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PTP1B deficiency effect on mammary gland development and differentiation

ABSTRACT: Analysis of protein tyrosine phosphatase 1B (PTP1B) deficient mammary glands from nulliparous mice at estrous and pregnancy day 3, 7, 10 and 15. We used a genetically ablated PTP1B mouse model to gain a deeper knowledge of the role PTP1B plays in mammary gland development and to define the mechanism regulated by this phosphatase. Results provide insight into the role of PTP1B in mammary gland development and differentiation.

ORGANISM(S): Mus musculus

PROVIDER: GSE41768 | GEO | 2012/10/23

SECONDARY ACCESSION(S): PRJNA178146

REPOSITORIES: GEO

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PTP1B deficiency effect on mammary gland development and differentiation

Project description:Analysis of protein tyrosine phosphatase 1B (PTP1B) deficient mammary glands from nulliparous mice at estrous and pregnancy day 3, 7, 10 and 15. We used a genetically ablated PTP1B mouse model to gain a deeper knowledge of the role PTP1B plays in mammary gland development and to define the mechanism regulated by this phosphatase. Results provide insight into the role of PTP1B in mammary gland development and differentiation. Mouse mammary glands were isolated from PTP1B -/- and PTP1B +/+ nulliparous mice at estrous and pregnancy day 3, 7, 10 and 15 for RNA extraction and hybridization on Affymetrix microarrays.

2012-10-23 | E-GEOD-41768 | biostudies-arrayexpress

Identification of the role of PTP1B in acute kidney injury and its regulation via siRNA delivery with milk-derived extracellular vesicles

Project description:Acute kidney injury (AKI) is a critical condition marked by a sudden decline in kidney function, often triggered by ischemia-reperfusion (IR) injury. Its pathophysiology involves inflammation, oxidative stress, and endoplasmic reticulum (ER) stress. Recently, protein tyrosine phosphatase 1B (PTP1B) has been highlighted as a therapeutic target for ischemic disease due to its potential implication in activating ER stress. In this study, we observed significant overexpression of PTP1B in human kidney tissues during AKI. Additionally, in mouse models of AKI, we confirmed that this overexpression is associated with the upregulation of ER stress and inflammatory pathways mediated by Src. To explore the effect of PTP1B inhibition in AKI, we employed PTP1B-targeting siRNA (PTPi) delivered via extracellular vesicles derived from commercial milk (mEVs). PTPi@mEVs effectively reduced PTP1B expression in proximal tubular cells, decreasing ER stress and Src kinase activation. In an IR-AKI mouse, PTPi@mEVs alleviated renal dysfunction, reduced cell death, and restored gene expression related to inflammation, ROS, and ER stress. Histological analysis confirmed that PTP1B knockdown mitigated tight junction disruption in renal tissue. These findings underscore the therapeutic potential of targeting PTP1B to mitigate AKI symptoms, highlighting the efficacy of mEVs-mediated PTPi delivery in reducing acute inflammatory responses and renal dysfunction.

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The effect of PTP1B inhibitor (MSI-1436) on neutrophils.

Project description:Acute Lung Injury (ALI) can cause Acute Respiratory Distress Syndrome (ARDS), a lethal condition with limited treatment options and currently a common global cause of death due to COVID-19-induced ALI. ARDS secondary to Transfusion-Related Acute Lung Injury (TRALI) has been recapitulated pre-clinically by anti-MHC-I antibody administration to LPS-primed mice. In this model, we demonstrated that inhibitors of PTP1B, a protein tyrosine phosphatase that regulates signaling pathways of fundamental importance to homeostasis and inflammation, prevented lung injury and increased survival. Treatment with PTP1B inhibitors attenuated the aberrant neutrophil function that drives ALI, and was associated with release of myeloperoxidase, suppression of Neutrophil Extracellular Trap (NET) formation, and inhibition of neutrophil migration. Mechanistically, reduced signaling through the CXCR4 chemokine receptor, particularly to the activation of mTOR, was essential for these effects, linking PTP1B in hibition to promoting an aged neutrophil phenotype. Considering dysregulated activation of neutrophils is implicated in sepsis and can cause collateral tissue damage, we demonstrated also that PTP1B inhibitors improved survival and ameliorated lung injury in the LPS-induced sepsis model. Our data highlight PTP1B inhibition for prevention of TRALI and ARDS from multiple etiologies.

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Quantitative Proteomics Identifies Protein Tyrosine Phosphatase 1B as Modulator of B Cell Antigen Receptor Signaling

Project description:B cell antigen receptor (BCR) signaling is initiated by protein kinases and limited by counteracting phosphatases that currently are less well studied in their regulation of BCR signaling. We here used the B cell line Ramos to identify and quantify human B cell signaling components. Specifically, a protein tyrosine phosphatase profiling revealed a high expression of the protein tyrosine phosphatase 1B (PTP1B) in Ramos and human naive B cells. The loss of PTP1B leads to increased B cell activation. Through substrate trapping in combination with quantitative mass spectrometry, we identified 22 putative substrates or interactors of PTP1B. We validated Igalpha, CD22, PLCgamma1/2, CBL, BCAP and APLP2 as specific substrates of PTP1B in Ramos B cells. The tyrosine kinase BTK and the two adaptor proteins GRB2 and VAV1 were identified as direct binding partners and potential substrates of PTP1B. We showed that PTP1B dephosphorylates the inhibitory receptor protein CD22 at phosphotyrosine 807. We conclude that PTP1B negatively modulates BCR signaling by dephosphorylating distinct phosphotyrosines in B cell specific receptor proteins and various downstream signaling components.

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Quantitative Proteomics Identifies Protein Tyrosine Phosphatase 1B as Modulator of B Cell Antigen Receptor Signaling

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Transcriptomic Analysis of Pubertal and Adult Virgin Mouse Mammary Epithelial and Stromal Cell Populations

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