The Genes for Oncostatin M (OSM) and Leukemia Inhibitory Factor (LIF) Are Tightly Linked on Human Chromosome 22

Rose, Timothy M.; Lagrou, Michelle J.; Fransson, Ingegerd; Werelius, Barbro; Delattre, Olivier; Thomas, Gilles; Jong, Pieter J. de; Todaro, George J.; Dumanski, Jan P.

doi:10.1006/geno.1993.1294

Cited by 48 publications

(33 citation statements)

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“…While OSM-induced JakStat signaling was associated with the induction of morphological alterations indicative of renal tubular EMT (35), Stat3 signaling has been implicated in HGF-induced formation of epithelial tubules (2,60). OSM-induced responses consistent with a stimulatory role in cell differentiation have been also reported for glioma cells, mammary epithelial cells, hematopoietic cells, fibroblasts, and endothelial cells (13), while in totipotent embryonic stem cells OSM has been shown to inhibit cell differentiation (45). Moreover, we now report that OSM does not only activate Stat1 and Stat3 but is also a potent stimulator of the MAPKs ERK1, ERK2, and ERK5, which are important regulators of cell differentiation and proliferation (36,48).…”

Section: Discussionsupporting

confidence: 61%

Oncostatin M-induced effects on EMT in human proximal tubular cells: differential role of ERK signaling

Pollack¹,

Sarközi²,

Bánki³

et al. 2007

American Journal of Physiology-Renal Physiology

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Growing evidence suggests that a proportion of interstitial myofibroblasts detected during renal tubulointerstitial fibrosis originates from tubular epithelial cells by a process called epithelial-mesenchymal transition (EMT). The IL-6-type cytokine oncostatin M (OSM) has been recently implicated in the induction of EMT. We investigated OSM effects on the expression of both cell-cell contact proteins and mesenchymal markers and studied OSM-induced intracellular signaling mechanisms associated with these events in human proximal tubular cells. Human recombinant OSM attenuated the expression of N-cadherin, E-cadherin, and claudin-2 in human kidney-2 (HK-2) cells associated with the induction of HK-2 cell scattering in 3D collagen matrices. Conversely, expression of collagen type I, vimentin, and S100A4 was induced by OSM. OSM-stimulated cell scattering was inhibited by antibodies against gp130. Besides inducing phosphorylation of Stat1 and Stat3, OSM led to a strong concentration-and time-dependent phosphorylation of the mitogen-activated protein kinases ERK1, ERK2, and ERK5. MEK1/2 inhibitor U0126 (10 M) blocked basal and OSM-induced ERK1/2 phosphorylation but not phosphorylation of either ERK5 or Stat1/3. Both synthetic MEK1/2 inhibitors U0126 and Cl-1040, when used at concentrations which inhibit ERK1/2 phosphorylation but not ERK5 phosphorylation, restored N-cadherin expression in the presence of OSM, inhibited basal claudin-2 expression, but did not affect either basal or OSM-inhibited E-cadherin expression or OSM-induced expression of collagen type I and vimentin. These results suggest that in human proximal tubular cells ERK1/2 signaling represents an important component of OSM's inhibitory effect on N-cadherin expression. Furthermore, functional ERK1/2 signaling is necessary for basal claudin-2 expression.

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Section: Discussionsupporting

confidence: 61%

Oncostatin M-induced effects on EMT in human proximal tubular cells: differential role of ERK signaling

Pollack¹,

Sarközi²,

Bánki³

et al. 2007

American Journal of Physiology-Renal Physiology

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“…The genes encoding LIF and OSM are located in close proximity on the same locus in humans and mice (Rose et al 1993). The same is true for the LIFR and OSMR, suggesting that LIF and OSM as well as the genes encoding their receptors arose through gene duplication (Fig.…”

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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“…Among its family members, OSM resembles LIF most closely both in structure and function (22). The gene encoding for OSM, located on human chromosome 22q12, is only 20 kb away from LIF suggesting that these two genes evolved by gene duplication (22)(23)(24)(25).…”

mentioning

confidence: 99%

“…The gene encoding for OSM, located on human chromosome 22q12, is only 20 kb away from LIF suggesting that these two genes evolved by gene duplication (22)(23)(24)(25). Despite the striking similarities, OSM differs from LIF in its receptor binding.…”

mentioning

confidence: 99%

A Unique Loop Structure in Oncostatin M Determines Binding Affinity toward Oncostatin M Receptor and Leukemia Inhibitory Factor Receptor

Chollangi

Mather

Rodgers

et al. 2012

Journal of Biological Chemistry

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The Genes for Oncostatin M (OSM) and Leukemia Inhibitory Factor (LIF) Are Tightly Linked on Human Chromosome 22

Cited by 48 publications

References 0 publications

Oncostatin M-induced effects on EMT in human proximal tubular cells: differential role of ERK signaling

Oncostatin M-induced effects on EMT in human proximal tubular cells: differential role of ERK signaling

Phylogeny and evolution of class-I helical cytokines

A Unique Loop Structure in Oncostatin M Determines Binding Affinity toward Oncostatin M Receptor and Leukemia Inhibitory Factor Receptor

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