• Journal of Microbiology and Biotechnology
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• v.16 no.9
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• pp.1416-1421
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• 2006

We identified a gene encoding the N-acetylmuramoyl L-alanine amidase (amiB) of Vibrio anguillarum, which catalyzes the degradation of peptidoglycan in bacteria. The entire open reading frame (ORF) of the amiB gene was composed of 1,722 nucleotides and 573 amino acids. The deduced amino acid sequence of AmiB showed a modular structure with two main domains; an N-terminal region exhibiting an Ami domain and three highly conserved, continuously repeating LysM domains in the C-terminal portion. An amiB mutant was constructed by homologous recombination to study the biochemical function of the AmiB protein in V. anguillarum. Transmission electron microscopy (TEM) revealed morphological differences, and that the mutant strain formed trimeric and tetrameric unseparated cells, suggesting that this enzyme is involved in the separation of daughter cells after cell division. Furthermore, inactivation of the amiB gene resulted in a marked increase of sensitivity to oxidative stress and organic acids.

• The Korean Journal of Physiology and Pharmacology
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• v.23 no.6
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• pp.539-547
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• 2019

Anoctamin 5 (ANO5)/TMEM16E belongs to a member of the ANO/TMEM16 family member of anion channels. However, it is a matter of debate whether ANO5 functions as a genuine plasma membrane chloride channel. It has been recognized that mutations in the ANO5 gene cause many skeletal muscle diseases such as limb girdle muscular dystrophy type 2L (LGMD2L) and Miyoshi muscular dystrophy type 3 (MMD3) in human. However, the molecular mechanisms of the skeletal myopathies caused by ANO5 defects are poorly understood. To understand the role of ANO5 in skeletal muscle development and function, we silenced the ANO5 gene in C2C12 myoblasts and evaluated whether it impairs myogenesis and myotube function. ANO5 knockdown (ANO5-KD) by shRNA resulted in clustered or aggregated nuclei at the body of myotubes without affecting differentiation or myotube formation. Nuclear positioning defect of ANO5-KD myotubes was accompanied with reduced expression of Kif5b protein, a kinesin-related motor protein that controls nuclear transport during myogenesis. ANO5-KD impaired depolarization-induced $[Ca2^{+}]_i$ transient and reduced sarcoplasmic reticulum (SR) $Ca^{2+}$ storage. ANO5-KD resulted in reduced protein expression of the dihydropyridine receptor (DHPR) and SR $Ca^{2+}-ATPase$ subtype 1. In addition, ANO5-KD compromised co-localization between DHPR and ryanodine receptor subtype 1. It is concluded that ANO5-KD causes nuclear positioning defect by reduction of Kif5b expression, and compromises $Ca^{2+}$ signaling by downregulating the expression of DHPR and SERCA proteins.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.45 no.3
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• pp.287-297
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• 2019

This study was carried out to evaluate the antioxidant, anti-inflammation, and whitening effect of Hordeum vulgare L. extracts and their fractions. Total polyphenol and flavonoid contents in fractions were varied from 13.58 to 40.06 mg GAE/g and 7.67 ~ 13.67 mg CE/g, respectively. Among the three fractions(chloroform, hexane, and water), $400{\mu}g/mL$ of the chroloform fraction showed similar antioxidant activity to ascorbic acid ($30{\mu}M$) against the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical. The chloroform and hexane fractions inhibited the NO production of RAW 264.7 cells similar to quercetin ($15{\mu}M$) and the chloroform fraction of $100{\mu}g/mL$ significantly reduced IL-6, iNOS and COX2 gene expression. Additionally, the chloroform fraction inhibited ${\beta}$-hexosaminidase degranulation, IL-4, and IL-13 gene expression in RBL-2H3 cells. All of the fractions inhibited tyrosinase activity in a concentration-dependent manner, and the hexane fraction at $50{\mu}g/mL$ and the chloroform fraction at $100{\mu}g/mL$ significantly inhibited melanin production of B16F10 cells. These results indicated that H. vulgare L. can be used as an effective cosmetic ingredient having anti-inflammation and whitening activity.