scholarly journals Ovary growth and protein levels in ovary and fat body during adult-wintering period in the red mason bee, Osmia rufa

Apidologie ◽  
2011 ◽  
Vol 42 (6) ◽  
pp. 749-758 ◽  
Author(s):  
Oskar Wasielewski ◽  
Karol Giejdasz ◽  
Tatiana Wojciechowicz ◽  
Marek Skrzypski
Keyword(s):  
Fat Body ◽  
Protein Levels ◽  
Ovary Growth

scholarly journals Tip60 Phosphorylation at Ser 99 Is Essential for Autophagy Induction in Bombyx mori

2020 ◽  
Vol 21 (18) ◽  
pp. 6893
Author(s):  
Wenmei Wu ◽  
Kang Li ◽  
Haigang Zhao ◽  
Xianying Xu ◽  
Jing Xu ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Histone Acetyltransferase ◽  
Regulatory Mechanism ◽  
Fat Body ◽  
Critical Role ◽  
Phosphorylation Site ◽  
Protein Levels ◽  
Autophagy Induction ◽  
Phosphatase Treatment ◽  
Amp Activated Protein Kinase

Tip60, a key histone acetyltransferase of the MYST family and member of the nuclear multimeric protein complex (NuA4), regulates the activity and stability of proteins involved in the cell cycle, DNA damage responses, autophagy, etc. However, the function and regulatory mechanism of Tip60 homolog in Bombyx mori are not elucidated. In the present study, Bombyx Tip60 (BmTip60) was functionally identified. Developmental profiles showed that the protein levels and nuclear localization of BmTip60 peaked in fat body during the larval–pupal metamorphosis when autophagy was intensive; simultaneously, the BmTip60 protein migrated to form an upper band as detected by Western blot. Interestingly, the upper band of BmTip60 was reduced by λ-phosphatase treatment, indicating that it was a phosphorylated form of BmTip60. Results showed that BmTip60 was promoted by starvation but not 20-hydroxyecdysone treatment. Transcription factor AMP-activated protein kinase (AMPK) affected by starvation was pivotal for BmTip60 protein migration. In addition, one mammalian phosphorylation site was identified in BmTip60 at Ser99, the constitutive-activation mutation of Ser99 to Asp99 but not its inactive mutation to Ala99 significantly upregulated autophagy, showing the critical role of phosphorylation at Ser99 for BmTip60-mediated autophagy. In conclusion, the starvation-AMPK axis promotes BmTip60 in B. mori, which was requisite for autophagy induction. These results reveal a regulatory mechanism of histone acetyltransferase Tip60 homologs by phosphorylation in insects, and sheds light on further related studies of acetylation regulation.

Effects of two juvenile hormone analogs on hemolymph and fat-body metabolites of the eastern spruce budworm, Choristoneura fumiferana (Clemens) (Lepidoptera: Tortricidae)

1993 ◽  
Vol 71 (6) ◽  
pp. 1169-1174 ◽  
Author(s):  
Hemendra Mulye ◽  
Roger Gordon
Keyword(s):  
Juvenile Hormone ◽  
Soluble Protein ◽  
Fat Body ◽  
Choristoneura Fumiferana ◽  
Experimental Period ◽  
Protein Levels ◽  
Carbohydrate Concentration ◽  
Eastern Spruce Budworm ◽  
Fat Bodies ◽  
Hormone Analogs

Early sixth instar larvae of Choristoneura fumiferana were treated with LD50 doses of the juvenile hormone analogs fenoxycarb and methoprene. Fenoxycarb caused an initial decrease, then an increase, in hemolymph carbohydrate concentration; fat-body glycogen was depleted initially, then increased in concentration (cf. controls) toward the end of the 6-day experimental period. Methoprene caused an opposite effect on hemolymph carbohydrates, but a similar effect (cf. fenoxycarb) on fat-body glycogen. Protein concentrations in the hemolymph of fenoxycarb-treated and methoprene-treated insects were lower than those of controls. The concentration of fat-body soluble protein of fenoxycarb-treated insects was initially lower, then higher, than that of controls. Methoprene did not alter soluble protein levels in the fat bodies. Lipids in the hemolymph of fenoxycarb-treated insects were depleted (cf. controls) throughout the experimental period; in the fat bodies, lipid concentration was elevated initially, then lowered. In methoprene-treated insects, hemolymph lipid levels were similar to those of controls up to 96 h post-treatment, then declined to lower than control levels; fat-body lipid content was initially higher, then lower, and finally higher, than that of controls. Fenoxycarb and methoprene caused severe, yet dissimilar, disruptions in metabolism of all three nutrients.

scholarly journals The cockroach Blattella germanica obtains nitrogen from uric acid through a metabolic pathway shared with its bacterial endosymbiont

2014 ◽  
Vol 10 (7) ◽  
pp. 20140407 ◽  
Author(s):  
Rafael Patiño-Navarrete ◽  
Maria-Dolors Piulachs ◽  
Xavier Belles ◽  
Andrés Moya ◽  
Amparo Latorre ◽  
...  
Keyword(s):  
Uric Acid ◽  
Dietary Protein ◽  
Fat Body ◽  
Blattella Germanica ◽  
Symbiotic Association ◽  
Nitrogen Recycling ◽  
Recycling Process ◽  
Protein Levels ◽  
Genes Encoding ◽  
Cockroach Blattella Germanica

Uric acid stored in the fat body of cockroaches is a nitrogen reservoir mobilized in times of scarcity. The discovery of urease in Blattabacterium cuenoti , the primary endosymbiont of cockroaches, suggests that the endosymbiont may participate in cockroach nitrogen economy. However, bacterial urease may only be one piece in the entire nitrogen recycling process from insect uric acid. Thus, in addition to the uricolytic pathway to urea, there must be glutamine synthetase assimilating the released ammonia by the urease reaction to enable the stored nitrogen to be metabolically usable. None of the Blattabacterium genomes sequenced to date possess genes encoding for those enzymes. To test the host's contribution to the process, we have sequenced and analysed Blattella germanica transcriptomes from the fat body. We identified transcripts corresponding to all genes necessary for the synthesis of uric acid and its catabolism to urea, as well as for the synthesis of glutamine, asparagine, proline and glycine, i.e. the amino acids required by the endosymbiont. We also explored the changes in gene expression with different dietary protein levels. It appears that the ability to use uric acid as a nitrogen reservoir emerged in cockroaches after its age-old symbiotic association with bacteria.

The Structure and Development of Microbodies in the Fat Body and other Tissues of an Insect (Calpodes Ethlius)

1970 ◽  
Vol 28 ◽  
pp. 148-149
Author(s):  
M. Locke ◽  
J. T. McMahon
Keyword(s):  
Electron Microscopy ◽  
Liquid Crystals ◽  
Fat Body ◽  
Competitive Inhibitor ◽  
Dense Core ◽  
Urate Oxidase ◽  
Blood Proteins ◽  
Free Base ◽  
The Core ◽  
The Matrix

The fat body of insects has always been compared functionally to the liver of vertebrates. Both synthesize and store glycogen and lipid and are concerned with the formation of blood proteins. The comparison becomes even more apt with the discovery of microbodies and the localization of urate oxidase and catalase in insect fat body.The microbodies are oval to spherical bodies about 1μ across with a depression and dense core on one side. The core is made of coiled tubules together with dense material close to the depressed membrane. The tubules may appear loose or densely packed but always intertwined like liquid crystals, never straight as in solid crystals (Fig. 1). When fat body is reacted with diaminobenzidine free base and H2O2 at pH 9.0 to determine the distribution of catalase, electron microscopy shows the enzyme in the matrix of the microbodies (Fig. 2). The reaction is abolished by 3-amino-1, 2, 4-triazole, a competitive inhibitor of catalase. The fat body is the only tissue which consistantly reacts positively for urate oxidase. The reaction product is sharply localized in granules of about the same size and distribution as the microbodies. The reaction is inhibited by 2, 6, 8-trichloropurine, a competitive inhibitor of urate oxidase.

Vitamin B6 Deficiency can Reduce Fuel Storage and Utilization in Physically Trained Rats

2008 ◽  
Vol 78 (2) ◽  
pp. 64-69 ◽  
Author(s):  
Choi ◽  
Cho
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Muscle Protein ◽  
Plasma Free Fatty Acid ◽  
Vitamin B ◽  
Liver Protein ◽  
Protein Levels ◽  
Before And After ◽  
Fuel Storage ◽  
Exercise Muscle

This study investigated the effect of vitamin B6 deficiency on the utilization and recuperation of stored fuel in physically trained rats. 48 rats were given either vitamin B6-deficient (B6–) diet or control (B6+) diet for 4 weeks and were trained on treadmill for 30 minutes daily. All animals were then subdivided into 3 groups: before-exercise (BE); during-exercise (DE); after-exercise (AE). The DE group was exercised on treadmill for 1 hour just before being sacrificed. Animals in the AE group were allowed to take a rest for 2 hours after being exercised like the DE group. Glucose and free fatty acids were compared in plasma. Glycogen and triglyceride were compared in liver and skeletal muscle. Protein levels were compared in plasma, liver, and skeletal muscle. Compared with the B6+ group, plasma glucose levels of the B6– group were significantly lower before and after exercise. Muscle glycogen levels of the B6– group were significantly lower than those of the B6+ group regardless of exercise. The liver glycogen level of the B6– group was also significantly lower than that of B6+ group during and after exercise. Before exercise, plasma free fatty acid levels were not significantly different between the B6+ and B6– groups, and plasma free fatty acid levels of the B6– group were significantly lower during and after exercise. The muscle triglyceride level of the B6– group was significantly lower than that of the B6+ group before exercise, and there were no differences between B6+ and B6– groups during and after exercise. Liver triglyceride levels were not significantly different between B6+ and B6– groups. Plasma protein levels of the B6– group were lower than those of B6+ before and after exercise. Muscle protein levels of the B6– group were not significantly different from those of the B6+ group. Liver protein levels of the B6– group were significantly lower than that of the B6+ group after exercise. Liver protein levels of both B6+ and B6– groups were not significantly changed, regardless of exercise. Thus, it is suggested that vitamin B6 deficiency may reduce fuel storage and utilization with exercise in physically trained rats.

Conjugated Linoleic Acid Causes a Marked Increase in Liver α-Tocopherol and Liver α-Tocopherol Transfer Protein in C57BL/6 J Mice

2010 ◽  
Vol 80 (1) ◽  
pp. 65-73 ◽  
Author(s):  
Pei-Min Chao ◽  
Wan-Hsuan Chen ◽  
Chun-Huei Liao ◽  
Huey-Mei Shaw
Keyword(s):  
Antioxidant Enzymes ◽  
Linoleic Acid ◽  
Conjugated Linoleic Acid ◽  
Thiobarbituric Acid ◽  
Control Group ◽  
Thiobarbituric Acid Reactive Substances ◽  
Control Groups ◽  
Protein Levels ◽  
Transfer Protein ◽  
And Control

Conjugated linoleic acid (CLA) is a collective term for the positional and geometric isomers of a conjugated diene of linoleic acid (C18:2, n-6). The aims of the present study were to evaluate whether levels of hepatic α-tocopherol, α-tocopherol transfer protein (α-TTP), and antioxidant enzymes in mice were affected by a CLA-supplemented diet. C57BL/6 J mice were divided into the CLA and control groups, which were fed, respectively, a 5 % fat diet with or without 1 g/100 g of CLA (1:1 mixture of cis-9, trans-11 and trans-10, cis-12) for four weeks. α-Tocopherol levels in plasma and liver were significantly higher in the CLA group than in the control group. Liver α-TTP levels were also significantly increased in the CLA group, the α-TTP/β-actin ratio being 2.5-fold higher than that in control mice (p<0.01). Thiobarbituric acid-reactive substances were significantly decreased in the CLA group (p<0.01). There were no significant differences between the two groups in levels of three antioxidant enzymes (superoxide dismutase, glutathione peroxidase, and catalase). The accumulation of liver α-tocopherol seen with the CLA diet can be attributed to the antioxidant potential of CLA and the ability of α-TTP induction. The lack of changes in antioxidant enzyme protein levels and the reduced lipid peroxidation in the liver of CLA mice are due to α-tocopherol accumulation.

L-Ascorbic Acid Addition to Chitosan Reduces Body Weight in Overweight Women

2014 ◽  
Vol 84 (1-2) ◽  
pp. 5-11 ◽  
Author(s):  
Eun Y. Jung ◽  
Sung C. Jun ◽  
Un J. Chang ◽  
Hyung J. Suh
Keyword(s):  
Ascorbic Acid ◽  
Body Weight ◽  
Fat Body ◽  
Body Weight Gain ◽  
Skinfold Thickness ◽  
The Body ◽  
Control Group ◽  
Percentage Body Fat ◽  
Overweight Women ◽  
Body Weights

Previously, we have found that the addition of L-ascorbic acid to chitosan enhanced the reduction in body weight gain in guinea pigs fed a high-fat diet. We hypothesized that the addition of L-ascorbic acid to chitosan would accelerate the reduction of body weight in humans, similar to the animal model. Overweight subjects administered chitosan with or without L-ascorbic acid for 8 weeks, were assigned to three groups: Control group (N = 26, placebo, vehicle only), Chito group (N = 27, 3 g/day chitosan), and Chito-vita group (N = 27, 3 g/day chitosan plus 2 g/day L-ascorbic acid). The body weights and body mass index (BMI) of the Chito and Chito-vita groups decreased significantly (p < 0.05) compared to the Control group. The BMI of the Chito-vita group decreased significantly compared to the Chito group (Chito: -1.0 kg/m2 vs. Chito-vita: -1.6 kg/m2, p < 0.05). The results showed that the chitosan enhanced reduction of body weight and BMI was accentuated by the addition of L-ascorbic acid. The fat mass, percentage body fat, body circumference, and skinfold thickness in the Chito and Chito-vita groups decreased more than the Control group; however, these parameters were not significantly different between the three groups. Chitosan combined with L-ascorbic acid may be useful for controlling body weight.

Positive correlation between neovascularization degree of carotid atherosclerosis determined by contrast-enhanced ultrasound and level of serum C-reactive protein

VASA ◽  
2015 ◽  
Vol 44 (3) ◽  
pp. 0187-0194 ◽  
Author(s):  
Xiaoni Chang ◽  
Jun Feng ◽  
Litao Ruan ◽  
Jing Shang ◽  
Yanqiu Yang ◽  
...  
Keyword(s):  
Contrast Enhancement ◽  
Rank Correlation ◽  
Artery Stenosis ◽  
Contrast Enhanced Ultrasound ◽  
C Reactive Protein ◽  
Protein Levels ◽  
Reactive Protein ◽  
Contrast Enhanced ◽  
Grade 3 ◽  
Axis View

Background: Neovascularization is one of the most important risk factors for unstable plaque. This study was designed to correlate plaque thickness, artery stenosis and levels of serum C-reactive protein with the degree of intraplaque enhancement determined by contrast-enhanced ultrasound. Patients and methods: Contrast-enhanced ultrasound was performed on 72 carotid atherosclerotic plaques in 48 patients. Contrast enhancement within the plaque was categorized as grade 1, 2 or 3. Maximum plaque thickness was measured in short-axis view. Carotid artery stenosis was categorized as mild, moderate or severe. Results: Plaque contrast enhancement was not associated with the degree of artery stenosis or with plaque thickness. Serum C-reactive protein levels were positively correlated with the number of new vessels in the plaque. C-reactive protein levels increased in the three groups(Grade 1: 3.72±1.79mg/L; Grade 2: 7.88±4.24 mg/L; Grade 3: 11.02±3.52 mg/L), with significant differences among them (F=10.14, P<0.01), and significant differences between each two groups (P<0.05). Spearman’s rank correlation analysis showed that serum C-reactive protein levels were positively correlated with the degree of carotid plaque enhancement (Rs =0.69, P<0.01). Conclusions: The combination of C-reactive protein levels and intraplaque neovascularization detected by contrast-enhanced ultrasound may allow more accurate evaluation of plaque stability.

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