scholarly journals Cell-Surface Protein Profiling Identifies Distinctive Markers of Progenitor Cells in Human Skeletal Muscle

2016 ◽  
Vol 7 (2) ◽  
pp. 263-278 ◽  
Author(s):  
Akiyoshi Uezumi ◽  
Masashi Nakatani ◽  
Madoka Ikemoto-Uezumi ◽  
Naoki Yamamoto ◽  
Mitsuhiro Morita ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Surface ◽  
Progenitor Cells ◽  
Human Skeletal Muscle ◽  
Surface Protein ◽  
Protein Profiling ◽  
Cell Surface Protein

scholarly journals Comprehensive Cell Surface Protein Profiling Identifies Specific Markers of Human Naive and Primed Pluripotent States

2017 ◽  
Vol 20 (6) ◽  
pp. 874-890.e7 ◽  
Author(s):  
Amanda J. Collier ◽  
Sarita P. Panula ◽  
John Paul Schell ◽  
Peter Chovanec ◽  
Alvaro Plaza Reyes ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Protein ◽  
Protein Profiling ◽  
Cell Surface Protein

Immunogold and immunoblot studies on a cell surface protein found in primary mesenchyme cells and in the cortical secretory vesicles of the sea urchin egg

1987 ◽  
Vol 45 ◽  
pp. 832-833
Author(s):  
G.L. Decker ◽  
M.C. Valdizan
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Surface Protein ◽  
Egg Cell ◽  
Secretory Vesicles ◽  
Cell Surface Protein ◽  
Surface Complexes ◽  
Mesenchyme Cells ◽  
Lowicryl K4m ◽  
Primary Mesenchyme Cells

A monoclonal antibody designated MAb 1223 has been used to show that primary mesenchyme cells of the sea urchin embryo express a 130-kDa cell surface protein that may be directly involved in Ca2+ uptake required for growth of skeletal spicules. Other studies from this laboratory have shown that the 1223 antigen, although in relatively low abundance, is also expressed on the cell surfaces of unfertilized eggs and on the majority of blastomeres formed prior to differentiation of the primary mesenchyme cells.We have studied the distribution of 1223 antigen in S. purpuratus eggs and embryos and in isolated egg cell surface complexes that contain the cortical secretory vesicles. Specimens were fixed in 1.0% paraformaldehyde and 1.0% glutaraldehyde and embedded in Lowicryl K4M as previously reported. Colloidal gold (8nm diameter) was prepared by the method of Mulpfordt.

Effect of insulin on GLUT4 cell surface content and turnover rate in human skeletal muscle as measured by the exofacial bis-mannose photolabeling technique

Diabetes ◽  
1997 ◽  
Vol 46 (12) ◽  
pp. 1965-1969 ◽  
Author(s):  
S. Lund ◽  
G. D. Holman ◽  
J. R. Zierath ◽  
J. Rincon ◽  
L. A. Nolte ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Surface ◽  
Human Skeletal Muscle ◽  
Turnover Rate ◽  
Surface Content

scholarly journals Monomer–dimer dynamics and distribution of GPI-anchored uPAR are determined by cell surface protein assemblies

2007 ◽  
Vol 179 (5) ◽  
pp. 1067-1082 ◽  
Author(s):  
Valeria R. Caiolfa ◽  
Moreno Zamai ◽  
Gabriele Malengo ◽  
Annapaola Andolfo ◽  
Chris D. Madsen ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Cell Surface ◽  
Plasminogen Activator ◽  
Fluorescent Protein ◽  
Surface Protein ◽  
Basal Membrane ◽  
Membrane Dynamics ◽  
Live Cells ◽  
Cell Surface Protein ◽  
Protein Assemblies

To search for functional links between glycosylphosphatidylinositol (GPI) protein monomer–oligomer exchange and membrane dynamics and confinement, we studied urokinase plasminogen activator (uPA) receptor (uPAR), a GPI receptor involved in the regulation of cell adhesion, migration, and proliferation. Using a functionally active fluorescent protein–uPAR in live cells, we analyzed the effect that extracellular matrix proteins and uPAR ligands have on uPAR dynamics and dimerization at the cell membrane. Vitronectin directs the recruitment of dimers and slows down the diffusion of the receptors at the basal membrane. The commitment to uPA–plasminogen activator inhibitor type 1–mediated endocytosis and recycling modifies uPAR diffusion and induces an exchange between uPAR monomers and dimers. This exchange is fully reversible. The data demonstrate that cell surface protein assemblies are important in regulating the dynamics and localization of uPAR at the cell membrane and the exchange of monomers and dimers. These results also provide a strong rationale for dynamic studies of GPI-anchored molecules in live cells at steady state and in the absence of cross-linker/clustering agents.

scholarly journals Cell-surface remodelling during mammalian erythropoiesis

1982 ◽  
Vol 208 (1) ◽  
pp. 239-242 ◽  
Author(s):  
D C Wraith ◽  
C J Chesterton
Keyword(s):  
Surface Modification ◽  
Membrane Proteins ◽  
Cell Surface ◽  
Protein Composition ◽  
Surface Protein ◽  
Current Evidence ◽  
Cell Surface Protein ◽  
Erythroid Cells ◽  
Selective Loss ◽  
Before And After

Current evidence suggests that the major cell-surface modification occurring during mammalian erythropoiesis could be generated by two separate mechanisms: either selective loss of membrane proteins during enucleation or endocytosis at the subsequent reticulocyte and erythrocyte stages. The former idea was tested by collecting developing rabbit erythroid cells before and after the enucleation step and comparing their cell-surface protein composition via radiolabelling and electrophoresis. Few changes were observed. Our data thus lend support to the endocytosis mechanism.

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