Elevated plasma cell membrane glycoprotein levels and diminished insulin receptor autophosphorylation in obese, insulin-resistant rhesus monkeys

Metabolism ◽  
2002 ◽  
Vol 51 (4) ◽  
pp. 465-470 ◽  
Author(s):  
Celia Pender ◽  
Heidi K. Ortmeyer ◽  
Barbara C. Hansen ◽  
Ira D. Goldfine ◽  
Jack F. Youngren
Keyword(s):  
Cell Membrane ◽  
Insulin Receptor ◽  
Plasma Cell ◽  
Rhesus Monkeys ◽  
Membrane Glycoprotein ◽  
Elevated Plasma ◽  
Insulin Resistant

The 121Q allele of the plasma cell membrane glycoprotein 1 gene predisposes to polycystic ovary syndrome

2004 ◽  
Vol 82 (3) ◽  
pp. 743-745 ◽  
Author(s):  
Seppo Heinonen ◽  
Seija Korhonen ◽  
Seppo Helisalmi ◽  
Riitta Koivunen ◽  
Juha S. Tapanainen ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Polycystic Ovary Syndrome ◽  
Plasma Cell ◽  
Polycystic Ovary ◽  
Membrane Glycoprotein ◽  
Ovary Syndrome

The K121Q polymorphism in the plasma cell membrane glycoprotein 1 gene predisposes to early myocardial infarction

2002 ◽  
Vol 80 (12) ◽  
pp. 791-795 ◽  
Author(s):  
Georg Endler ◽  
Christine Mannhalter ◽  
Heike Sunder-Plassmann ◽  
Martin Schillinger ◽  
Alexandra Klimesch ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Cell Membrane ◽  
Plasma Cell ◽  
Membrane Glycoprotein

scholarly journals Divalent cations stabilize the conformation of plasma cell membrane glycoprotein PC-1 (alkaline phosphodiesterase I)

1994 ◽  
Vol 304 (1) ◽  
pp. 75-80 ◽  
Author(s):  
S I Belli ◽  
A Sali ◽  
J W Goding
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Membrane ◽  
Plasma Cell ◽  
Polyclonal Antibodies ◽  
Divalent Cations ◽  
Enzymic Activity ◽  
Membrane Glycoprotein ◽  
Sequence Motifs ◽  
Intact Cells ◽  
Ef Hand

The plasma cell-membrane glycoprotein PC-1 is an ectoenzyme with alkaline phosphodiesterase I/5′-nucleotide phosphodiesterase (EC 3.1.4.1) and nucleotide pyrophosphatase (EC 3.6.1.9) activities. It contains sequence motifs which closely match the consensus EF-hand (helix-loop-helix) Ca(2+)-binding regions of parvalbumin, troponin-C and calmodulin, and its enzymic activity is increased in the presence of divalent cations and decreased in the presence of chelating agents. We have undertaken experiments to determine whether divalent cations affect the conformation of the PC-1 protein, as assessed by their effect on thermal stability, resistance to proteolysis and binding of polyclonal antibodies to the whole native protein and monoclonal antibodies to a putative Ca(2+)-binding region. Divalent cations were found to protect solubilized PC-1 against thermal denaturation and proteolysis. They also stabilized PC-1 on intact cells; this form was much more resistant to proteolysis than Triton X-100 solubilized PC-1. Ca2+, Mg2+ and Zn2+ ions were equally effective. Monoclonal antibodies to the bacterially expressed C-terminal EF-hand homology region only bound to mammalian PC-1 in the absence of Ca2+. In contrast, the great majority of polyclonal antibodies to native PC-1 bound regardless of whether Ca2+ was present or not, but with increased binding when Ca2+ was present. These results provide evidence that divalent cations bind to PC-1 and stabilize its conformation.

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