scholarly journals Differentiation of Four Tuna Species by Two-Dimensional Electrophoresis and Mass Spectrometric Analysis

10.5772/29679 ◽  
2012 ◽  
Author(s):  
Tiziana Pepe ◽  
Marina Ceruso ◽  
Andrea Carpentieri ◽  
Iole Ventrone ◽  
Angela Amoresano ◽  
...  
Keyword(s):  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

scholarly journals Immunoglobulin G Subclasses and Prolactin (PRL) Isoforms in Macroprolactinemia Due to Anti-PRL Autoantibodies

2005 ◽  
Vol 90 (5) ◽  
pp. 3036-3044 ◽  
Author(s):  
Naoki Hattori ◽  
Katsuji Ikekubo ◽  
Yasuhisa Nakaya ◽  
Kaori Kitagawa ◽  
Chiyoko Inagaki
Keyword(s):  
Mass Spectrometry ◽  
Mass Spectrometric ◽  
Igg Subclasses ◽  
Two Dimensional ◽  
Human Pituitary ◽  
Two Dimensional Electrophoresis ◽  
Antigen Stimulation ◽  
Immunoglobulin G Subclasses ◽  
Specific Igg ◽  
Dimensional Electrophoresis

Although macroprolactinemia due to antiprolactin (anti-PRL) autoantibodies is not uncommon among hyperprolactinemic patients, the pathogenesis of such macroprolactinemia is still unknown. We examined IgG subclasses of anti-PRL autoantibodies by enzyme immunoassay, and PRL phosphorylation and isoforms by Western blotting, mass spectrometry, and two-dimensional electrophoresis in six patients with anti-PRL autoantibodies and in 29 controls. PRL-specific IgG subclasses in patients with anti-PRL autoantibodies were heterogeneous, but five of six patients showed IgG4 predominance, which is known to be produced by chronic antigen stimulation. Western blot and mass spectrometric analyses revealed that human pituitary PRL was phosphorylated at serine 194 and serine 163, whereas serine 163 in serum PRL was dephosphorylated. On two-dimensional electrophoresis, serum PRL mainly consisted of isoform with isoelectric point (pI) 6.58 in control hyperprolactinemic patients, whereas acidic isoforms (pIs 6.43 and 6.29) were also observed in patients with anti-PRL autoantibodies. Our data first demonstrate that human pituitary PRL is serine phosphorylated and partially dephosphorylated in serum, and suggest that the acidic isoforms may give rise to chronic antigen stimulation in patients with anti-PRL autoantibodies.

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