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The lumbar multifidus is characterised by larger type I muscle fibres compared to the erector spinae
Anouk Agten,Sjoerd Stevens,Jonas Verbrugghe,Bert O,Eijnde,Annick Timmermans,Frank Vandenabeele 대한해부학회 2020 Anatomy & Cell Biology Vol.53 No.2
The metabolic capacity of a muscle is one of the determinants of muscle function. Muscle fiber type characteristics give an indication about this metabolic capacity. Therefore it might be expected that the lumbar multifidus (MF) as a local stabilizer contains higher proportions of slow type I fibers, compared to the erector spinae (ES) as a global mobilizer. The aim of this study is to determine the muscle fiber characteristics of the ES and MF to provide insight into their structural and metabolic characteristics, and thereby the functional capacity of both muscles. Muscle fiber type characteristics in the ES and MF were investigated with an immunofluorescence staining of the myosin heavy chain isoforms. In both the ES and MF, type I muscle fibers are predominantly present. The cross-sectional area (CSA) of type I muscle fibers is significantly larger in the lumbar MF compared to the ES. However, the mean muscle fiber type percentage for type I was not significantly different, which resulted in an insignificant difference in relative cross-sectional area (RCSA) for type I. No significant differences were found for all other muscle fiber types. This may indicate that the MF displays muscle fiber type characteristics that tend to be more appropriate to maintain stability of the spine. However, because we could not demonstrate significant differences in RCSA between ES and MF, we cannot firmly state that there are functional differences between the ES an MF based only on structural characteristics.
Chondroid metaplasia of paraspinal connective tissue in the degenerative spine
Sjoerd Stevens,Sjoerd Stevens,Anouk Agten,Erika Wisanto,Melissa Lo Monaco,Jonas Verbrugghe,Annick Timmermans,Ivo Lambrichts,Frank Vandenabeele 대한해부학회 2019 Anatomy & Cell Biology Vol.52 No.2
A 51-year-old male was routinely biopsied during a paraspinal muscle study. The biopsy sample was taken from the right erector spinae muscle at the fourth lumbar vertebra. The patient had no history of (diagnosed) major back trauma. The obtained sample was histologically analyzed (hematoxylin and eosin, safranin O), and complementary magnetic resonance imaging was performed. The biopsied sample contained chondroid tissue. Based on its location, the biopsy sample was appointed as chondroid metaplasia. Although chondroid metaplasia is not uncommon in humans, this is the first report of chondroid metaplasia within the paraspinal connective tissue. We propose a novel mechanism to explain the paraspinal chrondrogenic changes, related to spinal degeneration.
USP8 suppresses death receptor-mediated apoptosis by enhancing FLIP<sub>L</sub> stability
Jeong, M,Lee, E-W,Seong, D,Seo, J,Kim, J-H,Grootjans, S,Kim, S-Y,Vandenabeele, P,Song, J Nature Publishing Group 2017 Oncogene Vol.36 No.4
<P>FLICE-like inhibitory protein (FLIP) is a critical regulator of death receptor-mediated apoptosis. Here, we found ubiquitin-specific peptidase 8 (USP8) to be a novel deubiquitylase of the long isoform of FLIP (FLIPL). USP8 directly deubiquitylates and stabilizes FLIPL, but not the short isoform. USP8 depletion induces FLIPL destabilization, promoting anti-Fas-, tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)- and tumor necrosis factor alpha-induced extrinsic apoptosis by facilitating death-inducing signaling complex or TNFR1 complex II formation, which results in the activation of caspase-8 and caspase-3. USP8 mRNA levels are elevated in melanoma and cervical cancers, and the protein levels of USP8 and FLIPL are positively correlated in these cancer cell lines. Xenograft analyses using ME-180 cervical cancer cells showed that USP8 depletion attenuated tumor growth upon TRAIL injection. Taken together, our data indicate that USP8 functions as a novel deubiquitylase of FLIPL and inhibits extrinsic apoptosis by stabilizing FLIPL.</P>
CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3
Seo, Jinho,Lee, Eun-Woo,Sung, Hyerim,Seong, Daehyeon,Dondelinger, Yves,Shin, Jihye,Jeong, Manhyung,Lee, Hae-Kyung,Kim, Jung-Hoon,Han, Su Yeon,Lee, Cheolju,Seong, Je Kyung,Vandenabeele, Peter,Song, Jae Nature Publishing Group 2016 NATURE CELL BIOLOGY Vol. No.
<P>Receptor-interacting protein kinase 3 (RIPK3) functions as a key regulator of necroptosis. Here, we report that the RIPK3 expression level is negatively regulated by CHIP (carboxyl terminus of Hsp70-interacting protein; also known as STUB1) E3 ligase-mediated ubiquitylation. Chip(-/-) mouse embryonic fibroblasts and CHIP-depleted L929 and HT-29 cells exhibited higher levels of RIPK3 expression, resulting in increased sensitivity to necroptosis induced by TNF (also known as TNF alpha). These phenomena are due to the CHIP-mediated ubiquitylation of RIPK3, which leads to its lysosomal degradation. Interestingly, RIPK1 expression is also negatively regulated by CHIP-mediated ubiquitylation, validating the major role of CHIP in necrosome formation and sensitivity to TNF-mediated necroptosis. Chip(-/-) mice (C57BL/6) exhibit inflammation in the thymus and massive cell death and disintegration in the small intestinal tract, and die within a few weeks after birth. These phenotypes are rescued by crossing with Ripk3(-/-) mice. These results imply that CHIP is a bona fide negative regulator of the RIPK1-RIPK3 necrosome formation leading to desensitization of TNF-mediated necroptosis.</P>