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1.
Anim Biosci ; 34(3): 457-462, 2021 Mar.
Article in English | MEDLINE | ID: mdl-32898960

ABSTRACT

OBJECTIVE: The aim of this study was to investigate the effects of Enteromorpha powder supplementation on reproduction-related hormones and genes in the late laying period of Zi geese. METHODS: A total of 312 (1-year-old) Zi geese with similar laying rate were randomly divided into 2 groups with 6 replicates each, each with 21 female geese and 5 male geese. The control group was fed with a basal diet and the test group was fed with a diet containing 3% Enteromorpha powder. The trial period lasted for 7 weeks. RESULTS: Our results showed that the laying rate was improved in the test group at each week of trial (p<0.01), and the levels of estradiol in serum and prolactin in ovary were increased compared with the control group (p<0.05). CONCLUSION: Based on above results, Enteromorpha powder supplementation at 3% could promote reproductive performance during the late laying period of Zi geese.

2.
Mitochondrial DNA B Resour ; 4(2): 2287-2288, 2019 Jul 11.
Article in English | MEDLINE | ID: mdl-33365508

ABSTRACT

Poncirus polyandra is a threatened plant in China Now, the complete chloroplast (cp) genome of P. polyandra was assembled. The cp genome of P. polyandra was 160,212 bp in length, it consists of a pair of inverted repeats ((IRa and IRb) regions (27,016 bp) separated by the large single-copy (LSC, 87,407 bp) and small single-copy (SSC, 18,775 bp) regions. The cp genome encodes 105 unique genes, including 70 protein-coding genes, 30 transfer RNA genes, 4 ribosomal RNA genes, and 1 pseudogene. The phylogenetic tree of Rutaceae showed that P. polyandra was clustered together with genus Citrus and Poncirus.

3.
Mol Med Rep ; 16(4): 5062, 2017 10.
Article in English | MEDLINE | ID: mdl-28791408

ABSTRACT

Following the publication of this article, we regret to report that we have been unable to reproduce the results presented in the paper in our subsequent studies. At the present time, we have not been able to ascertain the reason behind this. Therefore, we would like to retract this article from publication. All the named authors agree to this retraction. We regret any inconvenience to the readers that this retraction will cause. [The original article was published in Molecular Medicine Reports 14: 819-824, 2016; DOI: 10.3892/mmr.2016.5294].

4.
Mol Med Rep ; 14(1): 819-24, 2016 Jul.
Article in English | MEDLINE | ID: mdl-27220600

ABSTRACT

The aim of the present study was to evaluate the effects of the eukaryotic initiation factor 6 (eIF6) gene on the secretion of M2 macrophage fibrosis­associated factors and the expression levels of key proteases during scar repair. Male eIF6 wild­type (eIF6+/+) and knockout (eIF6+/­) C57BL/6 mice were intraperitoneally lavaged to obtain macrophages, which were induced to the M2 type using interleukin­4. Differences between the gene expression profiles of these macrophages were compared with gene microarrays, and the results were validated using reverse transcription-quantitative polymerase chain reaction analysis and ELISA. Compared with the eIF6+/­ mice, the mRNA and protein expression levels of vascular endothelial growth factor (VEGF) and tissue inhibitor of metalloproteinase­2 (TIMP­2) in the M2 macrophages of the eIF6+/+ mice were significantly downregulated (P<0.05), whereas the mRNA and protein expression levels of matrix metalloproteinase­2 (MMP­2) were significantly upregulated (P<0.05). Therefore, the results indicated that eIF6 alleviated cicatrization, possibly by inhibiting the generation of VEGF, in order to prevent overgrowth of blood vessels and granulation tissues, and to regulate the MMP-2/TIMP-2 ratio to balance the degradation and deposition of the extracellular matrix.


Subject(s)
Cicatrix/genetics , Cicatrix/metabolism , Inflammation Mediators/metabolism , Macrophages/metabolism , Peptide Initiation Factors/genetics , Wound Healing , Animals , Antigens, Surface/metabolism , Biomarkers , Cluster Analysis , Disease Models, Animal , Gene Expression Profiling , Immunophenotyping , Macrophages, Peritoneal/immunology , Macrophages, Peritoneal/metabolism , Male , Matrix Metalloproteinase 2/metabolism , Mice , Mice, Knockout , Reproducibility of Results , Tissue Inhibitor of Metalloproteinase-2/metabolism
5.
Yi Chuan ; 28(4): 470-8, 2006 Apr.
Article in Chinese | MEDLINE | ID: mdl-16606602

ABSTRACT

The internet-based softwares SignalP v3.0, TargetP v1.01, big-PI predictor and TMHMM v2.0 were combined to predict the signal peptides and the signal peptide-dependent secreted proteins from the 19,855 ORFs in Caenorthaditis elegans ws123 genome. 1,990 proteins were predicted to be secreted and to contain signal peptides among 19,855 proteins, among which 1,936 have SignalPase I signal peptide (containing 41 with RR-motif signal peptide), 53 have SignalPase II signal peptide and one has SignalPase IV signal peptide. The signal peptides of 742 secreted proteins include only H-domain and C-domain, but no typical N-domain; the signal peptides of other 1,248 secreted proteins include all three domains. Although the amino acids constitution of the SignalPase I signal peptides were similar in general between Caenorthaditis elegans and prokaryote, there were apparently small differences, and the amino acid composition of Caenorthaditis elegans are more diverse and less conserved. But there are distinct differences on the amino acid composition of SignalPase II signal peptides. The signal peptides of Caenorthaditis elegans were more diverse than unicellular eukaryotic organism. The signal peptides of a few proteins were exactly the same. We used the BLAST 2 SEQUENECES aligning method to compare the homology among the secreted proteins with the same signal peptides. The alignment results indicated that the genes sharing the same signal peptide sequences were homologous to each other and were likely to have arisen from gene duplication.


Subject(s)
Caenorhabditis elegans Proteins/chemistry , Caenorhabditis elegans Proteins/metabolism , Caenorhabditis elegans/metabolism , Computational Biology/methods , Protein Sorting Signals/genetics , Algorithms , Amino Acid Sequence , Animals , Caenorhabditis elegans/chemistry , Caenorhabditis elegans/genetics , Conserved Sequence/physiology , Molecular Sequence Data , Peptides/metabolism , Protein Conformation , Protein Sorting Signals/physiology , Sequence Alignment , Sequence Analysis, Protein/methods , Sequence Homology, Amino Acid
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