Transcripts and protein levels of CSN1S1 and CSN3 genes in dairy cattle mammary gland secretory tissue during chronic staphylococcal infection

2021 ◽  
Vol 88 (1) ◽  
pp. 73-77
Author(s):  
Ewelina Kawecka-Grochocka ◽  
Magdalena Zalewska ◽  
Aleksandra Kapusta ◽  
Tomasz Ząbek ◽  
Magdalena Rzewuska ◽  
...  
Keyword(s):  
Protein Level ◽  
Mrna Level ◽  
Milk Proteins ◽  
Staphylococcal Infection ◽  
Coagulase Negative Staphylococci ◽  
Post Translational Modifications ◽  
Protein Levels ◽  
Secretory Tissue ◽  
Cheese Curd ◽  
Coagulase Positive Staphylococci

AbstractOur objective was to determine the influence of chronic coagulase-positive staphylococci (CoPS) or coagulase-negative staphylococci (CoNS) infection on the mRNA and protein levels of two main milk proteins responsible for cheese curd quantity and quality, alpha-S1-casein (CSN1S1) and kappa-casein (CSN3). Measurements were made in cow mammary parenchyma with a prevalence of secretory tissue (MGST). Samples of MGST were collected from the separate quarters and divided into CoPS, CoNS and bacteria-free (H) groups according to the microbiological status of the quarter milk. No differences in CSN1S1 and CSN3 mRNA level were found between groups, however, CSN1S1 protein level was significantly higher in the H group than the CoNS group, and CSN3 protein level was significantly higher in H than CoPS group. Hence, while the CSN1S1 and CSN3 genes appear to be constitutively expressed at the mRNA level in dairy cow MGST during mastitis, CoNS infection negatively affected CSN1S1 protein level, and CoPS infection negatively affected CSN3 protein level. The lack of change at the mRNA level suggests that staphylococcal infection may affect the post-transcriptional or post-translational modifications.

scholarly journals Levels of G-proteins in liver and brain of lean and obese (ob/ob) mice

1992 ◽  
Vol 282 (1) ◽  
pp. 15-23 ◽  
Author(s):  
N McFarlane-Anderson ◽  
J Bailly ◽  
N Bégin-Heick
Keyword(s):  
Gene Expression ◽  
G Proteins ◽  
Protein Level ◽  
Mrna Level ◽  
Beta Subunits ◽  
Obese Mice ◽  
Protein Levels ◽  
Alpha Subunits ◽  
Brain Membranes ◽  
Liver Membranes

G-protein levels were assessed in liver and brain membranes of lean and obese mice. ADP-ribosylation and immunodetection studies revealed a decrease in the abundance of Gs and Gi alpha-subunits in the liver membranes of obese mice compared with lean mice. In contrast, in brain membranes, the abundance of these proteins was not significantly different between lean and obese mice. Studies at the mRNA level in both liver and brain revealed no difference in gene expression between lean and obese mice. Protein and mRNA studies both showed that Gs, Gi alpha 1, Gi alpha 2, Go alpha and G beta subunits are present in brain membranes, and Gi alpha 3 is barely detectable. In liver, Ga alpha, Gi alpha 2 and G beta subunits are the major constituents, whereas Gi alpha 1, Gi alpha 3 and Go alpha are barely detectable. It is possible that the differences observed at the protein level are due to different rates of translation of the mRNA. Different rates of release of the alpha-subunits from the membrane and/or different rates of degradation would also explain these results.

Aging influences cellular and molecular responses of apoptosis to skeletal muscle unloading

2005 ◽  
Vol 288 (2) ◽  
pp. C338-C349 ◽  
Author(s):  
Parco M. Siu ◽  
Emidio E. Pistilli ◽  
David C. Butler ◽  
Stephen E. Alway
Keyword(s):  
Satellite Cell ◽  
Muscle Atrophy ◽  
Protein Level ◽  
Mrna Level ◽  
Age Groups ◽  
Experimental Period ◽  
Immunofluorescent Staining ◽  
Cell Nuclei ◽  
Protein Levels ◽  
Nuclear Apoptosis

The influence of aging on skeletal myocyte apoptosis is not well understood. In this study we examined apoptosis and apoptotic regulatory factor responses to muscle atrophy induced via limb unloading following loading-induced hypertrophy. Muscle hypertrophy was induced by attaching a weight to one wing of young and aged Japanese quails for 14 days. Removing the weight for 7 or 14 days after the initial 14 days of loading induced muscle atrophy. The contralateral wing served as the intra-animal control. A time-released bromodeoxyuridine (BrdU) pellet was implanted subcutaneously with wing weighting to identify activated satellite cells/muscle precursor cells throughout the experimental period. Bcl-2 mRNA and protein levels decreased after 7 days of unloading, but they were unchanged after 14 days of unloading in young muscles. Bcl-2 protein level but not mRNA level decreased after 7 days of unloading in muscles of aged birds. Seven days of unloading increased the mRNA level of Bax in muscles from both young and aged birds. Fourteen days of unloading increased mRNA and protein levels of Bcl-2, decreased protein levels of Bax, and decreased nuclear apoptosis-inducing factor (AIF) protein level in muscles of aged birds. BrdU-positive nuclei were found in all unloaded muscles from both age groups, but the number of BrdU-positive nuclei relative to the total nuclei decreased after 14 days of unloading compared with 7 days of unloading. The TdT-mediated dUTP nick end labeling (TUNEL) index was higher after 7 days of unloading in both young and aged muscles and after 14 days of unloading in aged muscles. Immunofluorescent staining revealed that almost all of the TUNEL-positive nuclei were also BrdU immunopositive, suggesting that activated satellite cell nuclei (both fused and nonfused) underwent nuclear apoptosis during unloading. There were significant correlations among levels of Bcl-2, Bax, and AIF and TUNEL index. Our data are consistent with the hypothesis that apoptosis regulates, at least in part, unloading-induced muscle atrophy and loss of activated satellite cell nuclei in previously loaded muscles. Moreover, these data suggest that aging influences the apoptotic responses to prolonged unloading following hypertrophy in skeletal myocytes.

Differential regulation of G protein expression in rat hearts exposed to chronic hypoxia

1995 ◽  
Vol 269 (6) ◽  
pp. H1865-H1873 ◽  
Author(s):  
R. Kacimi ◽  
J. M. Moalic ◽  
A. Aldashev ◽  
D. E. Vatner ◽  
J. P. Richalet ◽  
...  
Keyword(s):  
Gene Expression ◽  
G Protein ◽  
Functional Activity ◽  
Protein Level ◽  
Chronic Hypoxia ◽  
Mrna Level ◽  
Mrna Levels ◽  
Protein Levels ◽  
Rat Hearts ◽  
And Function

Chronic hypoxia impairs adrenergic responsiveness. A modulation of Gs and/or G1 protein alpha-subunits may be associated with the downregulation of the beta-adrenergic receptors previously found in chronic hypoxia. G protein gene expression and protein level and function in rat hearts exposed to a 30-day hypobaric chronic hypoxia were compared with control rat hearts. No change was observed in G alpha s mRNA levels in either right or left ventricles. In right ventricles, mRNA levels of G alpha i-2 increased by 40% (P < 0.05), but not in left ventricles. In both left and right ventricles, chronic hypoxia did not modify G alpha i-2 and G alpha s protein amounts, but significantly decreased functional activity of G alpha s. In conclusion, gene expression, protein levels of G alpha s and G alpha i-2, and activity of G alpha s do not change in parallel fashion with chronic hypoxia. In chronic hypoxic right ventricles, although the mRNA level of G alpha i-2 is increased, the protein level is unchanged. One potential mechanism of desensitization to catecholamines in chronic hypoxia appears to involve a decreased functional activity of G alpha s in spite of normal mRNA and protein levels

scholarly journals Losartan Protects the Heart Against Ischemia Reperfusion Injury: Sirtuin3 Involvement

2015 ◽  
Vol 18 (1) ◽  
pp. 112 ◽  
Author(s):  
Mohsen Sharifi Klishadi ◽  
Farideh Zarei ◽  
Seyyed Hassan Hejazian ◽  
Ali Moradi ◽  
Mahdieh Hemati ◽  
...  
Keyword(s):  
Protein Level ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Mrna Level ◽  
Experimental Studies ◽  
Control Group ◽  
Signaling Mechanism ◽  
Survival Factors ◽  
Protein Levels ◽  
Ischemic Tissue

PURPOSE: Sirtuin-3 (SIRT3) deacetylase protects the heart against oxidative stress via survival factors upregulation. Clinical and experimental studies have demonstrated that activation of systemic and local renin-angiotensin system (RAS) is implicated in ischemia-induced cardiac injury. However, the relation between RAS and SIRT3 in pathophysiology of myocardial ischemia reperfusion is unknown. In this study, the cardiac transcription and expression of SIRT3 levels was examined in response to ischemia reperfusion in untreated and losartan treated rats. METHODS: Rats were divided into control group, losartan group (L), and ischemia reperfusion (IR) groups with (L+IR) or without losatran pretreatment. Some rats were included as sham-operated and saline groups. IR was induced by left anterior descending artery occlusion. SIRT3 protein levels were determined by Western blot technique. The genes expression was specified by real-time RT-PCR. Arrhythmias were assessed according to the Lambeth conventions. RESULTS: In L+IR group a significant reduction was noted in the number of ventricular ectopic beats (VEBs) and episodes of ventricular tachycardia (VT) (VEBs: P<0.001; VT: P<0.01 vs. IR). In IR group, SIRT3 protein level was decreased in the ischemic tissue by 26.7±5.9% (P<0.01 vs. Control). However, in the non-ischemic tissue the changes of SIRT3 protein content were not significant. In L+IR group SIRT3 protein levels in the ischemic part of Left ventricle were significantly different from IR group (P<0.001). SIRT3 mRNA level did not change significantly among the experimental groups. Thioredoxin-1 and catalase transcription level was increased in L+IR group compared to IR group (P<0.01). CONCLUSION: A decreased SIRT3 protein levels subsequent to IR might be a novel signaling mechanism involved in IR injury. Losartan at non–hypotensive dose exerts anti-ischemic effects in part by normalizing the SIRT3 protein level and upregulating the survival factors encoding genes transcription in ischemic tissue of the heart. This article is open to POST-PUBLICATION REVIEW. Registered readers (see “For Readers”) may comment by clicking on ABSTRACT on the issue’s contents page.

scholarly journals Reduction of serotonin receptor 2A protein level in peripheral blood lymphocytes during antipsychotic medication is biomarker of therapy safety

2020 ◽  
pp. 58-59
Author(s):  
А.М. Заботина ◽  
М.Н. Грунина ◽  
Е.В. Волкова ◽  
Р.Ф. Насырова ◽  
А.Е. Тараскина
Keyword(s):  
Peripheral Blood ◽  
Protein Level ◽  
Serotonin Receptor ◽  
Mrna Level ◽  
Peripheral Blood Lymphocytes ◽  
Antipsychotic Therapy ◽  
Blood Lymphocytes ◽  
Protein Levels ◽  
Potential Biomarker ◽  
Serotonin Receptor 2A

В лимфоцитах периферической крови (ЛПК) в группе пациентов с коморбидным течением шизофрении с синдромом алкогольной зависимости показаны более низкие значения количества белка рецептора 5-НТ2А и уровня его мРНК по сравнению с группой с неотягощенной психической патологией (р<0.001). Безопасная фармакотерапия ассоциирована со снижением количества рецептора 5-НТ2А в ЛПК на 28-й день без изменения уровня транскрипции гена, возможно вызванного интернализацией рецептора. We studied mRNA and protein levels of serotonin receptor 2A (5-НТ2А) in lymphocytes of schizophrenia patients both before and after 28 days of antipsychotic therapy in order to estimate biomarkers of efficacy and safety of the treatment. We found lower mRNA and protein levels of 5-НТ2А in peripheral blood lymphocytes (PBL) of schizophrenia patients with alcohol addiction syndrome than in PBL of schizophrenia patients without addictions (р<0.001). Absence of common adverse side effects (antipsychotic-induced weight gain, parkinsonism, akathisia) during antipsychotic therapy was associated with reduction of 5-НТ2А protein level in PBL by 28th day of the treatment, while HTR2A mRNA level was not changed. Reduction of 5-НТ2А protein level in PBL by 28th day may be a potential biomarker of the antipsychotic therapy safety.

scholarly journals Expression of cytokines in dairy cattle mammary gland parenchyma during chronic staphylococcal infection

2021 ◽  
Vol 52 (1) ◽  
Author(s):  
Ewelina Kawecka-Grochocka ◽  
Magdalena Zalewska ◽  
Magdalena Rzewuska ◽  
Ewa Kościuczuk ◽  
Tomasz Ząbek ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Staphylococcal Infection ◽  
Microbiological Analysis ◽  
Mrna Levels ◽  
Coagulase Negative Staphylococci ◽  
Protein Levels ◽  
Expression Of Genes ◽  
Holstein Friesian ◽  
Chemokine Ligand ◽  
Factor Α

AbstractThe study aim was to determine the expression of genes potentially related to chronic mastitis at the mRNA and protein levels, viz. chemokine C–C motif receptor 1 (CCR1), C–C motif chemokine ligand 2 (CCL2), C–C motif chemokine ligand 5 (CXCL5), tumor necrosis factor α (TNFα), interleukin 1β (IL-1β), interleukin 6 (IL-6), interleukin 8 (IL-8), interleukin 18 (IL-18), in bovine mammary gland parenchyma. The study examines the differences in expression of selected genes between cows with chronic mastitis caused by coagulase-positive (CoPS) or coagulase-negative staphylococci (CoNS) and those with healthy udders (H). Samples were collected from the udder quarters from 40 Polish Holstein–Friesian cows; 54 of these samples were chosen for analysis based on microbiological analysis of milk taken two days before slaughter. They were categorized into three groups: CoPS (N = 27), CoNS (N = 14) and H (N = 13). The RNA expression was analyzed by RT-qPCR and protein concentration by ELISA. No differences in the mRNA levels of seven genes (TNFα, IL-18, CCR1, IL-1β, CCL2, IL-8, IL-6) and four proteins (TNFα, IL-18, CCR1, IL-1β) were identified between the CoPS and H groups. Higher transcript levels of CXCL5 (p ≤ 0.05) gene were noted in CoPS than in H. Compared to H, higher concentrations of IL-8 and CXCL5 (p ≤ 0.05) were observed in CoPS (0.05 < p < 0.1) and CCL2 (0.05 < p < 0.1) in CoNS, while lower levels of Il-6 were found in CoPS. This may suggest that during chronic mastitis the organism stops producing pro-inflammatory cytokines, probably to protect the host tissues against their damage during prolonged infection.

Pengaruh Lama Pengasinan Terhadap Kadar Protein Putih Telur Itik

2014 ◽  
Vol 1 (1) ◽  
pp. 36 ◽  
Author(s):  
Siti Fatimah ◽  
Muji Rahayu ◽  
Siti Aminah
Keyword(s):  
Protein Level ◽  
Egg White ◽  
Special Treatment ◽  
Egg White Protein ◽  
Protein Levels ◽  
Duck Egg ◽  
Egg Period ◽  
Graph Presentation ◽  
And Control ◽  
The Impact

Background : Egg  is one of the animal protein source, which has delicious taste, easy to digest and highly nutritious. Besides its affordable price, its supply availability is unquestionable as well. However, due to its short storability, it requires special treatment, such as preserving, to store it for long period. One way to preserve the egg is by pickling egg, which generally requires seven to ten days of marinating. During the process of marinating, there will be a visual change of egg white and yolk. Their structures  will be more solid (the occurrence of thickening process) because salinization will lead to protein denaturalization. Consequently, it has an influence as well towards the content of egg white protein of duck egg. This study is aimed to explore the impact of various time of pickling egg towards egg white protein of duck egg. Method  : The study where takes place in a laboratories, is a true experimental study for the reason that the researcher must provide intervention, hence all of potentially confounding variables are manageable. Samples that had been used in this study are duck eggs which were bought from North Brebes. This study is expected to generate data from four various time of pickling egg and control (no treatment). Since there are four samples, accordingly the number of data resulted are twenty. The resulted data will be descriptively presented in table, graph, presentation, and narration. Result  : Protein level examination within duck white egg shows changes  in protein levels that occurs in every variation of pickling egg time, where the average results of the assay of duck egg white protein is 14.94% without treatment (control), in five days of pickling time is 13.68%, in seven days of pickling time is 13.29%, in nine days of pickling time is 12.87% and eleven days of pickling time is 12.78%. Conclusion  : There is a significant impact among the period of pickling time to the protein level degradation of duck white egg. Keywords : Duck egg, period of pickling time, level protein of duck white egg.

scholarly journals Post translational modifications of milk proteins in geographically diverse goat breeds

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
P. K. Rout ◽  
M. Verma
Keyword(s):  
Protein Function ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Goat Milk ◽  
Peptide Sequence ◽  
Cow Milk ◽  
Post Translational Modification ◽  
Post Translational Modifications ◽  
Functional Roles ◽  
Dpp Iv

AbstractGoat milk is a source of nutrition in difficult areas and has lesser allerginicity than cow milk. It is leading in the area for nutraceutical formulation and drug development using goat mammary gland as a bioreactor. Post translational modifications of a protein regulate protein function, biological activity, stabilization and interactions. The protein variants of goat milk from 10 breeds were studied for the post translational modifications by combining highly sensitive 2DE and Q-Exactive LC-MS/MS. Here we observed high levels of post translational modifications in 201 peptides of 120 goat milk proteins. The phosphosites observed for CSN2, CSN1S1, CSN1S2, CSN3 were 11P, 13P, 17P and 6P, respectively in 105 casein phosphopeptides. Whey proteins BLG and LALBA showed 19 and 4 phosphosites respectively. Post translational modification was observed in 45 low abundant non-casein milk proteins mainly associated with signal transduction, immune system, developmental biology and metabolism pathways. Pasp is reported for the first time in 47 sites. The rare conserved peptide sequence of (SSSEE) was observed in αS1 and αS2 casein. The functional roles of identified phosphopeptides included anti-microbial, DPP-IV inhibitory, anti-inflammatory and ACE inhibitory. This is first report from tropics, investigating post translational modifications in casein and non-casein goat milk proteins and studies their interactions.

scholarly journals Functional Comparison between VP64-dCas9-VP64 and dCas9-VP192 CRISPR Activators in Human Embryonic Kidney Cells

2021 ◽  
Vol 22 (1) ◽  
pp. 397
Author(s):  
Nasir Javaid ◽  
Thuong L. H. Pham ◽  
Sangdun Choi
Keyword(s):  
Protein Level ◽  
Reference Genes ◽  
Mrna Level ◽  
High Specificity ◽  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Human Embryonic Kidney Cells ◽  
Sox2 Expression

Reversal in the transcriptional status of desired genes has been exploited for multiple research, therapeutic, and biotechnological purposes. CRISPR/dCas9-based activators can activate transcriptionally silenced genes after being guided by gene-specific gRNA(s). Here, we performed a functional comparison between two such activators, VP64-dCas9-VP64 and dCas9-VP192, in human embryonic kidney cells by the concomitant targeting of POU5F1 and SOX2. We found 22- and 6-fold upregulations in the mRNA level of POU5F1 by dCas9-VP192 and VP64-dCas9-VP64, respectively. Likewise, SOX2 was up-regulated 4- and 2-fold using dCas9-VP192 and VP64dCas9VP64, respectively. For the POU5F1 protein level, we observed 3.7- and 2.2-fold increases with dCas9-VP192 and VP64-dCas9-VP64, respectively. Similarly, the SOX2 expression was 2.4- and 2-fold higher with dCas9-VP192 and VP64-dCas9-VP64, respectively. We also confirmed that activation only happened upon co-transfecting an activator plasmid with multiplex gRNA plasmid with a high specificity to the reference genes. Our data revealed that dCas9-VP192 is more efficient than VP64-dCas9-VP64 for activating reference genes.

scholarly journals A new non-aggregative splicing isoform of human Tau is decreased in Alzheimer’s disease

2021 ◽  
Author(s):  
Vega García-Escudero ◽  
Daniel Ruiz-Gabarre ◽  
Ricardo Gargini ◽  
Mar Pérez ◽  
Esther García ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neuroblastoma Cells ◽  
Rna Seq ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma ◽  
Post Translational Modifications ◽  
Protein Levels ◽  
Tau Isoform ◽  
Human Specific

AbstractTauopathies, including Alzheimer’s disease (AD) and frontotemporal lobar degeneration with Tau pathology (FTLD-tau), are a group of neurodegenerative disorders characterized by Tau hyperphosphorylation. Post-translational modifications of Tau such as phosphorylation and truncation have been demonstrated to be an essential step in the molecular pathogenesis of these tauopathies. In this work, we demonstrate the existence of a new, human-specific truncated form of Tau generated by intron 12 retention in human neuroblastoma cells and, to a higher extent, in human RNA brain samples, using qPCR and further confirming the results on a larger database of human RNA-seq samples. Diminished protein levels of this new Tau isoform are found by Westernblotting in Alzheimer’s patients’ brains (Braak I n = 3; Braak II n = 6, Braak III n = 3, Braak IV n = 1, and Braak V n = 10, Braak VI n = 8) with respect to non-demented control subjects (n = 9), suggesting that the lack of this truncated isoform may play an important role in the pathology. This new Tau isoform exhibits similar post-transcriptional modifications by phosphorylation and affinity for microtubule binding, but more interestingly, is less prone to aggregate than other Tau isoforms. Finally, we present evidence suggesting this new Tau isoform could be linked to the inhibition of GSK3β, which would mediate intron 12 retention by modulating the serine/arginine rich splicing factor 2 (SRSF2). Our results show the existence of an important new isoform of Tau and suggest that further research on this less aggregation-prone Tau may help to develop future therapies for Alzheimer’s disease and other tauopathies.

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