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See PI3 peptidase inhibitor 3 in the Gene database

pi3 in Homo sapiens Macaca mulatta Canis lupus familiaris All 178 Gene records

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Select item 14152801.

Madame Curie Bioscience Database [Internet].

Austin (TX): Landes Bioscience; 2000-2013.

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Select item 23639742.

Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis.

Arvin A, Campadelli-Fiume G, Mocarski E, et al., editors.

Cambridge: Cambridge University Press; 2007.

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Select item 16686903.

Holland-Frei Cancer Medicine. 6th edition.

Kufe DW, Pollock RE, Weichselbaum RR, et al., editors.

Hamilton (ON): BC Decker; 2003.

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Select item 34012944.

Endotext [Internet].

Feingold KR, Anawalt B, Blackman MR, et al., editors.

South Dartmouth (MA): MDText.com, Inc.; 2000-.

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Select item 18602425.

WormBook: The Online Review of C. elegans Biology [Internet].

Pasadena (CA): WormBook; 2005-2018.

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Select item 44036686.

StatPearls [Internet].

Treasure Island (FL): StatPearls Publishing; 2024 Jan-.

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Select item 14563907.

Endocrinology: An Integrated Approach.

Nussey S, Whitehead S.

Oxford: BIOS Scientific Publishers; 2001.

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Select item 14589848.

GeneReviews® [Internet].

Adam MP, Feldman J, Mirzaa GM, et al., editors.

Seattle (WA): University of Washington, Seattle; 1993-2024.

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Select item 41031749.

Brain Neurotrauma: Molecular, Neuropsychological, and Rehabilitation Aspects.

Kobeissy FH, editor.

Boca Raton (FL): CRC Press/Taylor & Francis; 2015.

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Select item 480224610.

Nicotinic Acetylcholine Receptor Signaling in Neuroprotection [Internet].

Akaike A, Shimohama S, Misu Y, editors.

Singapore: Springer; 2018.

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Select item 455477411.

Magnesium in the Central Nervous System [Internet].

Vink R, Nechifor M, editors.

Adelaide (AU): University of Adelaide Press; 2011.

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Select item 296478812.

Pancreatic Cancer and Tumor Microenvironment.

Grippo PJ, Munshi HG, editors.

Trivandrum (India): Transworld Research Network; 2012.

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Select item 485381613.

LiverTox: Clinical and Research Information on Drug-Induced Liver Injury [Internet].

Bethesda (MD): National Institute of Diabetes and Digestive and Kidney Diseases; 2012-.

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Select item 235805214.

Probe Reports from the NIH Molecular Libraries Program [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2010-.

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Select item 219516215.

StemBook [Internet].

Cambridge (MA): Harvard Stem Cell Institute; 2008-.

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Select item 408515616.

Biological Agents.

IARC Working Group on the Evaluation of Carcinogenic Risks to Humans.

Lyon (FR): International Agency for Research on Cancer; 2012. (IARC Monographs on the Evaluation of Carcinogenic Risks to Humans, No. 100B.)

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Select item 150279217.

Molecular Imaging and Contrast Agent Database (MICAD) [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2004-2013.

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Select item 150206818.

Annual Reviews Collection [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2002 Nov.

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Select item 532167219.

Essentials of Glycobiology [Internet]. 4th edition.

Varki A, Cummings RD, Esko JD, et al., editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2022.

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Select item 544913420.

15th Report on Carcinogens [Internet].

National Toxicology Program.

Research Triangle Park (NC): National Toxicology Program; 2021 Dec 21.

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Supplemental Content

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Figure 5

Major signal transduction pathways induced by VEGF. In endothelial cells and neurons, VEGF signaling through activated VEGFR-2 involves the MAP-kinase pathway (MEK-ERK) as well as the PI₃ kinase-AKT pathway. In endothelial cells, activation of the MAP-kinase pathway mediates cell proliferation, while signaling through the PI₃ kinase-AKT pathway leads to cell survival. Recruitment of phospholipase C γ (PLC-γ) followed by activation of protein kinase C (PKC) and endothelial nitric oxide synthetase (eNOS), finally, is involved in induction of vascular permeability. In neurons, both PI₃ kinase-AKT and MAP-kinase pathways seem to be involved in VEGF-mediated neuroprotection. All these signaling events are mediated through activation of VEGFR-2, while confirmed data are not available about the role of VEGFR-1 and neuropilin-1. (Adapted from ref. 2).

Vascular Endothelial Growth Factor.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.
Figure 3A

PLC? contributes to activation of cPLA₂ during Fc?R-mediated phagocytosis. Fc?R cross-linking results in the phosphorylation of the ITAMs by a src family kinase member. The phosphorylated ITAMs form a docking site for several proteins, including Syk and p85/p110 PI3 Kinase. PI3K activation results in the formation of PI(3,4,5)P₃ which can bind to the C terminal SH2 domain of PLCγ, localizing it to the phagosome. Additionally, Syk phosphorylates PLCγ, enhancing its activity. Activated PLCγ hydrolyzes PI(4,5)P₂ to generate IP₃ and DAG. DAG, generated by PLC or the combined action of PLD and PAP-1, activates the novel PKC-ε, which is upstream of ERK. The combined effects of the rise in Ca_i²⁺ and phosphorylation by ERK activate cPLA₂ to release AA for production of prostaglandins.

Phospholipases and Phagocytosis.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.
FIGURE 44.8

Effects of hyaluronan (HA) on oncogenic signaling. Endogenous HA–CD44 interaction is required for the formation of constitutive signaling complexes containing CD44, activated receptor tyrosine kinases (RTKs), phosphatidylinositol–3-kinase (PI3 kinase), and several other signaling molecules involved in cell survival, proliferation, and invasiveness. In addition, PI3 kinase stimulates HA production, thus setting up a positive feedback loop that amplifies these pathways. Antagonists of HA–CD44 interaction (e.g., HA oligomers, soluble HA-binding proteins, or siRNA against CD44) cause disassembly of constitutive complexes present in tumor cells with high levels of RTK activity and consequently inhibit their activity. On the other hand, increased HA production induces assembly of these complexes in cells with low levels of RTK activity and consequently stimulates RTK activity. HA-stimulated RTK activity is essential for correct embryonic morphogenesis and epithelial-mesenchymal transitions (EMT), whereas increased, deregulated RTK activity promotes the progression of malignant properties such as invasiveness, increased cell survival, and drug resistance in cancer cells.
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Glycosylation Changes in Cancer.

Varki A, Cummings RD, Esko JD, et al., editors. Essentials of Glycobiology. 2nd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2009.