Disease relevance of RPLP0

• Baculovirus expression systems appear to provide recombinant human P0 samples that can be used for studies on the structure and function [1].
• We have studied the allele specific expression of c-myc P0- and P3-RNA in Burkitt's lymphoma (BL) cells [2].
• IgG antibodies to P0 were slightly less common than IgM antibodies, being present in only 7.9% of GBS, 0% of CIDP and 3% of ONP patients and 0% of NC subjects [3].
• Antibody responses to P0 and P2 myelin proteins in Guillain-Barré syndrome and chronic idiopathic demyelinating polyradiculoneuropathy [3].

High impact information on RPLP0

• cDNA clones encoding three antigenically related human ribosomal phosphoproteins (P-proteins) P0, P1, and P2 were isolated and sequenced [4].
• Unlike P1 and P2, P0 was not removable from ribosomes by an ethanol-NH4Cl washing procedure [5].
• P2 along with its other family members, P0 and P1, constitutes a part of the elongation factor-binding site connected to the GTPase center in the 60S ribosomal subunit [6].
• We have isolated and sequenced a 1308bp clone from a pupal brain cDNA library of the flesh fly, Sarcophaga crassipalpis, showing 97% amino acid (aa) sequence similarity to Ceratitis capitata 60S acidic ribosomal protein P0 (CcP0) and 93% aa sequence similiarity to Drosophila melanogaster P0 (DmP0) [7].
• We discovered IgM antibodies to human P0 protein in the sera of 18.5% of the patients with GBS, 15.6% with CIDP, 6.4% with ONP and 3.8% of NC subjects [3].

Biological context of RPLP0

• We have identified a new point mutation in the myelin protein zero (P0) gene in two genetically identical twins with a demyelinating neuropathy [8].
• Therefore, in gene expression microarray experiments, genes whose expression is inhibited by subculture from passage 0 (P0) to passage 8 (P8) and enhanced by micropatterning and stretching were sought out [9].

Anatomical context of RPLP0

• Immunisation with the peripheral nerve myelin proteins P0 or P2 induces inflammatory neuropathy in animals [3].
• We serially investigated antigen-induced cytokine secretion from circulating T-cells stimulated with human peptides from the P0 and P2 proteins in seven patients and compared to results from seven serially investigated healthy controls [10].

Associations of RPLP0 with chemical compounds

• A 35.5- to 36-kD acidic protein was released at low levels from ribosomes with 1.0 M NH4Cl/50% ethanol and identified as P0 [11].
• In 1993 Hayasaka and colleagues found a point mutation in the myelin P0 gene (Asp 90 Glu) in this family, giving CMT1B a molecular basis [12].

Other interactions of RPLP0

• The addition of PGK1 and RPLP0 increased the robustness in qRT-PCR applications not stratified by disease [13].
• The housekeeping genes RPS9 and RPLP0 were applied to normalize differences in mRNA quality and quantity [14].
• T helper type 2 like cytokine responses to peptides from P0 and P2 myelin proteins during the recovery phase of Guillain-Barré syndrome [10].

Analytical, diagnostic and therapeutic context of RPLP0

• The P0 cDNA was initially identified by translation of hybrid-selected mRNA and immunoprecipitation of the products [4].

References