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REFERENCE LINKING PLATFORM OF KOREA S&T JOURNALS
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Journal DOI :
Korean Society for Biochemistry and Molecular Biology
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Volume & Issues
Volume 41, Issue 12 - Dec 2008
Volume 41, Issue 11 - Nov 2008
Volume 41, Issue 10 - Oct 2008
Volume 41, Issue 9 - Sep 2008
Volume 41, Issue 8 - Aug 2008
Volume 41, Issue 7 - Jul 2008
Volume 41, Issue 6 - Jun 2008
Volume 41, Issue 5 - May 2008
Volume 41, Issue 4 - Apr 2008
Volume 41, Issue 3 - Mar 2008
Volume 41, Issue 2 - Feb 2008
Volume 41, Issue 1 - Jan 2008
Selecting the target year
ESCRT, autophagy, and frontotemporal dementia
Lee, Jin-A ; Gao, Fen-Biao ;
BMB Reports , volume 41, issue 12, 2008, Pages 827~832
DOI : 10.5483/BMBRep.2008.41.12.827
Many age-dependent neurodegenerative diseases are associated with the accumulation of abnormally folded proteins within neurons. One of the major proteolytic pathways in the cell is the autophagy pathway, which targets cytoplasmic contents and organelles to the lysosomes for bulk degradation under various physiological and stressful conditions. Although the importance of autophagy in cellular physiology is well appreciated, its precise roles in neurodegeneration remain largely unclear. Recent studies indicate that components of the endosomal sorting complex required for transport (ESCRT) are important in the autophagy pathway. Reduced activity of some ESCRT subunits leads to the accumulation of autophagosomes and failure to clear intracellular protein aggregates. Interestingly, rare mutations in CHMP2B, an ESCRT-III subunit, are associated with frontotemporal dementia linked to chromosome 3 (FTD3). Mutant CHMP2B proteins seem to disrupt the fusion of autophagosomes and lysosomes in cell culture models. These findings suggest a potential mechanism for the pathogenesis of FTD3 and possibly other neurodegenerative diseases as well.
The hepatocyte growth factor/c-Met signaling pathway as a therapeutic target to inhibit angiogenesis
You, Weon-Kyoo ; McDonald, Donald M. ;
BMB Reports , volume 41, issue 12, 2008, Pages 833~839
DOI : 10.5483/BMBRep.2008.41.12.833
Angiogenesis in tumors is driven by multiple growth factors that activate receptor tyrosine kinases. An important driving force of angiogenesis in solid tumors is signaling through vascular endothelial growth factor (VEGF) and its receptors (VEGFRs). Angiogenesis inhibitors that target this signaling pathway are now in widespread use for the treatment of cancer. However, when used alone, inhibitors of VEGF/VEGFR signaling do not destroy all blood vessels in tumors and do not slow the growth of most human cancers. VEGF/VEGFR signaling inhibitors are, therefore, used in combination with chemotherapeutic agents or radiation therapy. Additional targets for inhibiting angiogenesis would be useful for more efficacious treatment of cancer. One promising target is the signaling pathway of hepatocyte growth factor (HGF) and its receptor (HGFR, also known as c-Met), which plays important roles in angiogenesis and tumor growth. Inhibitors of this signaling pathway have been shown to inhibit angiogenesis in multiple in vitro and in vivo models. The HGF/c-Met signaling pathway is now recognized as a promising target in cancer by inhibiting angiogenesis, tumor growth, invasion, and metastasis.
Disruption of ATP binding destabilizes NPM/B23 and inhibits anti-apoptotic function
Choi, Joung-Woo ; Lee, Sang-Bae ; Ahn, Jee-Yin ; Lee, Kyung-Hoon ;
BMB Reports , volume 41, issue 12, 2008, Pages 840~845
DOI : 10.5483/BMBRep.2008.41.12.840
Nucleophosmin/B23, a major nucleolar phosphoprotein, is overexpressed in actively proliferating cells. In this study, we demonstrate that B23 exclusively localizes in the nucleolus, whereas ATP depletion results in the redistribution of B23 throughout the whole nucleus and destabilizes B23 via caspase-3 mediated cleavage. Interestingly, ATP binding precedes PI(3,4,5)P3 binding at lysine 263 and ATP binding mutants fail to restore the anti-apoptotic functions of B23 in PC12 cells. Thus, the ATP-B23 interaction is required for the stability of the B23 protein and regulates cell survival, confining B23 within the nucleolus in PC12 cells.
Identification of marbling-related candidate genes in M. longissimus dorsi of high- and low marbled Hanwoo (Korean Native Cattle) steers
Lee, Seung-Hwan ; Cho, Yong-Min ; Lee, Sang-Hong ; Kim, Bum-Soo ; Kim, Nam-Kuk ; Choy, Yeon-Ho ; Kim, Kyoung-Hoon ; Yoon, Du-Hak ; Im, Seok-Ki ; Oh, Sung-Jong ; Park, Eung-Woo ;
BMB Reports , volume 41, issue 12, 2008, Pages 846~851
DOI : 10.5483/BMBRep.2008.41.12.846
This study was conducted to identify marbling-related candidate genes in M. longissimus dorsi of high- and low-marbled Hanwoo. The longissimus dorsi muscles were selected for gene expression from eight Hanwoo steer carcasses based on crude fat content. In the analysis of variance, gene expression of five candidate genes, FABP4, SCD,
, Titin and Nebulin was determined to be significantly different between high- and low-marbled Hanwoo steers (P < 0.0001). The Pik-4 and CaMK II genes were also shown to have a significant effect on crude fat content (P < 0.01). In the analysis of the differential expression between high- and low marbled groups, FABP4 gene expression was approximately 2 times higher in the high marbled group relative to the low marbled group. However, the
and SCD gene were highly expressed in the low marbled group. In addition, Titin and Nebulin were highly expressed in the low marbled group when placed under relatively high shear force. Finally, the Pik-4 and CaM K II gene also displayed a high expression pattern in the low marbled group.
Direct characterization of E2-dependent target specificity and processivity using an artificial p27-linker-E2 ubiquitination system
Ryu, Kyoung-Seok ; Choi, Yun-Seok ; Ko, Jun-Sang ; Kim, Seong-Ock ; Kim, Hyun-Jung ; Cheong, Hae-Kap ; Jeon, Young-Ho ; Choi, Byong-Seok ; Cheong, Chae-Joon ;
BMB Reports , volume 41, issue 12, 2008, Pages 852~857
DOI : 10.5483/BMBRep.2008.41.12.852
Little attention has been paid to the specificity between E2 and the target protein during ubiquitination, although RING-E3 induces a potential intra-molecular reaction by mediating the direct transfer of ubiquitin from E2 to the target protein. We have constructed artificial E2 fusion proteins in which a target protein (p27) is tethered to one of six E2s via a flexible linker. Interestingly, only three E2s (UbcH5b, hHR6b, and Cdc34) are able to ubiquitinate p27 via an intra-molecular reaction in this system. Although the first ubiquitination of p27 (p27-Ub) by Cdc34 is less efficient than that of UbcH5b and hHR6b, the additional ubiquitin attachment to p27-Ub by Cdc34 is highly efficient. The E2 core of Cdc34 provides specificity to p27, and the residues 184-196 are required for possessive ubiquitination by Cdc34. We demonstrate direct E2 specificity for p27 and also show that differential ubiquitin linkages can be dependent on E2 alone.
Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity
Kim, Hye-Nan ; Chung, Hye-Shin ;
BMB Reports , volume 41, issue 12, 2008, Pages 858~862
DOI : 10.5483/BMBRep.2008.41.12.858
Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a zinc-dependent proteinase found in cholesterol-rich lipid rafts on the plasma membrane. MT1-MMP hydrolyzes extracellular matrix (ECM) proteins, activates pro-matrix metalloproteinase-2 (proMMP-2) and plays an important role in ECM remodeling, cancer cell migration and metastasis. The role of caveolin-1, an integral protein of caveolae, in the activation of MT1-MMP remains largely unknown. Here, we show that the expression of caveolin-1 attenuates the activation of proMMP-2, reduces proteolytic cleavage of ECM and inhibits cell migration. We utilized the cytoplasmic tail domain deletion (
) or the E240A mutant of MT1-MMP. Co-expression of caveolin-1 with the wild-type or the
MT1-MMP decreased the proMMP-2 activation and inhibited collagen degradation and cell migration. Caveolin-1 had no effect on the catalytically inert E240A MT1-MMP. Our findings suggest that caveolin-1 is essential in the down-regulation of MT1-MMP activity by promoting internalization from the cell surface.
Expression of CD320 in human B cells in addition to follicular dendritic cells
Cho, Wha-Jung ; Choi, Jin-Suk ; Park, Chan-Hum ; Yoon, Sun-Ok ; Jeoung, Doo-Il ; Kim, Young-Myeong ; Choe, Jong-Seon ;
BMB Reports , volume 41, issue 12, 2008, Pages 863~867
DOI : 10.5483/BMBRep.2008.41.12.863
CD320 has been recently discovered and reported as a follicular dendritic cell (FDC) protein. Although CD320 is known to enhance proliferation of germinal center (GC) B cells, little other information is available. In this study, we investigated its cellular distribution in the GC. Confocal microscopy of human tonsil sections revealed co-localization of CD320 with CD19 and CD38 but not with CD3 indicating that GC B cells expressed CD320 in addition to FDC. In purified GC B cells, CD320 expression was inhibited in the nucleus, membrane and cytoplasm. Reverse transcriptase-polymerase chain reaction confirmed CD320 mRNA expression in B cells. These finding indicate that CD320 is expressed in B cells in addition to FDC, and that its GC activity may be more complicated than previously thought.
The effect of rod domain A148V mutation of neurofilament light chain on filament formation
Lee, In-Bum ; Kim, Sung-Kuk ; Chung, Sang-Hee ; Kim, Ho ; Kwon, Taeg-Kyu ; Min, Do-Sik ; Chang, Jong-Soo ;
BMB Reports , volume 41, issue 12, 2008, Pages 868~874
DOI : 10.5483/BMBRep.2008.41.12.868
Neurofilaments (NFs) are neuronal intermediate filaments composed of light (NF-L), middle (NF-M), and heavy (NF-H) subunits. NF-L self-assembles into a "core" filament with which NF-M or NF-H co-assembles to form the neuronal intermediate filament. Recent reports show that point mutations of the NF-L gene result in Charcot-Marie-Tooth disease (CMT). However, the most recently described rod domain mutant of human NF-L (A148V) has not been characterized in cellular level. We cloned human NF-L and used it to engineer the A148V. In phenotypic analysis using SW13 cells, A148V mutation completely abolished filament formation despite of presence of NF-M. Moreover, A148V mutation reduced the levels of in vitro self-assembly using GST-NF-L (H/R) fusion protein whereas control (A296T) mutant did not affect the filament formation. These results suggest that alanine at position 148 is essentially required for NF-L self-assembly leading to subsequent filament formation in neuronal cells.
Characterization of tissue-specific mbu-3 gene expression in the mouse central nervous system
Lee, Chae-Jin ; Cho, Eun-Young ; Kim, Sun-Jung ;
BMB Reports , volume 41, issue 12, 2008, Pages 875~880
DOI : 10.5483/BMBRep.2008.41.12.875
Mbu-3 is a novel mouse brain unigene that was identified by digital differential display. In this study, expression of the gene was chased through developmental stages and the protein product was identified in the brain. The cDNA sequence was 3,995-bp long and contained an ORF of 745 AA. Database searches revealed that the chicken SST273 gene containing LRR- and Ig-domain was an mbu-3 orthologue. Tissue specificity for the gene was examined in embryos and in brains at post-natal and adult stages. During the embryonic stages, mbu-3 was localized to the central nervous system in the brain and spinal cord. In the early post-natal stages, the gene was evenly expressed in the brain. However, with aging, expression was confined to specific regions, particularly the hippocampus. The protein was approximately 95 kDa as determined by Western blot analysis of brain extracts.
The nonconserved N-terminus of protein phosphatases 1 influences its active site
Xie, XiuJie ; Huang, Wei ; Xue, ChengZhe ; Wei, Qun ;
BMB Reports , volume 41, issue 12, 2008, Pages 881~885
DOI : 10.5483/BMBRep.2008.41.12.881
Protein phosphatase 1 consists of a secondary structure arrangement, conserved in the serine/threonine protein phosphatase gene family, flanked by nonconserved N-terminal and C-terminal domains. The deletion mutant of PP1 with the 8 nonconserved N-terminal residues removed was designated PP1-(9-330). PP1-(9-330) had a higher activity and affinity than PP1 when assayed against four different substrates, and it also demonstrated a 6-fold higher sensitivity to the inhibitor okadaic acid. This suggested that the N-terminal domain suppresed the activity of PP1 and interfered with its inhibition by okadaic acid. The ANS fluorescence intensity of PP1-(9-330) was greater than that of PP1, which implies that the hydrophobic groove running from active site in the truncated PP1 was more hydrophobic than in PP1. Our findings provide evidence that the nonconserved N-terminus of PP1 functions as an important regulatory domain that influences the active site and its pertinent properties.