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Articles by L Meng
Total Records ( 4 ) for L Meng
  Z Han , Z Hong , C Chen , Q Gao , D Luo , Y Fang , Y Cao , T Zhu , X Jiang , Q Ma , W Li , L Han , D Wang , G Xu , S Wang , L Meng , J Zhou and D. Ma

Tumor cells acquire the ability to proliferate uncontrollably, resist apoptosis, sustain angiogenesis and evade immune surveillance. Signal transducer and activator of transcription (STAT) 3 regulates all of these processes in a surprisingly large number of human cancers. Consequently, the STAT3 protein is emerging as an ideal target for cancer therapy. This paper reports the generation of an oncolytic adenovirus (M4), which selectively blocks STAT3 signaling in tumor cells as a novel therapeutic strategy. M4 selectively replicated in tumor cells and expressed high levels of antisense STAT3 complementary DNA during the late phase of the viral infection in a replication-dependent manner. The viral progeny yield of M4 in tumor cells was much higher than that of the parent adenoviral mutants, Ad5/dE1A. M4 effectively silenced STAT3 and its target genes in tumor cells while sparing normal cells and exhibited potent antitumoral efficacy in vitro and in vivo. Systemic administration of M4 significantly inhibited tumor growth in an orthotopic gastric carcinoma mouse model, eliminated abdominal cavity metastases and prolonged survival time. In summary, M4 has low toxicity and great potential as a therapeutic agent for different types of cancers.

  L Meng , K. C Ruth , J. C Fletcher and L. Feldman

The CLE (CLVATA3/ESR-related) family of plant polypeptide signaling molecules shares a conserved 14-amino-acid (aa) motif, designated the CLE motif, which recent studies suggest is sufficient for CLE function in vitro. In this study, we report that Arabidopsis CLE proteins can function in a tissue-specific manner and confirm some CLE factors can act through different receptors. Using domain swapping, we show for the first time that the CLE motif likely determines much of the functional tissue-specificity of the proteins in planta. However, we also provide evidence in support of the new view that sequences outside the CLE motif (14 aa) contribute to CLE function and functional specificity in vivo. Additionally, we report that deletion of the putative signal peptide from different CLE proteins completely inactivates CLE function in vivo, whereas exchanging the CLE signal peptides with a conventional signal peptide from a rice glycine-rich cell wall protein also influences CLE function. We thus propose that the CLE motif itself determines its functional tissue-specificity by dictating the direct recognition and interaction of each CLE peptide with its optimal receptor(s), whereas the receptor(s) may be available in a tissue-specific manner. On the other hand, the sequences outside the CLE motif may influence CLE function by affecting the processing of CLE peptides, resulting in a change in the availability and/or abundance of CLE peptides in specific tissues and/or cells.

  Q Zhu , L Meng , J. K Hsu , T Lin , J Teishima and R. Y.L. Tsai

Telomeric repeat binding factor 1 (TRF1) is a component of the multiprotein complex "shelterin," which organizes the telomere into a high-order structure. TRF1 knockout embryos suffer from severe growth defects without apparent telomere dysfunction, suggesting an obligatory role for TRF1 in cell cycle control. To date, the mechanism regulating the mitotic increase in TRF1 protein expression and its function in mitosis remains unclear. Here, we identify guanine nucleotide-binding protein-like 3 (GNL3L), a GTP-binding protein most similar to nucleostemin, as a novel TRF1-interacting protein in vivo. GNL3L binds TRF1 in the nucleoplasm and is capable of promoting the homodimerization and telomeric association of TRF1, preventing promyelocytic leukemia body recruitment of telomere-bound TRF1, and stabilizing TRF1 protein by inhibiting its ubiquitylation and binding to FBX4, an E3 ubiquitin ligase for TRF1. Most importantly, the TRF1 protein-stabilizing activity of GNL3L mediates the mitotic increase of TRF1 protein and promotes the metaphase-to-anaphase transition. This work reveals novel aspects of TRF1 modulation by GNL3L.

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