Disease relevance of RPL14

• Alteration of RPL14 in squamous cell carcinomas and preneoplastic lesions of the esophagus [1].
• In addition, RPL14 shows significant differences in allele frequency distribution in ethnically-defined populations, making this sequence a useful marker for the study of ethnicity-adjusted lung cancer risk [2].
• Trinucleotide repeat length variation in the human ribosomal protein L14 gene (RPL14): localization to 3p21.3 and loss of heterozygosity in lung and oral cancers [2].
• We generated six AAV2 capsid mutants by inserting a 14-amino-acid targeting peptide, L14, into six different putative loops of the AAV2 capsid protein identified by comparison with the known three-dimensional structure of canine parvovirus [3].
• To verify this, the gene for Bacillus stearothermophilus L14 has been cloned, and the protein has been purified and crystallized [4].

High impact information on RPL14

• Analysis of sequence covariation using the entire RNase P RNA data set reveals elements of tertiary structure in the RNA; the third nucleotides (underlined) of the GNRA tetraloops L14 and L18 are seen to interact with adjacent Watson-Crick base pairs in helix P8, forming A:G/C or G:A/U base triples [5].
• This ranges from 145 pseudogenes for RPL21 down to 3 pseudogenes for RPL14 [6].
• To investigate the interaction between a signal peptide and the lipid bilayer, two kinds of peptides, L8-M5 (L8 = MRL8PLAALG, M5 = KVFER) and L14-M5 (L14 = MRL14PLAALG), were examined in membranes composed of dioleoylphosphatidylcholine (DOPC) [7].
• In the tested informative cases, loss of heterozygosity (LOH) of RPL14 was observed in 29 out of 68 (43%) tumors [1].
• The data suggest that alteration of RPL14 occurred frequently in ESCC and might be an earlier event in the tumorigenesis of the esophagus [1].

Chemical compound and disease context of RPL14

• During the last 17 years, 494 adults aged 15 to greater than 70 with acute nonlymphoblastic leukemia (ANLL) were treated with one of five successive multiple drug treatment protocols of varying intensity (arabinosylcytosine + 6-thioguanine [n = 36]; L6 [n = 101]; L12 [n = 104]; L14/14M [n = 121]; and L16/16M [n = 132]) [8].

Biological context of RPL14

• The COOH-terminal region of the transcripts contained fifteen triplet repeats (GCT; alanine) at nucleotide 465 to 509, which is significantly expanded compared to the rat RL14 [9].
• A significant identity for hRL14 was observed with rat RL14 (85% identity), with exception of COOH-terminal region, but not with any eukaryote amino acid sequences so far deposited to database [9].
• No mutation was found in the remaining RPL14 allele of the tumors with LOH [1].
• The human ribosomal protein L14 gene (RPL14) is located on chromosome 3p21 [1].
• Genotype analysis of RPL14 shows that this locus is 68% heterozygous in the normal population, compared with 25% in non-small cell lung cancer (NSCLC) cell lines (p = 0.008) [2].

Anatomical context of RPL14

• Triplet repeat-containing ribosomal protein L14 gene in immortalized human endothelial cell line (t-HUE4) [9].
• The phylogenetic relationship of Cistanche deserticola, C. salsa and C. tubulosa was analyzed by comparing the nucleotide sequences of the plastid rps2 gene and the intergenic spacer region between rpl16 and rpl14 [10].
• Concomitantly ribosomal protein L14, which is not significantly phosphorylated in normal cells, became phosphorylated, as did a non-structural protein of Mr = 27000, associated with the ribosomes [11].
• Mutations in the sites for FIII/YY1 did not change reporter activity, nor did overexpression of FIII/YY1 in the oocytes prior to injection with L1 and L14 constructs [12].
• When total lysates of Jurkat cells undergoing apoptosis induced by doxorubicin were analyzed by Western blotting, degradation of three ribosomal proteins, S18, L5, and L14, was detected at 48 h after the induction of apoptosis [13].

Associations of RPL14 with chemical compounds

• The polypeptides present in the different eluted fractions were resolved by SDS-PAGE and were either silver stained or analysed by immunoblotting with monoclonal or polyclonal antibodies, respectively, raised against the glucose-binding protein CBP67 and the galactose-binding proteins CBP35 and L14 [14].

Other interactions of RPL14

• When cells shocked at 45 degrees C for 10 min were returned to 37 degrees C for 2 h there was rephosphorylation of ribosomal protein S6 and dephosphorylation of the 27 kDa protein, but not of ribosomal protein L14 [11].

Analytical, diagnostic and therapeutic context of RPL14

• Crystallization and preliminary X-ray diffraction studies of bacterial ribosomal protein L14 [4].

References