Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2018 Dec;22(12):759-769.
doi: 10.1089/omi.2018.0160.

Proteomic Analysis of the Human Anterior Pituitary Gland

Soujanya D Yelamanchi  1 , Ankur Tyagi  2 , Varshasnata Mohanty  2 , Pinaki Dutta  3 , Márta Korbonits  4 , Sandip Chavan  1 , Jayshree Advani  1   5 , Anil K Madugundu  1   5   6   7 , Gourav Dey  1   5 , Keshava K Datta  1 , M Rajyalakshmi  8 , Nandini A Sahasrabuddhe  1 , Abhishek Chaturvedi  9 , Amit Kumar  10 , Apabrita Ayan Das  11 , Dhiman Ghosh  12 , Gajendra M Jogdand  10 , Haritha H Nair  13 , Keshav Saini  14 , Manoj Panchal  15 , Mansi Ashwinsinh Sarvaiya  16 , Soundappan S Mohanraj  17 , Nabonita Sengupta  18 , Priti Saxena  14 , Pradeep Annamalai Subramani  19 , Pradeep Kumar  20 , Rakhil Akkali  21 , Saraswatipura Vishwabrahmachar Reshma  22 , Ramachandran Sarojini Santhosh  23 , Sangita Rastogi  24 , Sudarshan Kumar  25 , Susanta Kumar Ghosh  19 , Vamshi Krishna Irlapati  26 , Anand Srinivasan  27 , Bishan Das Radotra  28 , Premendu P Mathur  29 , G William Wong  30 , Parthasarathy Satishchandra  31 , Aditi Chatterjee  1 , Harsha Gowda  1 , Anil Bhansali  3 , Akhilesh Pandey  1   5   6   7   32   33   34   35 , Susarla K Shankar  36   37 , Anita Mahadevan  36   37 , T S Keshava Prasad  1   2
Affiliations

Proteomic Analysis of the Human Anterior Pituitary Gland

Soujanya D Yelamanchi et al. OMICS. 2018 Dec.

Abstract

The pituitary function is regulated by a complex system involving the hypothalamus and biological networks within the pituitary. Although the hormones secreted from the pituitary have been well studied, comprehensive analyses of the pituitary proteome are limited. Pituitary proteomics is a field of postgenomic research that is crucial to understand human health and pituitary diseases. In this context, we report here a systematic proteomic profiling of human anterior pituitary gland (adenohypophysis) using high-resolution Fourier transform mass spectrometry. A total of 2164 proteins were identified in this study, of which 105 proteins were identified for the first time compared with high-throughput proteomic-based studies from human pituitary glands. In addition, we identified 480 proteins with secretory potential and 187 N-terminally acetylated proteins. These are the first region-specific data that could serve as a vital resource for further investigations on the physiological role of the human anterior pituitary glands and the proteins secreted by them. We anticipate that the identification of previously unknown proteins in the present study will accelerate biomedical research to decipher their role in functioning of the human anterior pituitary gland and associated human diseases.

Keywords: anterior pituitary; biomarkers; diagnostics; endocrinology; ophthalmology; proteomics.

PubMed Disclaimer

Conflict of interest statement

The authors declare that no conflicting financial interests exist.

Figures

<b>FIG. 1.</b>
FIG. 1.
Schematic representation of anatomical structure and proteomic analysis of human pituitary gland. (A) The detailed structure of human pituitary glands. (B) The methodology used using different fractionation techniques and LC-MS/MS analysis for the identification of proteins from human adenohypophysis. LC-MS/MS, liquid chromatography–mass spectrometry/mass spectrometry.
<b>FIG. 2.</b>
FIG. 2.
Representative MS/MS spectra. MS/MS spectra for peptides corresponding to proteins identified from human pituitary gland—(A) synapsin-1 [SYN1]; (B) aquaporin-1 [AQP1]; (C) calmodulin [CALM3]; and (D) prolyl endopeptidase [PREP]. The fragmented ions are indicated as b, y, and a ions. Internal fragmented ions are also clearly represented.
<b>FIG. 3.</b>
FIG. 3.
GO analysis. (A) Biological processes such as signal transduction, protein metabolism, and transport were the GO terms derived from human adenohypophysis proteins; (B) cellular components, including cytoplasm, nucleus, extracellular and plasma membrane, are illustrated. GO, Gene Ontology.
<b>FIG. 4.</b>
FIG. 4.
Aryl-hydrocarbon signaling pathway. The signaling pathway map exhibiting distinct reactions under receptor activation. Twenty-four proteins were identified to be associated with this pathway, as highlighted.
See this image and copyright information in PMC

References

    1. Allaerts W, and Vankelecom H. (2005). History and perspectives of pituitary folliculo-stellate cell research. Eur J Endocrinol 153, 1–12 - PubMed
    1. Balakrishnan L, Nirujogi RS, Ahmad S, et al. (2014). Proteomic analysis of human osteoarthritis synovial fluid. Clin Proteomics 11, 6. - PMC - PubMed
    1. Cao J, Patisaul HB, and Petersen SL. (2011). Aryl hydrocarbon receptor activation in lactotropes and gonadotropes interferes with estradiol-dependent and -independent preprolactin, glycoprotein alpha and luteinizing hormone beta gene expression. Mol Cell Endocrinol 333, 151–159 - PMC - PubMed
    1. Evans CO, Moreno CS, Zhan X, et al. (2008). Molecular pathogenesis of human prolactinomas identified by gene expression profiling, RT-qPCR, and proteomic analyses. Pituitary 11, 231–245 - PubMed
    1. Gartner W, Lang W, Leutmetzer F, Domanovits H, Waldhausl W, and Wagner L. (2001). Cerebral expression and serum detectability of secretagogin, a recently cloned EF-hand Ca(2+)-binding protein. Cereb Cortex 11, 1161–1169 - PubMed

Publication types