abstract] [Full Text]  
  • Alam, T. N., O'Hare, M. J., Laczko, I., Freeman, A., Al-Beidh, F., Masters, J. R., Hudson, D. L. (2004). Differential Expression of CD44 During Human Prostate Epithelial Cell Differentiation. J. Histochem. Cytochem. 52: 1083-1090 [Abstract] [Full Text]  
  • Sturge, J., Wienke, D., East, L., Jones, G. E., Isacke, C. M. (2003). GPI-anchored uPAR requires Endo180 for rapid directional sensing during chemotaxis. JCB 162: 789-794 [Abstract] [Full Text]  
  • Wienke, D., MacFadyen, J. R., Isacke, C. M. (2003). Identification and Characterization of the Endocytic Transmembrane Glycoprotein Endo180 as a Novel Collagen Receptor. Mol. Biol. Cell 14: 3592-3604 [Abstract] [Full Text]  
  • East, L., Rushton, S., Taylor, M. E., Isacke, C. M. (2002). Characterization of Sugar Binding by the Mannose Receptor Family Member, Endo180. J. Biol. Chem. 277: 50469-50475 [Abstract] [Full Text]  
  • Howard, M. J., Isacke, C. M. (2002). The C-type Lectin Receptor Endo180 Displays Internalization and Recycling Properties Distinct from Other Members of the Mannose Receptor Family. J. Biol. Chem. 277: 32320-32331 [Abstract] [Full Text]  
  • Sheikh, H, Yarwood, H, Ashworth, A, Isacke, C. (2000). Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor. J. Cell Sci. 113: 1021-1032 [Abstract]  
  • Hudson, D., Sleeman, J, Watt, F. (1995). CD44 is the major peanut lectin-binding glycoprotein of human epidermal keratinocytes and plays a role in intercellular adhesion. J. Cell Sci. 108: 1959-1970 [Abstract]  
  • Isacke, C. (1994). The role of the cytoplasmic domain in regulating CD44 function. J. Cell Sci. 107: 2353-2359  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»