LEUKAEMIA INHIBITORY FACTOR AND INTERLEUKIN 6 INHIBIT SECRETION OF PROLACTIN AND GROWTH HORMONE BY RAT PITUITARY MtT/SM CELLS

Tomida, Mikio; Yoshida, Urara; Mogi, Chihiro; Maruyama, Minoru; Goda, Hideki; Hatta, Yuki; Inoue, Kinji

doi:10.1006/cyto.2001.0874

Cited by 20 publications

(10 citation statements)

References 25 publications

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“…Among the particularly interesting proteins are the 29-amino acid CRISPP peptide (cancer-associated serine protease protecting peptide), isolated earlier from plasma of cancer patients (24), a proteolytic fragment of the mut S homolog that has been associated with hereditary non-polyposis colon cancer (25), glioma pathogenesis-related protein (26), which is normally overexpressed in brain tumors, the proto-oncogene c-ets-1 (27), oncogene lbc (28), and the novel oncogene DJ1, which has been shown to interact with c-myc and also transform NIH 3T3 cells in cooperation with ras (29). In addition proteins such as the angiotensinogen precursor, the prostatic tumor suppressor Kangai-1 antigen (30), and the cytokines interleukin-15, and leukemia inhibitory factor (31), which is present in serum at a concentration below 10 pg/ml (32), were also identified. * This project has been funded in whole or in part with Federal funds from the National Cancer Institute, National Institutes of Health, under Contract No.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Low Molecular Weight Human Serum Proteome

Tirumalai

Chan

Prieto

et al. 2003

Molecular & Cellular Proteomics

788

742

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Serum potentially carries an archive of important histological information whose determination could serve to improve early disease detection. The analysis of serum, however, is analytically challenging due to the high dynamic concentration range of constituent protein/peptide species, necessitating extensive fractionation prior to mass spectrometric analyses. The low molecular weight (LMW) serum proteome is that protein/peptide fraction from which high molecular weight proteins, such as albumin, immunoglobulins, transferrin, and lipoproteins, have been removed. This LMW fraction is made up of several classes of physiologically important proteins such as cytokines, chemokines, peptide hormones, as well as proteolytic fragments of larger proteins. Centrifugal ultrafiltration of serum was used to remove the large constituent proteins resulting in the enrichment of the LMW proteins/ peptides. Because albumin is known to bind and transport small molecules and peptides within the circulatory system, the centrifugal ultrafiltration was conducted under solvent conditions effecting the disruption of protein-protein interactions. The LMW serum proteome sample was digested with trypsin, fractionated by strong cation exchange chromatography, and analyzed by microcapillary reversed-phase liquid chromatography coupled on-line with electrospray ionization tandem mass spectrometry. Analysis of the tandem mass spectra resulted in the identification of over 340 human serum proteins; however, not a single peptide from serum albumin was observed. The large number of proteins identified demonstrates the efficacy of this method for the removal of large abundant proteins and the enrichment of the LMW serum proteome.

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Section: Discussionmentioning

confidence: 99%

Characterization of the Low Molecular Weight Human Serum Proteome

Tirumalai

Chan

Prieto

et al. 2003

Molecular & Cellular Proteomics

788

742

View full text Add to dashboard Cite

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“…Additional actions of OSM and LIF include the induction of hepatocyte acute phase protein production (Baumann & Wong 1989, Richards et al 1997) and the stimulation of various haematopoietic lineages, mostly in concert with other growth factors (Metcalf 2003, Tanaka & Miyajima 2003. LIF and OSM also stimulate the production of adrenocorticotrophic hormone (ACTH) production in the pituitary (Kim et al 2000, Chesnokova & Melmed 2002, Auernhammer et al 2004 and affect the secretion of PRL and GH (Tomida et al 2001). Moreover, LIF is required for blastocyst implantation (Chen et al 2000, Song et al 2000 and exerts a multitude of proliferative and differentiating effects on various neuronal cell populations (Metcalf 2003).…”

Section: Lif and Osmmentioning

confidence: 99%

Phylogeny and evolution of class-I helical cytokines

Huising¹,

Kruiswijk

Flik³

2006

Journal of Endocrinology

193

136

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The class-I helical cytokines constitute a large group of signalling molecules that play key roles in a plethora of physiological processes including host defence, immune regulation, somatic growth, reproduction, food intake and energy metabolism, regulation of neural growth and many more. Despite little primary amino acid sequence similarity, the view that all contemporary class-I helical cytokines have expanded from a single ancestor is widely accepted, as all class-I helical cytokines share a similar three-dimensional fold, signal via related class-I helical cytokine receptors and activate similar intracellular signalling cascades. Virtually all of our knowledge on class-I helical cytokine signalling derives from research on primate and rodent species. Information on the presence, structure and function of class-I helical cytokines in non-mammalian vertebrates and non-vertebrates is fragmentary. Consequently, our ideas about the evolution of this versatile multigene family are often based on a limited comparison of human and murine orthologs. In the last 5 years, whole genome sequencing projects have yielded draft genomes of the early vertebrates, pufferfish (Takifugu rubripes), spotted green pufferfish (Tetraodon nigroviridis) and zebrafish (Danio rerio). Fuelled by this development, fish orthologs of a number of mammalian class-I helical cytokines have recently been discovered. In this review, we have characterised the mammalian class-I helical cytokine family and compared it with the emerging class-I helical cytokine repertoire of teleost fish. This approach offers important insights into cytokine evolution as it identifies the helical cytokines shared by fish and mammals that, consequently, existed before the divergence of teleosts and tetrapods. A 'fish-mammalian' comparison will identify the class-I helical cytokines that still await discovery in fish or, alternatively, may have been evolutionarily recent additions to the mammalian cytokine repertoire.

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“…In addition, MtT/E cells also show PACAP-induced IL-6 secretion [17]. Furthermore, IL-6 and LIF stimulate the growth of MtT/S somatotrope cells and MtT/SM somatomammotrope cells [14,19]. These data show that not only FS cells but also endocrine progenitor cells may facilitate tumor growth through gp130 cytokines.…”

Section: Discussionmentioning

confidence: 68%

Somatotropes Maintain Their Immature Cells Through Insulin-like Growth Factor I (IGF-I)

et al. 2007

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A pituitary tumor is considered to be composed of a heterogeneous population of hormone-producing endocrine cells, folliculo-stellate (FS) cells, and potential hormone-inactive progenitor cells to maintain a microenvironment such as that in angiogenesis for tumor development cooperatively. However, the system that maintains such a heterogeneous cell population has not been clarified yet. In the present study, we examined the mechanism for maintaining a heterogeneous cell population using two rat cell lines, MtT/S and MtT/E cells, which are known growth hormone (GH)-producing cells, and their progenitor cells, respectively. We found that conditioned medium of MtT/S cells could stimulate the growth of MtT/E cells. In addition, GH and insulin-like growth factor I (IGF-I) stimulated the growth of MtT/E cells. The messenger RNAs (mRNAs) of receptors for IGF-I and GH were expressed in the MtT/E cells. Moreover, IGF-I receptor inhibitor AG1024 could abolish the growth stimulatory activity in the conditioned medium of MtT/S cells. Therefore, we concluded that somatotropes (MtT/S) maintain their progenitor cells (MtT/E) through the GH-IGF-I signaling and IGF-I directly, which might be involved in the maintenance of progenitors of GH-producing cells and might contribute to pituitary tumor development.

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LEUKAEMIA INHIBITORY FACTOR AND INTERLEUKIN 6 INHIBIT SECRETION OF PROLACTIN AND GROWTH HORMONE BY RAT PITUITARY MtT/SM CELLS

Cited by 20 publications

References 25 publications

Characterization of the Low Molecular Weight Human Serum Proteome

Characterization of the Low Molecular Weight Human Serum Proteome

Phylogeny and evolution of class-I helical cytokines

Somatotropes Maintain Their Immature Cells Through Insulin-like Growth Factor I (IGF-I)

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