Disease relevance of Plcb3

• The 5'-upstream region of the rat phospholipase C-beta 3 gene contains two critical Sp1 sites and an HIV Inr-like element [1].
• We also used antibodies against the subunits of heterotrimeric G-proteins to show that the activation of PLC-beta 1 and PLC-beta 3 by both progestins involved the G alpha q/11 subunit, which was insensitive to pertussis toxin, whereas G alpha i, G alpha s, and G beta gamma subunits were not [2].
• Likewise, the elevated mRNA levels for PLC beta3 in RV at 1 week and in LVat 4 weeks of cardiac hypertrophy were decreased by losartan [3].
• Suppression of the neoplastic phenotype by transfection of phospholipase C beta 3 to neuroendocrine tumor cells [4].

High impact information on Plcb3

• Increased expression of phospholipase C (PLC)-beta1 and PLC-beta3 proteins was apparent in the scar and viable tissues after MI versus controls and is associated with increased PLC-beta1 activity in experimental hearts [5].
• The interaction of phospholipase C-beta3 with Shank2 regulates mGluR-mediated calcium signal [6].
• Importantly, microinjection of a synthetic peptide specifically mimicking the C terminus of PLC-beta3 markedly reduces the mGluR-mediated intracellular calcium response [6].
• Homer 1b, a Shank-interacting protein that is linked to group I metabotropic glutamate receptors and IP3 receptors, forms a multiple complex with Shank2 and PLC-beta3 [6].
• CXCR2 and the mutant 331T induced phospholipase C beta3 phosphorylation to an extent equivalent to that of CXCR1 [7].

Biological context of Plcb3

• With the use of antibodies raised against synthetic peptides corresponding to PLC-beta 3-specific amino acid sequences, we purified PLC-beta 3 from a rat brain particulate fraction [8].
• The increased muscle mass as well as the mRNA levels for PLC beta1 and beta3 in atria and RV, unlike PLC beta3 gene expression in LV, at 3 days of AVshunt were attenuated by losartan [3].
• These results suggest that the extracellular signals that induce the dissociation of G(o) or Gi, the heterotrimeric G proteins abundant in brain, should enhance the hydrolysis of PtdIns 4,5-P2 in brain primarily through activation of PLC-beta 3 (PLC-beta 2 is not detectable in brain) [9].
• The upregulation of G alpha q/11, PLC beta 3 and ERK1/2 in NRVMs occurred prior to [(3)H]-leucine incorporation increases, and could be inhibited with losartan [10].
• CONCLUSION: AngII can initiate cardiac hypertrophy and upregulate signal molecules in the G alpha q/11-mediated signal transduction pathway, such as G alpha q/11, PLC beta 3 and ERK1/2, at both tissue and cellular levels [10].

Anatomical context of Plcb3

• However, the levels of PLC-beta1, PLC-beta3, and PLC-beta4 were significantly lower in the hippocampus of RHA/Verh than in RLA/Verh rats [11].
• Membrane signaling and progesterone in female and male osteoblasts. II. Direct involvement of G alpha q/11 coupled to PLC-beta 1 and PLC-beta 3 [2].
• During pregnancy the levels of expression of the phospholipase C-beta3, phospholipase C-gamma1, and phospholipase C-delta1 isoforms were increased compared with the levels of expression in myometrium from nonpregnant rats [12].
• The immunohistochemical studies demonstrated localization of the phospholipase C-beta3, -gamma1, -gamma2, -delta1 and to a lesser degree phospholipase C-beta1 isoforms within the longitudinal and circular smooth muscle layers of the near-term pregnant rat uterus [13].
• Additionally, these membranes exhibited comparable, immunologically detectable, levels of PLC beta 3, G alpha q/11, and G beta [14].

Associations of Plcb3 with chemical compounds

• Similar alterations in cell morphology and in the expression of PLC-beta1, PLC-beta3, and Galpha(q/11) expression were observed when NT2 cells were differentiated with berberine, a compound structurally unrelated to retinoic acid [15].
• Exposure to carbachol resulted in a rapid and specific (homologous) attenuation of the subsequent muscarinic responses in terms of inositol phosphate production, PLC-beta3 translocation to membrane, and contraction [16].
• In the estrogen-treated rat myometrium, carbachol increased the generation of inositol phosphates by stimulating the muscarinic receptor-Gq/G11-phospholipase C-beta3 (PLC-beta3) cascade [16].
• Angiotensin II induced upregulation of G alpha q/11, phospholipase C beta 3 and extracellular signal-regulated kinase 1/2 via angiotensin II type 1 receptor [10].

Physical interactions of Plcb3

• Supershift mobility assays, site-directed mutagenesis and DNase I footprints indicated that Sp1 binds to three GC boxes within the sequence between -128 and -14 of the PLC-beta 3 promoter [1].

Other interactions of Plcb3

• The C terminus of PLC-beta3, but not other PLC-beta isotypes, specifically interacts with the PDZ domain of Shank2 [6].
• We identified PKC-alpha, -betaI, -betaII, -delta, -eta, -zeta, -theta, and -mu, PLC-beta3, and Gqalpha in adult and newborn type II cells [17].
• There was little difference between newborn and adult type II cells in the levels of PKC-delta, -eta, and -mu, PLC-beta3, and Gqalpha [17].
• RESULTS: These reverse transcriptase-polymerase chain reaction studies have confirmed expression of the phospholipase C-beta1a, phospholipase C-beta3, phospholipase C-gamma1, phospholipase C-beta2, and phospholipase C-delta1 isoforms in rat myometrial tissue [12].
• PLC-beta 1, PLC-beta 3 and PLC-delta 1 quantified by Western blot analysis, were present in the highest concentrations in the inner medulla of rats at both 4 and 12 weeks of age [18].

Analytical, diagnostic and therapeutic context of Plcb3

• RT-PCR showed that the cells express PLC-beta1a, PLC-beta1b, PLC-beta3 and PLC-gamma1 mRNA [19].
• RESULTS: The Western blot studies confirmed expression of the phospholipase C-beta3, -gamma1, -gamma2, and -delta1 proteins in both the membrane and cytosolic fractions of rat myometrium; in contrast, only trace amounts of the phospholipase C-beta1 protein was observed in this tissue [13].
• Immunoblotting analysis revealed the expression of PLC beta 3 and -gamma 1, but not PLC beta 1, -beta 2, or -beta 4 in the rat colonic epitheliums [20].
• The total SL PLC was decreased in diabetes and was associated with a decrease in SL PLC beta3 activity, which immunofluorescence in frozen diabetic left ventricular tissue sections revealed to be due to a decrease in PLC beta3 protein abundance [21].

References