Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P43146 (tumour suppressor)
 5,935 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

p53 tumour suppressor gene mutations were studied in 118 renal cell carcinomas using paraffin-embedded surgical material. Optimal results were obtained with analysis of exon lengths between 150 and 200 base pairs for polymerase chain reaction. Single strand conformation polymorphism and sequencing analysis revealed only two point mutations (2/118, 2%): one involving codon 135; TGC-->TTC (cysteine-->phenylalanine) and the other codon 175; CGC-->CAC (arginine-->histidine). Both of these cases were classified as granular cell subtype on microscopic observation. The data suggest that the p53 tumour suppressor gene is not related to tumour initiation, promotion, or progression of renal cell carcinomas. However, there is the possibility that granular cell type carcinomas may have a different genetic background from clear cell type renal neoplasms.
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PMID:Polymerase chain reaction-single strand conformation polymorphism analysis of the p53 gene in paraffin-embedded surgical material from human renal cell carcinomas. 818 88

Recent findings indicate that substantial cross-talk may exist between transcriptional and post-transcriptional processes. Firstly, there are suggestions that specific promoters influence the post-transcriptional fate of transcripts, pointing to communication between protein complexes assembled on DNA and nascent pre-mRNA. Secondly, an increasing number of proteins appear to be multifunctional, participating in transcriptional and post-transcriptional events. The classic example is TFIIIA, required for both the transcription of 5S rRNA genes and the packaging of 5S rRNA. TFIIIA is now joined by the Y-box proteins, which bind DNA (transcription activation and repression) and RNA (mRNA packaging). Furthermore, the tumour suppressor WT1, at first thought to be a typical transcription factor, may also be involved in splicing; conversely, hnRNP K, a bona fide pre-mRNA-binding protein, appears to be a transcription factor. Other examples of multifunctional proteins are mentioned: notably PTB, Sxl, La and PU.1. It is now reasonable to assert that some proteins, which were first identified as transcription factors, could just as easily have been identified as splicing factors, hnRNP, mRNP proteins and vice versa. It is no longer appropriate to view gene expression as a series of compartmentalised processes; instead, multifunctional proteins are likely to co-ordinate different steps of gene expression.
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PMID:Multifunctional proteins suggest connections between transcriptional and post-transcriptional processes. 936 84

Tensins are large intracellular proteins believed to link the extracellular matrix to the cytoskeleton via integrins. Tensins are multidomain proteins consisting of homologous C1, PTPase, C2, SH2 and PTB domains. Full-length Tensin proteins can undergo cleavage inside cells, thus yielding domains in isolation that may have discrete subcellular localisations and downstream effects. We expressed different isoforms of Tensin2 and their individual domains as recombinant green fluorescent protein (GFP)-fusion constructs in DU145 human prostate cancer cells. Under fluorescence confocal microscopy, the isolated domains of Tensin2 all displayed discrete distributions throughout the cytoplasm and the nucleus. In particular, partial constructs containing the C1 domain localised preferentially to the nucleus, including the isolated C1 domain and the PTPase domain. In contrast, all three full-length isoforms of Tensin2 were present exclusively in discrete punctate bodies throughout the cytoplasm. This punctate staining showed colocalisation with the tumour suppressor protein DLC-1 as well as with actin (phalloidin). Furthermore, DU145 cells transiently expressing partial Tensin2 constructs containing the PTB domain showed an increased haptotactic migration. In addition, stimulation of renal carcinoma cells stably expressing Tensin2 by the survival factor Gas6 caused phosphorylation of its receptor Axl, but no effect on Tensin2, which was already maximally phosphorylated at time 0. In conclusion, our results indicate that differential proteolytic cleavage of Tensin2 can liberate domains with discrete localisations and functions, which has implications for the role of Tensins in cancer cell survival and motility.
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PMID:Individual domains of Tensin2 exhibit distinct subcellular localisations and migratory effects. 1974 64