Disease relevance of RPLP2

• P2. The expression of P2 mRNA was significantly higher (Student's t test, one tail; P less than or equal to 0.01) in seven fibroadenomas than in seven carcinomas, with an average five-fold difference [1].
• This enhanced expression level P2 mRNA in benign fibroadenomas compared with malignant carcinomas is contrary to that expected, based on earlier work with normal colonic mucosa, colorectal carcinoma and hepatic metastasis [1].
• Breast cancer underexpressed P2 compared to normal tissue (p < 0.001) [2].
• Anti-P antibodies present in sera from patients with chronic Chagas heart disease (cChHD) recognize peptide R13, EEEDDDMGFGLFD, which encompasses the C-terminal region of the Trypanosoma cruzi ribosomal P1 and P2 proteins [3].
• Based on the physiological behavior of mutants in groups II and V, it appears that P2 protein and nucleoprotein are required for virion RNA synthesis during influenza virus replication [4].

High impact information on RPLP2

• Taken together, these data define specific molecular requirements for alpha(M)beta(2) to mediate cell migration to Fg derivatives and assign a novel proinflammatory activity to the P2 peptide [5].
• Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly [6].
• We found that a wide range of GnRH-I or GnRH-II concentrations (0.1-10 nM) inhibit the expression of mRNA encoding the 60S acidic ribosomal phosphoproteins, P1 and P2 [7].
• Two forms of gonadotropin-releasing hormone (GnRH) are expressed in human breast tissue and overexpressed in breast cancer: a putative mechanism for the antiproliferative effect of GnRH by down-regulation of acidic ribosomal phosphoproteins P1 and P2 [7].
• In addition, the following constitutive ACHN proteins were identified: copper zinc superoxide dismutase, 60S acidic ribosomal protein P2, and a second heat shock protein 27 isoform [8].

Chemical compound and disease context of RPLP2

• Thus, the 60S acidic ribosomal protein P2 of F venenatum probably is the reason for the described severe hypersensitivity reactions of the patient to Quorn-mycoprotein because of its potential cross-reactivity to the F culmorum allergen Fus c 1 [9].

Biological context of RPLP2

• The identities of the P1 and P2 cDNAs were confirmed by the strong similarities of their encoded amino acid sequences to published primary structures of the homologous rat, brine shrimp, and Saccharomyces cerevisiae proteins [6].
• Phosphorylation of P2 is known to regulate protein synthesis in vitro [10].
• Sequence and hybridization analysis of this cosmid showed that the TP2 gene resided 3' of the P2 gene at a distance of approximately 7 kilobases (kb) [11].
• This new genomic organisation revealed that all known chromosomal translocations map upstream of P2, removing P1 and putative upstream regulatory sequences leaving P2 intact [12].
• The human and bovine genomes each contain two expressed nuclear genes, called P1 and P2, for subunit c, a hydrophobic subunit of the membrane sector, Fo, of mitochondrial ATP synthase [13].

Anatomical context of RPLP2

• The synthetic P0, P1, and P2 proteins were serologically and electrophoretically identical to P-proteins extracted from HeLa cells [6].
• The transcripts most strikingly over-expressed by the mutant cell lines were MARCKS, DKFZp547C244, and RPLP2 [14].
• P1 and P2 proteins were purified from ribosomes of maize embryonic axes and their physicochemical characteristics determined [15].
• Immunisation with the peripheral nerve myelin proteins P0 or P2 induces inflammatory neuropathy in animals [16].
• METHODS: Anti-P mAbs were prepared by a standard hybridoma procedure using recombinant human P1 and P2 proteins as immunogens [17].

Associations of RPLP2 with chemical compounds

• The ribosomal protein P2 was identified as an endogenous HEK-293 cell protein whose phosphorylation was increased following agonist stimulation of the beta2AR under conditions where tyrosine kinases, PKC and PKA, were inhibited [10].
• In order to map the immunodominant domains of the E1 glycoprotein, two epitopes from amino acid residues 210 to 223 (P1) and 315 to 327 (P2) were predicted from the HCV sequence [18].
• We have previously reported the occurrence of two serine endoproteases (referred to as P1 and P2) in dark-induced senescent wheat (Triticum aestivum L.) leaves [19].
• In contrast, P2 was already present in non-senescent leaves and showed increased levels in leaves senescing after N starvation or incubation in darkness [19].
• According to its biochemical and physical properties (inhibition by chymostatin and PMSF, broad pH range of activity, thermostability and ability to hydrolyse Suc-AAPF-pNA) P2 was classified as a serine protease with chymotrypsin-like activity [19].

Physical interactions of RPLP2

• It is concluded that the heterodimeric complex of the P1/P2 proteins is formed preferentially [20].

Regulatory relationships of RPLP2

• When injected to animals, P1 protein induced only experimental allergic neuritis while P2 protein induced both mild experimental allergic neuritis and experimental allergic encephalomyelitis [21].

Other interactions of RPLP2

• cDNA clones encoding three antigenically related human ribosomal phosphoproteins (P-proteins) P0, P1, and P2 were isolated and sequenced [6].
• Beta 2-adrenergic receptor stimulated, G protein-coupled receptor kinase 2 mediated, phosphorylation of ribosomal protein P2 [10].
• MMP9 secretion was passage-dependent, decreasing rapidly as the cells were passaged in culture and was not detected at P2 [22].
• This technique permitted the identification of the P2 protein, the nucleoprotein, and the M protein as the defective gene products in mutant groups II, V, and VII, respectively [4].
• Thus, there is an essential interaction(s) between 3CD and other viral P2 or P3 protein products required for efficient RNA replication which is not fully achieved between proteins from the two different members of the same virus genus [23].

Analytical, diagnostic and therapeutic context of RPLP2

• Protein P2 was measured using Western blotting [2].
• Expression of P1 and P2 mRNA transcripts was analyzed by Northern blots with specific cDNA probes [15].
• ELISA with P0, P1 and P2, premixed at equimolar concentrations, gave higher OD readings than each protein tested individually [24].
• The patient's serum produced nucleolar and cytoplasmic staining by indirect immunofluorescence analyses on HEp-2 cell substrate and reacted with P0, P1 and P2 proteins in immunoblotting using purified ribosomal antigens [25].
• P1, P2 proteins and the basic protein of the central nervous system have been shown to have different electrophoretic mobility, and each of the two peripheral basic proteins was shown to be homogeneous by disc electrophoresis [21].

References