Remarkable temporal stability of high-abundance human plasma proteins assessed by targeted mass spectrometry

2012 ◽  
Vol 6 (11-12) ◽  
pp. 626-634 ◽  
Author(s):  
Sarah A. Randall ◽  
Matthew J. McKay ◽  
Dana Pascovici ◽  
Kate Mahon ◽  
Lisa Horvath ◽  
...  
2016 ◽  
Author(s):  
Ole Kristian Brandtzaeg ◽  
Elin Johnsen ◽  
Hanne Roberg-Larsen ◽  
Knut Fredrik Seip ◽  
Siri Leknes ◽  
...  

Current approaches to measuring the cyclic peptide oxytocin in plasma/serum are associated with poor selectivity and/or inadequate sensitivity. We here describe a high performance nano liquid chromatography-mass spectrometry platform for measuring OT in human plasma/serum. The platform is extremely robust, allowing laborious sample clean-up steps to be omitted. OT binds strongly to plasma proteins, but a reduction/alkylation procedure breaks this bond, allowing ample detection of total OT. The method showed excellent quantitation properties, and was used to determine total OT levels to 0.5-1.2 ng/mL (evaluated with human plasma and cord serum). The method is compatible with accessible mass spectrometry instrumentation, finally allowing selective and easily comparable oxytocin measurements.


Author(s):  
Licia Carla da Silva Costa ◽  
Daniel Martins de Souza ◽  
Sheila Garcia Rosa ◽  
Paulo A. Baldasso ◽  
Johann Steiner

The proteome of blood plasma is an interesting source of biomarkers and a potential way to improve treatment outcomes in psychiatric disorders. Respire that, its wide dynamic concentration range makes reducing its complexity necessary. Thus, in proteomic studies, a few of the most abundant proteins are depleted and normally discarded. This high-abundance fraction, called the depletome, however, is a source of potential biomarkers due to nonspecific bindings with low abundance proteins. In this work, we aimed to characterize the high-abundance fraction using a shotgun mass spectrometry approach. These proteins show the importance of studying depletome proteins in the quest for biomarkers.


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