Mouse anterior pituitary gland

Analysis by ion trap mass spectrometry

Charles A. Blake, David G. Kakhniashvili, Steven Goodman

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

We investigated the proteome of the anterior pituitary gland (AP) in a species in which the genome has been sequenced. Subcellular fractions of APs from 2-month-old male mice were prepared for protein denaturation, treatment with trypsin and analyses utilizing micro liquid chromatography tandem mass spectrometry and the database search software SEQUEST. In the nuclear, non-nuclear 100,000 g and cytosolic fractions, we identified 49, 36 and 68 different proteins, respectively. A total of 115 distinct proteins were detected. We identified growth hormone, prolactin, pro-opiomelanocortin, the α-subunit for the glycoprotein hormones, and luteinizing hormone-β. Groups of other identified proteins included hormone-processing, secretion granule-associated, non-hormonal endoplasmic reticulum-associated, calcium-binding, protein kinase C-associated, histones, non-histone chromosomal, other RNA-binding, heterogeneous nuclear ribonucleoproteins, splicing factors, helicases, lamins, ribosomal, microtubule-associated, microfilament-associated, adenosine triphosphate- and guanosine triphosphate-associated, tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation, enzymes in glycolysis and the tricarboxylic and urea cycles and the pentose phosphate path, heat-shock, glutathione-associated, peroxidases, ubiquitin-associated, catabolic, protease inhibitors, other, and blood proteins. The 115 proteins reported in this study and the 145 proteins reported in a previous study on the AP of the adult male Golden Syrian hamster are compared and form a foundation for defining the proteome in normal adult male AP.

Original languageEnglish (US)
Pages (from-to)229-243
Number of pages15
JournalNeuroendocrinology
Volume81
Issue number4
DOIs
StatePublished - Oct 10 2005
Externally publishedYes

Fingerprint

Anterior Pituitary Gland
Mass Spectrometry
Ions
Proteome
Proteins
Hormones
Lamins
Heterogeneous-Nuclear Ribonucleoproteins
Tryptophan Hydroxylase
Pentoses
Protein Denaturation
Nuclear RNA
Pro-Opiomelanocortin
Calcium-Binding Proteins
Enzyme Activation
Subcellular Fractions
Mesocricetus
Tyrosine 3-Monooxygenase
Glycolysis
Luteinizing Hormone

All Science Journal Classification (ASJC) codes

  • Endocrinology, Diabetes and Metabolism
  • Endocrinology
  • Endocrine and Autonomic Systems
  • Cellular and Molecular Neuroscience

Cite this

Mouse anterior pituitary gland : Analysis by ion trap mass spectrometry. / Blake, Charles A.; Kakhniashvili, David G.; Goodman, Steven.

In: Neuroendocrinology, Vol. 81, No. 4, 10.10.2005, p. 229-243.

Research output: Contribution to journalArticle

Blake, Charles A. ; Kakhniashvili, David G. ; Goodman, Steven. / Mouse anterior pituitary gland : Analysis by ion trap mass spectrometry. In: Neuroendocrinology. 2005 ; Vol. 81, No. 4. pp. 229-243.
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