Developmental expression of the murine Prl-1 protein tyrosine phosphatase gene

Rundle, Charles H.; Kappen, Claudia

doi:10.1002/(sici)1097-010x(19990501)283:6<612::aid-jez14>3.0.co;2-x

Cited by 18 publications

(7 citation statements)

References 23 publications

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“…Consistent with this notion, PRL-1 mRNA was predominantly expressed in proliferating chondrocytes in early development of mouse embryos but was localized primarily to differentiated, hypertrophic chondrocytes in later stages of development (Rundle and Kappen 1999). Consistent with this notion, PRL-1 mRNA was predominantly expressed in proliferating chondrocytes in early development of mouse embryos but was localized primarily to differentiated, hypertrophic chondrocytes in later stages of development (Rundle and Kappen 1999).…”

supporting

confidence: 62%

“…These three closely related enzymes are distinctive in that they are among the smallest of the PTPs consisting primarily of a catalytic domain, and their amino acid sequences contain a carboxy terminal CAAX motif that is posttranslationally isoprenylated. Recent evidence suggests that these may be pleiotropic-signaling molecules that play diverse roles in various tissue and cell types (Diamond et al 1996;Rundle and Kappen 1999). Specific substrates and cellular roles of the PRLs remain to be defined; however, their high degree of conservation (Cates et al 1996;Zeng et al 1998), as well as their similarity to several dual-specificity phosphatases (DSPs) involved in cell cycle and cell growth control (Zeng et al 1998;Kozlov et al 2004;Sun et al 2005), suggests a critical role for these PTPs in cellular regulation.…”

mentioning

confidence: 99%

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Cellular Localization of PRL-1 and PRL-2 Gene Expression in Normal Adult Human Tissues

Dumaual

Sandusky

Crowell

et al. 2006

J Histochem Cytochem.

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Recent evidence suggests that the PRL-1 and -2 phosphatases may be multifunctional enzymes with diverse roles in a variety of tissue and cell types. Northern blotting has previously shown widespread expression of both transcripts; however, little is known about the cell type-specific expression of either gene, especially in human tissues. Therefore, we investigated expression patterns for PRL-1 and -2 genes in multiple normal, adult human tissues using in situ hybridization. Although both transcripts were ubiquitously expressed, they exhibited strikingly different patterns of expression. PRL-2 was expressed heavily in almost every tissue and cell type examined, whereas PRL-1 expression levels varied considerably both between tissue types and between individuals. Widespread expression of PRL-1 and -2 in multiple organ systems suggests an important functional role for these enzymes in normal tissue homeostasis. In addition, the variable patterns of expression for these genes may provide distinct activities in each tissue or cell type.

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supporting

confidence: 62%

mentioning

confidence: 99%

Cellular Localization of PRL-1 and PRL-2 Gene Expression in Normal Adult Human Tissues

Dumaual

Sandusky

Crowell

et al. 2006

J Histochem Cytochem.

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“…PRL-1 (20 kDa) was first discovered in regenerating liver following partial hepatectomy as the product of an early-immediate response gene (2) and has since been implicated in the repair of other tissues including neurons, oligodendrocytes and the cerebral cortex in response to transient forebrain ischemia (3). PRLs are normally expressed at low levels in most mature cells, while higher expression levels are observed during embryonic development (4) and during cellular proliferation (5–9) or differentiation (5, 10, 11) depending on the cell type. Recently, PRL enzymes have gained considerable interest because each of the three isoforms can aggressively promote cancer (12, 13).…”

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confidence: 99%

Enzyme Activity of Phosphatase of Regenerating Liver Is Controlled by the Redox Environment and Its C-Terminal Residues

et al. 2009

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Phosphatase of regenerating liver-1 (PRL-1) belongs to a unique subfamily of protein tyrosine phosphatases (PTPases) associated with oncogenic and metastatic phenotypes. While considerable evidence exists to supports a role for PRL-1 in promoting proliferation, the biological regulators and effectors of PRL-1 activity remain unknown. PRL-1 activity is inhibited by disulfide bond formation at the active site in vitro, suggesting PRL-1 may be susceptible to redox regulation in vivo. Because PRL-1 has been observed to localize to several different subcellular locations and cellular redox conditions vary with tissue type, age, stage of cell cycle and subcellular location, we determined the reduction potential of the active site disulfide bond that controls phosphatase activity to better understand the function of PRL-1 in various cellular environments. We used high-resolution solution NMR spectroscopy to measure the potential and found it to be −364.3 ± 1.5 mV. Because normal cellular environments range from −170 to −320 mV, we concluded that nascent PRL-1 would be primarily oxidized inside cells. Our studies show that a significant conformational change accompanies activation, suggesting a post-translational modification may alter the reduction potential, conferring activity. We further demonstrate that alteration of the C-terminus renders the protein reduced and active in vitro, implying the C-terminus is an important regulator of PRL-1 function. These data provide a basis for understanding how subcellular localization regulates the activity of PRL-1 and, with further investigation, may help reveal how PRL-1 promotes unique outcomes in different cellular systems, including proliferation in both normal and diseased states.Phosphatase of Regenerating Liver (PRL) enzymes are a unique subfamily of protein tyrosine phosphatases (PTPases) and play an important role in maintaining appropriate tyrosine phosphorylation levels in the cell during development and tissue regeneration (1). This subfamily includes three homologous members (PRL-1, −2 and −3) that share a high degree of amino acid sequence identity (>75%). PRL-1 (20 kDa) was first discovered in regenerating liver following partial hepatectomy as the product of an early-immediate response gene (2) and has since been implicated in the repair of other tissues including neurons, oligodendrocytes and the cerebral cortex in response to transient forebrain ischemia (3). PRLs are normally expressed at low levels in most mature cells, while higher expression levels are observed during embryonic development (4) and during cellular proliferation (5-9) or differentiation (5,10, † This publication was made possible by NIH grant number P20 RR-17708 from the National Center for Research Resources and the Kansas University Center for Research. This work was additionally supported by fellowships for Andria Skinner from Amgen and the Edith and Eleta Ernst Cancer Research Fellowship. The Q-Tof2tm was purchased with support from KSTAR, Kansas administered NSF EPSCoR and the U...

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“…Prl-1 appears to exhibit dual functions depending on the cellular context -in the liver it is associated with proliferation (48), however in the intestine it is expressed in the differentiated epithelium of the villus, but not in the crypts (49). Prl-1 is also expressed in a temporal and spatially specific manner in the mouse embryo (50). Its role in mammary gland development has not yet been described.…”

Section: Discussionmentioning

confidence: 99%

Intermediate Molecular Biomarkers for the Protective Effect of Pregnancy Against Breast Cancer

Ginger¹,

Rosen²

2003

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Developmental expression of the murine Prl-1 protein tyrosine phosphatase gene

Cited by 18 publications

References 23 publications

Cellular Localization of PRL-1 and PRL-2 Gene Expression in Normal Adult Human Tissues

Cellular Localization of PRL-1 and PRL-2 Gene Expression in Normal Adult Human Tissues

Enzyme Activity of Phosphatase of Regenerating Liver Is Controlled by the Redox Environment and Its C-Terminal Residues

Intermediate Molecular Biomarkers for the Protective Effect of Pregnancy Against Breast Cancer

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