Disease relevance of RPL4

• A number of clinical studies have implicated the cell adhesion molecule L1 in Hirschsprung's disease [1].
• Moreover, it contributes to knowledge of the structure of HPV-16 L1 VLPs and their derivatives [2].
• Identification of two cross-neutralizing linear epitopes within the L1 major capsid protein of human papillomaviruses [3].
• HPV-11 L1 VLPs could also be dissociated by treatment with carbonate buffer at pH 9.6, but VLPs could not be regenerated following carbonate treatment [4].
• We also show that plant-expressed L1 self-assembles into VLPs with immunological properties comparable to those of native HPV virions [5].

Psychiatry related information on RPL4

• Mutations in L1CAM, the gene encoding the transmembrane multifunctional neuronal adhesion molecule L1, are associated with neurodevelopmental disorders including X-linked hydrocephalus and mental retardation [6].

High impact information on RPL4

• The LINE-1 (L1) retrotransposon, the most important human mobile element, shapes the genome in many ways [7].
• RESULTS: We show that L1 is expressed by neural crest cells as they colonize the gut [1].
• L1-deficient mice show a small but significant reduction in neural crest cell migration at early developmental stages, but the entire gastrointestinal tract is colonized [1].
• We show here that L1-EGFP can undergo retrotransposition in vivo and produce fluorescence in mouse testis [8].
• Expression of GFP occurs only if L1-EGFP has undergone a cycle of transcription, reverse transcription, and integration into a transcriptionally permissive genomic region [8].

Chemical compound and disease context of RPL4

• The results suggested that reactivity of MAb HPV-16.I23 to L1 protein is lost when leucine 152 of the HPV-16 L1 protein is replaced by phenylalanine [3].
• Novel mechanism of resistance to oxazolidinones, macrolides, and chloramphenicol in ribosomal protein L4 of the pneumococcus [9].
• Increased antibody responses to human papillomavirus type 16 L1 protein expressed by recombinant vaccinia virus lacking serine protease inhibitor genes [10].
• In this work, we used a lactose-inducible system based on the Lactobacillus casei lactose operon promoter (plac) for expression of the HPV-16 L1 protein in L. casei [11].
• HPV antibody detection by ELISA with capsid protein L1 fused to glutathione S-transferase [12].

Biological context of RPL4

• The deduced amino acid sequence shows that human ribosomal protein L4 has 425 amino acid residues and a calculated molecular mass of 47,821 Da [13].
• To determine the frequency of L1-mediated transduction in the human genome, we selected 66 previously uncharacterized L1 sequences from the GenBank database [14].
• Active LINE-1 (L1) elements possess the ability to transduce non-L1 DNA flanking their 3' ends to new genomic locations [14].
• Taken together, these observations indicate that inhibition of p27(KIP1) transcription through PI3K-induced FKHR-L1 phosphorylation provides a novel mechanism of regulating cytokine-mediated survival and proliferation [15].
• Occasionally, the 3' end processing machinery may bypass the L1 polyadenylation signal and instead utilize a second downstream polyadenylation site [14].

Anatomical context of RPL4

• Here we show that in mammalian cells, Gu(alpha) physically interacts with ribosomal protein L4 (RPL4), a component of 60S ribosome large subunit [16].
• Translational control of ribosomal protein L4 mRNA is required for rapid neurite regeneration [17].
• This mRNA, which encodes the ribosomal protein L4, is translationally regulated during neurite regeneration in PC12 cells [17].
• We have generated Ba/F3 cell lines expressing a tamoxifen-inducible active FKHR-L1 mutant [FKHR-L1(A3):ER*] [15].
• It is the founder of a neural group of related cell surface receptors that share with L1 a highly conserved cytoplasmic domain that associates with the cytoskeleton [18].

Associations of RPL4 with chemical compounds

• Importantly, ingestion of transgenic L1 potato was associated with activation of an anti-VLP immune response in mice that was qualitatively similar to that induced by VLP parenteral administration, and this response was enhanced significantly by subsequent oral boosting with purified insect cell-derived VLPs [5].
• Finally, we found that the resistant strain harbored a 27-bp insertion in the highly conserved region of the gene encoding the ribosomal protein L4; this insertion may explain the existence of the resistance to erythromycin [19].
• Among the 31 strains studied that showed high-level resistance to both azithromycin and clarithromycin, 28 had ribosomal alterations, 7 had mutations in ribosomal protein L4, 11 had mutations in L22, 2 had mutations in 23S rRNA, 8 had multiple mutations, and 3 had no mutations [20].
• L1, beta1 integrin, and cadherins mediate axonal regeneration in the embryonic spinal cord [21].
• L1 RNA, but not protein, was detected biochemically in C3 cells [22].

Other interactions of RPL4

• If special attention to intraepithelial lesions is appropriate, RPL4 and PGK1 are recommended as the best combination of two genes [23].
• This nuclear wheat RPL5 acquired its targeting information by duplication of an existing targeting presequence for another mitochondrial protein, ribosomal protein L4 [24].
• Among the differentially expressed cDNAs, homologies of 96% and 87%, respectively, were found to the human proto-oncogene PTI-1 and the human ribosomal protein L4 [25].

Analytical, diagnostic and therapeutic context of RPL4

• Based on UV crosslinking and electrophoretic mobility-shift assays using purified components, we demonstrate here that the ORF1 protein encoded by mouse L1 binds nucleic acids with a strong preference for RNA and other single-stranded nucleic acids [26].
• L1 exon shuffling potential has been reported in cell culture assays, and two potential L1-mediated exon shuffling events have been identified in the genome [27].
• PCR analysis of human/rodent hybrid cell line DNA samples showed that the polymorphic L1 elements were located on several different chromosomes [28].
• Transgenic plants expressing the HPV major capsid protein L1 could be a system to produce virus-like particles for prophylactic vaccination or could even be used as edible vaccines to induce an L1-specific prophylactic immune response [29].
• However, Northern blot analysis revealed that most of the L1 transcripts were degraded [29].

References