• Title/Summary/Keyword: wild cat

Search Result 75, Processing Time 0.02 seconds

Fumonisin B1-Induced Toxicity Was Not Exacerbated in Glutathione Peroxidase-1/Catalase Double Knock Out Mice

  • Yayeh, Taddesse;Jeong, Ha Ram;Park, Yoon Soo;Moon, Sohyeon;Sur, Bongjun;Yoo, Hwan-Soo;Oh, Seikwan
    • Biomolecules & Therapeutics
    • /
    • v.29 no.1
    • /
    • pp.52-57
    • /
    • 2021
  • Fumonisin B1 (FB1) structurally resembles sphingolipids and interferes with their metabolism leading to sphingolipid dysregulation. We questioned if FB1 could exacerbate liver or kidney toxicities in glutathione peroxidase 1 (Gpx1) and catalase (Cat) knockout mice. While higher serum levels of thiobarbituric acid reactive substances (TBARS) and sphinganine (Sa) were measured in Gpx1/Cat knockout mice (Gpx1/Cat KO) than wild type mice after 5 days of FB1 treatment, serum levels of alanine aminotransferase (ALT), sphingosine-1 phosphate (So-1-P), and sphinganine-1 phosphate (Sa-1-P) were found to be relatively low. Although Sa was highly elevated in Gpx1/Cat KO mice and wild mice, lower levels of So and Sa were found in both the kidney and liver tissues of Gpx/Cat KO mice than wild type mice after FB1 treatment. Paradoxically, FB1-induced cellular apoptosis and necrosis were hastened under oxidative stress in Gpx1/Cat KO mice.

Fibrinous pleuritis associated with Streptococcus canis in a leopard cat (Prionailurus bengalensis euptilurus)

  • Min-Gyeong Seo;Kook-Young Han;Sang-Hyun Kim;Chang Keun Kang;Jong-Hyun, Kim;Il-Hwa Hong
    • Journal of Veterinary Science
    • /
    • v.24 no.5
    • /
    • pp.68.1-68.6
    • /
    • 2023
  • Leopard cat (Prionailurus bengalensis euptilurus) is a small wild cat assessed as an endangered wildlife in Korea. There have been very few reports of their diseases. Herein, we describe fibrinous pleuritis caused by Streptococcus canis infection with excessive pleural effusion, hydropericardium, mild ascites, and liver fibrosis in a leopard cat. S. canis is a commensal microflora in domestic cats and often affects the upper respiratory tract inducing chronic and severe respiratory diseases. However, there is no literature regarding the S. canis in leopard cats. Therefore, we first report fibrinous pleuritis associated with an S. canis infection in a leopard cat.

Rehabilitation of an Amur Leopard Cat (Prionailurus bengalensis) with Complex Injury by a Road Accident

  • Sungryong Kim;Sungin Lee;Ok-Joo Lim;Ki-Jeong Na;Dong-Hyuk Jeong
    • Journal of Veterinary Clinics
    • /
    • v.39 no.6
    • /
    • pp.411-416
    • /
    • 2022
  • A 2.2 kg adult female Amur leopard cat (Prionailurus bengalensis) injured in a road accident was rescued. Severe abrasions on the left chin were washed daily with an antiseptic and silver sulfadiazine ointment was applied. Corneal edema of the oculus sinister (OS) was treated with ofloxacin and 5% sodium chloride eye drops. The skin wounds gradually improved, but the eye condition did not improve and the lens was also found to be detached. In addition, on the 6th day of hospitalization, melena was observed. On radiographic examination, foreign bodies in the stomach and a fracture of the sternum were confirmed. Subsequently, endoscopic removal of foreign bodies and enucleation of the OS using an electrothermal vessel sealer were performed sequentially over several days. However, corrective surgery of the fractured sternum was not carried out because a natural union of the fracture had occurred, which was found to be fairly stable. The patient completely recovered on the 83rd day and was successfully released into the wild on the 97th day, after two weeks of adaptation training in a natural environment. This report describes the rehabilitation of a wild Amur leopard cat injured in a road accident through a series of diagnostic and treatment steps until its eventual return to the wild and highlights some improvements needed in the process.

Expression of Catalase (CAT) and Ascorbate Peroxidase (APX) in MuSI Transgenic Tobacco under Cadmium Stress

  • Kim, Kye-Hoon;Kim, Young-Nam;Lim, Ga-Hee;Lee, Mi-Na;Jung, Yoon-Hwa
    • Korean Journal of Soil Science and Fertilizer
    • /
    • v.44 no.1
    • /
    • pp.53-57
    • /
    • 2011
  • The MuSI is known as a multiple stress resistant gene with several lines. A previous study using RT-PCR showed that the expression of MuSI gene in tobacco plant induced its tolerance to Cd stress. This study was conducted to examine the enhanced Cd tolerance of the MuSI transgenic tobacco plant through germination test and to understand the role of the involved antioxidant enzymes for the exhibited tolerance. Germination rate of MuSI transgenic tobacco was more than 10% higher than that of wild-type tobacco, and seedlings of MuSI transgenic tobacco grew up to 1.6 times larger and greener than seedlings of wild-type tobacco at 200 and 300 ${\mu}M$ Cd. From the third to the fifth day, CAT activities at 100 and 200 ${\mu}M$ Cd and APX activities at 100, 200 and 300 ${\mu}M$ Cd of MuSI transgenic tobacco were up to two times higher than those of wild-type tobacco. MuSI gene is shown to enhance the activities of antioxidant enzymes resulting in higher tolerance to oxidative stress compared with the control plant.

The prevalence of feline parasites in Suwon, Korea

  • Youn, Heejeong;Cho, Myung-Rae;Lim, Yong-Suk;Kim, Kyoung Hee;Bae, Bo-Kyung;Shin, Namsik;Nam, Ho-Woo
    • Korean Journal of Veterinary Research
    • /
    • v.52 no.2
    • /
    • pp.65-68
    • /
    • 2012
  • Feline parasites were investigated in the area of Suwon in Korea from September to October, 2003. Wild cat had spread to zoonotic parasites, these parasites could cause infection with a person. People have a lot of interest in parasite infection of wild cat. This article reviews rate of infection of a parasites and kind of a parasite of wild cats. We will report the critical characteristic features of parasites to a better understanding of the disease. The incidence rates of Toxocara cati, Trichuris felis, Ancylostoma braziliense and Capillaria sp were 37.0, 4.3, 1.1 and 1.1% in nematodes. Those of Taenia taeniaformis and Opisthorchis sp were 2.2 and 1.1% in cestode and trematode. Those of Isospora felis, Toxoplasma gondii, and Sarcocystis sp were 8.7, 9.8, and 2.2% in protozoa. Almost of these were zoonotic parasites without Isospora felis.

Differential Frost Tolerance and Enzymatic Activities in the Leaves and Immature Fruits of Loquat (Eriobotrya japonica Lindl.)

  • Zheng, Guohua;Niu, Xianqian;Zhang, Jinbiao;Wu, Hanwen;Lin, Xiuxiang;Pan, Dongming
    • Horticultural Science & Technology
    • /
    • v.33 no.3
    • /
    • pp.309-316
    • /
    • 2015
  • In this experiment, five commercial cultivars and one wild species of loquat were used to investigate frost tolerance and enzymatic activities in leaves and young fruits under cold stress at $-3^{\circ}C$. The frost injury, malondialdehyde (MDA) content, and oxygen-scavenging enzyme activities of superoxide dismutase (SOD), peroxidase (POD), catalase (CAT) and ascorbate peroxidase (APX) were studied. This results showed that the wild species 'Wild Oak-leaf' loquat was the most frost tolerant among accessions tested, followed by the cultivar 'Golden Block'. Other cultivars, 'Wu Gong Bai', 'Taicheng 4', 'Xiangzhong 11' and 'Zaozhong 6', were relatively weak in frost tolerance. The enzymatic activities of SOD, POD and CAT increased initially and then decreased as the exposure time increased. However, the enzymatic peak occurred later in the frost-tolerant accession than in the frost-sensitive accession. The correlation coefficients of MDA contents between leaves and immature fruits were from 0.93 to 0.99 in the five commercial loquat cultivars. For the 'Wild Oak-leaf' loquat, the correlation coefficients of MDA and POD were 0.98 and 0.95, respectively, but the coefficients for SOD, CAT and APX were relatively low. In general, there were good correlations between loquat leaves and immature fruits in MDA content and enzyme activities. These results indicate that analysis of these physiological and biochemical activities in loquat leaves could potentially be used to predict the cold tolerance in loquat at immature fruit stage and to accelerate breeding programs for cold tolerance in loquat.

Functional Characterization of Pharmcogenetic Variants of Human Cytochrome P450 2C9 in Korean Populations

  • Cho, Myung-A;Yoon, Jihoon G.;Kim, Vitchan;Kim, Harim;Lee, Rowoon;Lee, Min Goo;Kim, Donghak
    • Biomolecules & Therapeutics
    • /
    • v.27 no.6
    • /
    • pp.577-583
    • /
    • 2019
  • Human cytochrome P450 2C9 is a highly polymorphic enzyme that is required for drug and xenobiotic metabolism. Here, we studied eleven P450 2C9 genetic variants-including three novel variants F69S, L310V, and Q324X-that were clinically identified in Korean patients. P450 2C9 variant enzymes were expressed in Escherichia coli and their bicistronic membrane fractions were prepared The CO-binding spectra were obtained for nine enzyme variants, indicating P450 holoenzymes, but not for the M02 (L90P) variant. The M11 (Q324X) variant could not be expressed due to an early nonsense mutation. LC-MS/MS analysis was performed to measure the catalytic activities of the P450 2C9 variants, using diclofenac as a substrate. Steady-state kinetic analysis revealed that the catalytic efficiency of all nine P450 2C9 variants was lower than that of the wild type P450 2C9 enzyme. The M05 (R150L) and M06 (P279T) variants showed high $k_{cat}$ values; however, their $K_m$ values were also high. As the M01 (F69S), M03 (R124Q), M04 (R125H), M08 (I359L), M09 (I359T), and M10 (A477T) variants exhibited higher $K_m$ and lower $k_{cat}$ values than that of the wild type enzyme, their catalytic efficiency decreased by approximately 50-fold compared to the wild type enzyme. Furthermore, the novel variant M07 (L310V) showed lower $k_{cat}$ and $K_m$ values than the wild type enzyme, which resulted in its decreased (80%) catalytic efficiency. The X-ray crystal structure of P450 2C9 revealed the presence of mutations in the residues surrounding the substrate-binding cavity. Functional characterization of these genetic variants can help understand the pharmacogenetic outcomes.

Cloning and Expression of Pseudomonas cepacia catB Gene in Pseudomonas putida

  • Song, Seung-Yeon;Jung, Young-Hee;Lee, Myeong-Sok;Lee, Ki-Sung;Kim, Young-Soo;Kim, Chi-Kyung;Choi, Sang-Ho;Min, Kyung-Hee
    • Journal of Microbiology
    • /
    • v.34 no.4
    • /
    • pp.334-340
    • /
    • 1996
  • The enzyme, cis,cis-muconate lactonizing enzyme has been proposed to play a key role in the $\beta$-ketoadipate pathway of benzoate degradation. A 3.2-kb EcoRI fragment termed as pRSU2, isolated from a Pseudomonas cepacia genomic library was able to complement the catB defective mutant. Several relevant restriction enzyme sites were determined within the cloned fragment. In Pseudomonas putida SUC2 carrying pRSU2, the enzyme activity was relatively higher than those of the induced or partially induced state of wild type P. putida PRS2000. It was probably due to higher expression of P. cepacia catB in P. putida PRS2000. It was probably due to higher expression of P. cepacia catB in P. putida. One possible interpretation of these results is that the catB promoter in P. cepacia is recognized within P. putida, resulting in the almost same expression level.

  • PDF

Mutational Analysis of Thermus caldophilus GK24 ${\beta}$-Glycosidase: Role of His119 in Substrate Binding and Enzyme Activity

  • Oh, Eun-Joo;Lee, Yoon-Jin;Choi, Jeong-Jin;Seo, Moo-Seok;Lee, Mi-Sun;Kim, Gun-A;Kwon, Suk-Tae
    • Journal of Microbiology and Biotechnology
    • /
    • v.18 no.2
    • /
    • pp.287-294
    • /
    • 2008
  • Three amino acid residues (His119, Glu164, and Glu338) in the active site of Thermus caldophilus GK24 ${\beta}$-glycosidase (Tca ${\beta}$-glycosidase), a family 1 glycosyl hydrolase, were mutated by site-directed mutagenesis. To verify the key catalytic residues, Glu164 and Glu338 were changed to Gly and Gln, respectively. The E164G mutation resulted in drastic reductions of both ${\beta}$-galactosidase and ${\beta}$-glucosidase activities, and the E338Q mutation caused complete loss of activity, confirming that the two residues are essential for the reaction process of glycosidic linkage hydrolysis. To investigate the role of His119 in substrate binding and enzyme activity, the residue was substituted with Gly. The H119G mutant showed 53-fold reduced activity on 5mM p-nitrophenyl ${\beta}$-D-galactopyranoside, when compared with the wild type; however, both the wild-type and mutant enzymes showed similar activity on 5mM p-nitrophenyl ${\beta}$-D-glucopyranoside at $75^{\circ}C$. Kinetic analysis with p-nitrophenyl ${\beta}$-D-galactopyranoside revealed that the $k_{cat}$ value of the H119G mutant was 76.3-fold lower than that of the wild type, but the $K_m$ of the mutant was 15.3-fold higher than that of the wild type owing to the much lower affinity of the mutant. Thus, the catalytic efficiency $(k_{cat}/K_m)$ of the mutant decreased to 0.08% to that of the wild type. The $k_{cat}$ value of the H119G mutant for p-nitrophenyl ${\beta}$-D-glucopyranoside was 5.l-fold higher than that of the wild type, but the catalytic efficiency of the mutant was 2.5% of that of the wild type. The H119G mutation gave rise to changes in optima pH (from 5.5-6.5 to 5.5) and temperature (from $90^{\circ}C\;to\;80-85^{\circ}C$). This difference of temperature optima originated in the decrease of H119G's thermostability. These results indicate that His119 is a crucial residue in ${\beta}$-galactosidase and ${\beta}$-glucosidase activities and also influences the enzyme's substrate binding affinity and thermostability.

Mutation of Cysteine-115 to Alanine in Nicotiana glutinosa Ornithine Decarboxylase Reduces Enzyme Activity

  • Lee, Yong-Sun;Cho, Young-Dong
    • BMB Reports
    • /
    • v.34 no.5
    • /
    • pp.472-477
    • /
    • 2001
  • Ornithine decarboxylase (ODC, EC 4.1.1.17) is the first and key enzyme in eukaryotic polyamine biosynthesis. The cDNA encoding ornithine decarboxylase from Nicotiana glutinosa was cloned ($GeBank^{TM}$ AF 323910) and expressed in E. coli. Site directed mutagenesis were performed on several highly conserved cysteine residues. Among the mutants, C115A showed significant changes in the kinetic properties. The $K_m$ value of the C115A mutant was $1790\;{\mu}M$, which was 3-fold higher than that of the wild-type ODC. There was a dramatic decrease in the $k_{cat}$, values of the C115A mutant, compared to that of the wild-type ODC, which had a $k_{cat}$ value of $77.75\;s^{-1}$. C115A caused a shift in the optimal pH from 8.0 to 8.4. Considering these results, we suggest that cys-115 is involved in the catalytic activity of N. glutinosa ODC.

  • PDF