PRL-1 PTPase expression is developmentally regulated with tissue-specific patterns in epithelial tissues

Kong, Weihong; Swain, Gary P.; Li, Shiuxing; Diamond, Robert H.

doi:10.1152/ajpgi.2000.279.3.g613

Cited by 30 publications

(38 citation statements)

References 35 publications

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“…Interestingly, several tissues, which displayed a nuclear localization pattern for PRL-1 in mature tissue, showed evidence of some cytoplasmic expression during tissue development. It was also observed that the expression of PRL-1 became more consistently nuclear, as well as more cell type restricted, as development progressed (19). Based on these findings, it is an intriguing possibility that PRL proteins localized to the nucleus might function in terminal differentiation and/or that localization to membranes might allow PRLs to be involved in cell growth and metastasis.…”

Section: Biological Functions Of Prlsmentioning

confidence: 86%

“…PRL-1 and PRL-2 seem to be more ubiquitously expressed than PRL-3, as they are detected at low levels in various tissues (10,11,18). In addition to adult tissues, PRL-1 expression has also been examined during development, where it is expressed in several digestive epithelial tissues (19). PRL expression in normal tissues seems to correlate most often with terminal differentiation.…”

Section: Prl Expressionmentioning

confidence: 99%

“…Although PRL-1 was first described as being localized to the nucleus (11), most subsequent studies (which have been focused on PRL expression in cancer) place PRL proteins at membrane structures, such as the plasma membrane, early endosomes, and endoplasmic reticulum (8,9,22). Using normal tissue samples from several digestive organs, Kong et al (19) observed that PRL-1 expression was mostly nuclear. Interestingly, several tissues, which displayed a nuclear localization pattern for PRL-1 in mature tissue, showed evidence of some cytoplasmic expression during tissue development.…”

Section: Biological Functions Of Prlsmentioning

confidence: 99%

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PRL phosphatases as potential molecular targets in cancer

Stephens¹,

Han

Gokhale

et al. 2005

Molecular Cancer Therapeutics

130

157

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The phosphatase of regenerating liver (PRL) family of phosphatases, consisting of PRL-1, PRL-2, and PRL-3, represents an intriguing group of proteins being validated as biomarkers and therapeutic targets in cancer. Individual PRLs are overexpressed in a variety of cancer cell lines and tissues when compared with their normal counterparts. More importantly, several recent studies have shown that PRL-3 is expressed at higher levels and at a greater frequency in colorectal cancer metastases compared with primary colorectal tumors and normal colon tissue. Ectopic expression of PRLs in nontumorigenic cells can influence proliferation and the migratory and invasive properties of cells, while knockdown of endogenous PRL-3 or PRL-1 in cancerous cells using small interfering RNA can abrogate cell motility and ability to metastasize in a mouse model. However, the exact biological function and cellular substrates of the PRLs remain unclear. This review will discuss what is known about the PRLs, what makes the PRLs possible attractive targets for therapeutic intervention, and the possible future directions in PRL biology and inhibitor identification. [Mol Cancer Ther 2005;4(11):1653 -61]

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Section: Biological Functions Of Prlsmentioning

confidence: 86%

Section: Prl Expressionmentioning

confidence: 99%

Section: Biological Functions Of Prlsmentioning

confidence: 99%

See 1 more Smart Citation

PRL phosphatases as potential molecular targets in cancer

Stephens¹,

Han

Gokhale

et al. 2005

Molecular Cancer Therapeutics

130

157

View full text Add to dashboard Cite

show abstract

“…PRL-1 was first identified as an immediate early gene expressed in regenerating liver and in serum-treated fibroblasts, and overexpression of PRL-1 in NIH 3T3 cells results in cell transformation, suggesting that the gene product plays a role in proliferation (23,30). Another role for PRL-1 has been proposed in the development and maintenance of differentiating epithelial tissues, as it is expressed in several developing tissues in fetal rat, and in the adult rat is found in terminally differentiated cells such as renal tubular epithelium, bronchiolar epithelium of the lung, and in villus but not crypt enterocytes of the intestine (31,32). Similarly, PRL-3 is specifically expressed in the differentiated epithelial cells of the villus but not in the proliferating crypt cells of the mouse small intestine (28).…”

mentioning

confidence: 99%

Interaction of Farnesylated PRL-2, a Protein-tyrosine Phosphatase, with the β-Subunit of Geranylgeranyltransferase II

Zeng

et al. 2001

Journal of Biological Chemistry

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Protein of regenerating liver (PRL)-1, -2, and -3 comprise a subgroup of closely related protein-tyrosine phosphatases featuring a C-terminal prenylation motif conforming to either the consensus sequence for farnesylation, CAAX, or geranylgeranylation, CCXX. Yeast two-hybrid screening for PRL-2-interacting proteins identified the ␤-subunit of Rab geranylgeranyltransferase II (␤GGT II). The specific interaction of ␤GGT II with PRL-2 but not with PRL-1 or -3 occurred in yeast and HeLa cells. Chimeric PRL-1/-2 molecules were tested for their interaction with ␤GGT II, and revealed that the C-terminal region of PRL-2 is required for interaction, possibly the PRL variable region immediately preceeding the CAAX box. Additionally, PRL-2 prenylation is prequisite for ␤GGT II binding. As prenylated PRL-2 is localized to the early endosome, we propose that this is where the interaction occurs. PRL-2 is not a substrate for ␤GGT II, as isoprenoid analysis showed that PRL-2 was solely farnesylated in vivo. Co-expression of the ␣-subunit (␣) of GGT II, ␤GGT II, and PRL-2 resulted in ␣/␤GGT II heterodimer formation and prevented PRL-2 binding. Expression of PRL-2 alone inhibited the endogenous ␣/␤GGT II activity in HeLa cells. Together, these results indicate that the binding of ␣GGT II and PRL-2 to ␤GGT II is mutually exclusive, and suggest that PRL-2 may function as a regulator of GGT II activity.

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“…The mechanism of phosphorylation in tyrosine residues of cellular proteins is of paramount importance in development and differentiation process of cell. Pleiotropic regulatory locus 1 (PRL-1) are immediateearly gene in liver regeneration their presence is linked by development on some tissues but with differentiation in others [23]. Tyrosine phosphorylation has regulatory cellular functions on enzymatic activity, gene expression, cell cycle progression and motility [24,25].…”

Section: Gain/loss Of Function Of Ptp Towards Cancermentioning

confidence: 99%

Protein Tyrosine Phosphatase-Prospective Target against Cancer: A Mini Review

Kanagarethinam¹,

Mahapatra²,

Jabalia³

et al. 2017

Cancer Surg

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Contemporary quantum leap on functional characterization of Protein Tyrosine Phosphatase (PTP) superfamily provides an incipient perspective on regulating signal transduction. PTPs are required in the regulation of several cellular processes; especially under stressed and pathogenic conditions leading to sundry human diseases. Concrete inhibition of PTP by oxyanions and active-site directed inhibitors (alkylating agents) may provide implements for human disease treatment involving them. The physiological paramountcy for the advancement of Protein Tyrosine Phosphatase, Non-receptor Type 1 (PTP1B) -predicated therapeutics is a prominent target for diabetes and inordinate corpulence treatment. PTPs are exhilarating quarry for active-site-mediated inhibitors generation. There, proneness to oxidation often create problem on high throughput screens, further the propensity for highly charged potent inhibitors, like non-hydrolysable pTyr mimetics, test with reverence to bioavailability. Subsequent preliminary concerns about specificity and quandaries with deference to hydrophilicity of phosphormimetics, promising successes attained by structure-predicated drug design, mainly the one exploit identical surface topology circumventing the catalytic pocket of each PTP. In PTP1B, it was found that a particular pTyr binding site could be habituated to succeed highly concrete bidentate inhibitors that bind both sites. This conventional approach can avail us to target highly categorical and efficacious inhibitors. Tyrosine phosphorylation increases 1-2% of total protein phosphorylation in tumorigenic transformation or magnification factor simulation essential for a controlled cellular event. This event is controlled by two molecular switches of enzymes protein tyrosine kinase and protein tyrosine phosphatase. Eccentric tyrosine phosphorylation is considered as one of the hallmarks of cancer. PTP has been recommended as next generation drug targets and a sum of PTP have been embroiled in sundry human disease, like cancer. The catalytic mechanism of PTP was demystified by site-directed mutagenesis then kinetic analyses with structural information. They have loss/ gain of function in cancer signaling events leading to dearth of inhibitors to control gain of function including modification of loss of function of PTP cognate genes. This review is about the consequentiality of tyrosine phosphatase enzyme and its role in the mundane cellular event and how it modifies the active site to agonise substrate and alter its action ultimately leading to tumorigenesis.

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PRL-1 PTPase expression is developmentally regulated with tissue-specific patterns in epithelial tissues

Cited by 30 publications

References 35 publications

PRL phosphatases as potential molecular targets in cancer

PRL phosphatases as potential molecular targets in cancer

Interaction of Farnesylated PRL-2, a Protein-tyrosine Phosphatase, with the β-Subunit of Geranylgeranyltransferase II

Protein Tyrosine Phosphatase-Prospective Target against Cancer: A Mini Review

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