The Pituitary Gland and Mass Spectrometry An Endocrinologists Perspective

The pituitary gland and mass spectrometry an endocrinologist s perspective 

In 1970, Guillemin and co-workers used MS to determine the amino acid sequence of the ovine thyrotrophin-releasing hormone (TRH), the first of the hypothalamic hypophysiohophic peptides to be discovered [23], Ten years earlier, the 

From a pathological perspective, the detailed MS study of pituitary tumors can be used to determine whether proteins that regulate cell growth or hormone secretion are over- or under-expressed in neoplastic tissue, and whether they can be used as blood biomarkers of tumor mass and activity. For example, secreta-gogin, which is important for pancreatic 8-cell insulin secretion, is a newly discovered protein in the normal adenohypophysis it and its mRNA are underexpressed in null cell/gonadotroph pituitary adenomas [17]. Further studies are needed to determine whether secretagogin plays a physiological role in pituitary hormone secretion. 

Proteomics is a multidisciplinary study that includes protein chemistry, MS, chromatography, bioinformatics, etc. The basic proteomics techniques are grouped into two types protein separation and protein identification. 2DGE and LC are the main protein- and peptide-separation techniques, respectively. MS coupled with bioinformatics analysis identifies proteins. Two types of proteomics systems (LC, gel) are used to analyze human pituitary tissues to obtain tumor-related proteins and PTMs. 

LC-separated peptides is used to determine the DEPs and the MS/MS data are used to search a protein database for protein identification. 

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