Vegetative storage protein expression during terminal bud formation in poplar

2001 ◽  
Vol 31 (6) ◽  
pp. 1098-1103 ◽  
Author(s):  
Susan D Lawrence ◽  
Janice EK Cooke ◽  
John S Greenwood ◽  
Theresa E Korhnak ◽  
John M Davis
Keyword(s):  
Protein Expression ◽  
Shoot Apex ◽  
Storage Protein ◽  
Messenger Rna ◽  
Storage Proteins ◽  
N Cycling ◽  
Mrna Levels ◽  
Vegetative Storage Protein ◽  
Bud Formation ◽  
Terminal Bud

Trees recycle nitrogen (N) to conserve this valuable nutrient. The processes that regulate N recycling within trees are poorly understood at the molecular level. Because vegetative storage proteins (VSPs) are thought to play important roles in within-plant N cycling, we are investigating the expression of VSP genes to gain insights into how seasonally controlled N cycling is regulated in trees. We compared steady-state mRNA levels of three different VSP homologs during short day induced terminal bud formation in hybrid poplar (Populus trichocarpa Torr. & Gray × Populus deltoides Bartr. ex Marsh.) – WIN4 (wound-inducible protein 4), BSP (bark storage protein), and pni288 (poplar nitrogen-regulated cDNA 288, a newly identified sequence). We determined that win4 and pni288 transcripts decrease, while bsp transcripts increase, as the terminal bud is formed. Immunolocalization analysis indicated that, during apical bud formation, BSP accumulates in the ground meristem and in parenchyma cells adjacent to xylem and proximal to the apical dome. Based on messenger RNA and protein expression analysis, we conclude that different VSPs play distinct roles in the poplar shoot apex, with BSP accumulating as a reserve near the shoot apex during terminal bud formation.

scholarly journals The Role of RNA-Binding Protein OsTudor-SN in Post-Transcriptional Regulation of Seed Storage Proteins and Endosperm Development

2019 ◽  
Vol 60 (10) ◽  
pp. 2193-2205
Author(s):  
Hong-Li Chou ◽  
Li Tian ◽  
Masako Fukuda ◽  
Toshihiro Kumamaru ◽  
Thomas W Okita
Keyword(s):  
Protein Expression ◽  
Seed Development ◽  
Storage Protein ◽  
Rna Binding ◽  
Storage Proteins ◽  
Protein Body ◽  
Grain Weight ◽  
Protein Accumulation ◽  
Body Type ◽  
Body Formation

Abstract Tudor-SN is involved in a myriad of transcriptional and post-transcriptional processes due to its modular structure consisting of 4 tandem SN domains (4SN module) and C-terminal Tsn module consisting of Tudor-partial SN domains. We had previously demonstrated that OsTudor-SN is a key player for transporting storage protein mRNAs to specific ER subdomains in developing rice endosperm. Here, we provide genetic evidence that this multifunctional RBP is required for storage protein expression, seed development and protein body formation. The rice EM1084 line, possessing a nonsynonymous mutation in the 4SN module (SN3 domain), exhibited a strong reduction in grain weight and storage protein accumulation, while a mutation in the Tudor domain (47M) or the loss of the Tsn module (43M) had much smaller effects. Immunoelectron microscopic analysis showed the presence of a new protein body type containing glutelin and prolamine inclusions in EM1084, while 43M and 47M exhibited structurally modified prolamine and glutelin protein bodies. Transcriptome analysis indicates that OsTudor-SN also functions in regulating gene expression of transcriptional factors and genes involved in developmental processes and stress responses as well as for storage proteins. Normal protein body formation, grain weight and expression of many genes were partially restored in EM1084 transgenic line complemented with wild-type OsTudor-SN gene. Overall, our study showed that OsTudor-SN possesses multiple functional properties in rice storage protein expression and seed development and that the 4SN and Tsn modules have unique roles in these processes.

A vegetative storage protein homolog is expressed in the growing shoot apex of hybrid poplar

Planta ◽  
1997 ◽  
Vol 203 (2) ◽  
pp. 237-244 ◽  
Author(s):  
Susan D. Lawrence ◽  
John S. Greenwood ◽  
Theresa E. Korhnak ◽  
John M. Davis
Keyword(s):  
Shoot Apex ◽  
Storage Protein ◽  
Hybrid Poplar ◽  
Vegetative Storage Protein ◽  
Growing Shoot

Effects of environmental factors and endogenous signals on N uptake, N partitioning and taproot vegetative storage protein accumulation in Medicago sativa

2001 ◽  
Vol 28 (4) ◽  
pp. 279 ◽  
Author(s):  
Carine Noquet ◽  
Jean-Christophe Avice ◽  
Alain Ourry ◽  
Jeffrey J. Volenec ◽  
Suzanne M. Cunningham ◽  
...  
Keyword(s):  
Low Temperature ◽  
Medicago Sativa ◽  
Methyl Jasmonate ◽  
Storage Proteins ◽  
N Uptake ◽  
Protein Accumulation ◽  
N Availability ◽  
Mrna Levels ◽  
Vegetative Storage Protein ◽  
N Partitioning

Our objectives were to study the regulation of N partitioning within tissues of non-nodulated alfalfa (Medicago sativa L.) and N storage in taproots as vegetative storage proteins (VSP) of 15, 19, and 32 kDa and β-amylase (57 kDa) by environmental (photoperiod, temperature, N availability) and endogenous factors (methyl jasmonate). When compared to long-day conditions (LD, 16 h day/8 h night), short-day (SD, 8 h day/16 h night), exposure to low temperature (5˚C) or application of methyl jasmonate (MeJA, 100 M ) for 35 d reduced the biomass shoot/ root ratio and modified the source–sink relationships for N. SD and MeJA treatments resulted in partitioning of N to taproots and a concomitant accumulation of VSPs. In comparison with LD, SD treatment also stimulated β-amylase gene expression 2.5-fold. Although low temperature increased the N partitioning to root tissues and the accumulation of soluble proteins in taproot, VSP concentration and β-amylase mRNA levels remained low. Increasing N concentration from 1 to 5 mM KNO3 doubled the total dry matter but did not affect the N partitioning within the plant, VSP accumulation, or ‚ β-amylase expression. These results suggested that short photoperiod can result in preferential N allocation toward taproots with a concomitant induction of VSP accumulation.

Elevated cytosolic phospholipase A2 expression and activity in human neutrophils during sepsis

Blood ◽  
2000 ◽  
Vol 95 (2) ◽  
pp. 660-665 ◽  
Author(s):  
R. Levy ◽  
R. Dana ◽  
I. Hazan ◽  
I. Levy ◽  
G. Weber ◽  
...  
Keyword(s):  
Protein Expression ◽  
Phospholipase A2 ◽  
Clinical Setting ◽  
Messenger Rna ◽  
Mrna Level ◽  
Neutrophil Function ◽  
Human Neutrophils ◽  
Clinical Settings ◽  
Mrna Levels ◽  
Cytosolic Phospholipase

Sepsis is defined as the systemic inflammatory response to infection. Phospholipase A2 (PLA2) plays an important role in inflammation processes by initiating the production of inflammatory mediators. The role of cytosolic PLA (cPLA2) has not yet been identified in inflammatory and infectious disease clinical settings. The aim of the present research was to determine whether cPLA2 activity has a role during sepsis. Since neutrophil activation has been documented during sepsis, these cells were chosen as a model to evaluate the function of cPLA2 in this clinical setting. cPLA2 was studied at 3 levels: activity, protein expression, and messenger RNA (mRNA). Neutrophils from 32 septic patients with and without bacteremia were examined. cPLA2 activity was measured using labeled phosphatidyl choline vesicles as a substrate, and total PLA2 was determined by the release of labeled arachidonic acid from prelabeled cells. A significant increase in cPLA2activity, protein expression, and total PLA2 activity in neutrophils was detected during sepsis. mRNA levels, detected by reverse transcriptase–polymerase chain reaction, were significantly higher during sepsis, indicating that the increase in the amount of cPLA2 is regulated on the mRNA level. The significant elevation of cPLA2 activity and expression in neutrophils during sepsis suggests that this enzyme plays a major role in neutrophil function in this clinical setting.

Interactions of airborne methyl jasmonate with vegetative storage protein gene and protein accumulation and biomass partitioning in Populus plants

2000 ◽  
Vol 30 (7) ◽  
pp. 1106-1113 ◽  
Author(s):  
T Beardmore ◽  
S Wetzel ◽  
M Kalous
Keyword(s):  
Methyl Jasmonate ◽  
Storage Protein ◽  
Storage Proteins ◽  
Nitrogen Concentration ◽  
Protein Accumulation ◽  
Vegetative Storage Protein ◽  
Short Term ◽  
Specific Expression ◽  
Vegetative Storage Proteins

In young poplar (Populus nigra Muench × Populus maximowiczii A. Henry) plants, vegetative storage proteins (VSPs), the bark storage protein (BSP), and (or) wound-inducible 4 protein (WIN4) mRNAs were present in the apical and basal leaves and in the basal leaves, respectively. VSPs accumulated in the apical leaves and to a lesser extent in the stem. The response of the plants to 20 µM airborne methyl jasmonate (MJ) was examined in four parts ( apical and basal leaves, stem, and roots) in both short-term (within 72 h) and long-term (1, 2, 3, and 4 weeks) experiments. In the short-term, MJ-treated plants either induced or increased the part-specific expression of win4 and bsp, and accumulation of BSP and (or) WIN4. In the long-term, MJ treatment resulted in part-specific alterations in protein and nitrogen concentration and further altered BSP and WIN4 accumulation. The MJ-treated plants increased both the biomass allocation to the stem, without a change in the relative growth rate, and the tolerance low temperature (-2°C). Together, these results suggest the BSP and WIN4 are both involved in short-term N cycling and that exogenous MJ treatment promotes changes in nitrogen metabolism in poplar.

MiR-493 Induces Cytotoxic Autophagy in Prostate Cancer Cells through Regulation on PHLPP2

2020 ◽  
Vol 21 (14) ◽  
pp. 1451-1456 ◽  
Author(s):  
Jun Deng ◽  
Ming Ma ◽  
Wei Jiang ◽  
Liangliang Zheng ◽  
Suping Cui
Keyword(s):  
Prostate Cancer ◽  
Protein Expression ◽  
Cell Function ◽  
Mrna Levels ◽  
Prostate Cancer Cells ◽  
Potent Inducer ◽  
Qrt Pcr ◽  
Autophagy Gene ◽  
The Relationship ◽  
Cancer Inhibition

Background: MiR-493 promotes the proliferation of prostate cancer (PC) cells by targeting PHLPP2. We aimed to explore the relationship between miR-493 and autophagy in PC. Methods: qRT-PCR and western blotting were used to determine the mRNA levels and protein expression of miR-493, PHLPP2, autophagy gene BECN1 and ATG7 in PC cells. The autophagy gene expression was determined after PC cells transfected with miR-493 precursor or PHLPP2 precursor. Corresponding changes of autophagy phenotype and PC cell function were also studied. Results: The mRNA levels and protein expression of miR-493, PHLPP2, BECN1 and ATG7 in PC cells were significantly decreased in PC cells. Overexpression of miR-493 or PHLPP2 markedly upregulated the expression levels of BECN1 and ATG7 in PC cells. Overexpression of miR-493 and PHLPP2 markedly promoted autophagy, and inhibited the invasion and cloning formation of PC cells. Conclusion: MiR-493 is a potent inducer of cytotoxic autophagy that leads to prostate cancer inhibition by regulating on PHLPP2.

Very Early Exercise Rehabilitation After Intracerebral Hemorrhage Promotes Inflammation in the Brain

2021 ◽  
pp. 154596832110063
Author(s):  
Keigo Tamakoshi ◽  
Madoka Maeda ◽  
Shinnosuke Nakamura ◽  
Nae Murohashi
Keyword(s):  
Intracerebral Hemorrhage ◽  
Protein Expression ◽  
Brain Regions ◽  
Motor Dysfunction ◽  
Inflammatory Factors ◽  
Mrna Levels ◽  
Exercise Rehabilitation ◽  
Early Exercise ◽  
Polymerase Chain ◽  
To Receive

Background Very early exercise has been reported to exacerbate motor dysfunction; however, its mechanism is largely unknown. Objective This study examined the effect of very early exercise on motor recovery and associated brain damage following intracerebral hemorrhage (ICH) in rats. Methods Collagenase solution was injected into the left striatum to induce ICH. Rats were randomly assigned to receive placebo surgery without exercise (SHAM) or ICH without (ICH) or with very early exercise within 24 hours of surgery (ICH+VET). We observed sensorimotor behaviors before surgery, and after surgery preexercise and postexercise. Postexercise brain tissue was collected 27 hours after surgery to investigate the hematoma area, brain edema, and Il1b, Tgfb1, and Igf1 mRNA levels in the striatum and sensorimotor cortex using real-time reverse transcription polymerase chain reaction. NeuN, PSD95, and GFAP protein expression was analyzed by Western blotting. Results We observed significantly increased skillful sensorimotor impairment in the horizontal ladder test and significantly higher Il1b mRNA levels in the striatum of the ICH+VET group compared with the ICH group. NeuN protein expression was significantly reduced in both brain regions of the ICH+VET group compared with the SHAM group. Conclusion Our results suggest that very early exercise may be associated with an exacerbation of motor dysfunction because of increased neuronal death and region-specific changes in inflammatory factors. These results indicate that implementing exercise within 24 hours after ICH should be performed with caution.

Hepatocellular expression of glucose-6-phosphatase is unaltered during hepatic regeneration

1998 ◽  
Vol 275 (4) ◽  
pp. G717-G722 ◽  
Author(s):  
Wisam F. Zakko ◽  
Carl L. Berg ◽  
John L. Gollan ◽  
Richard M. Green
Keyword(s):  
Gene Expression ◽  
Enzyme Activity ◽  
Protein Expression ◽  
Partial Hepatectomy ◽  
Initial Phase ◽  
Physiological Function ◽  
Liver Homogenate ◽  
Hepatic Regeneration ◽  
Mrna Levels ◽  
Microsomal Enzyme

Gluconeogenesis and glycogenolysis are essential hepatic functions required for glucose homeostasis. During the initial phase of hepatic regeneration, the immediate-early genes (IEG) are rapidly expressed, and the IEG RL-1 encodes for glucose-6-phosphatase (G-6- Pase). G-6- Pase is a microsomal enzyme essential for gluconeogenesis and glycogenolysis. This study employs a partial-hepatectomy model to examine the expression and activity of G-6- Pase. After partial hepatectomy, rat hepatic G-6- Pase gene expression is transcriptionally regulated, and mRNA levels are increased ≈30-fold. However, in contrast to this rapid gene induction, microsomal enzyme activity is unchanged after partial hepatectomy. Western blotting demonstrates that microsomal G-6- Pase protein expression is also unchanged after partial hepatectomy, and similar results are also noted in whole liver homogenate. Thus, despite marked induction in gene expression of the IEG G-6- Pase after partial hepatectomy, protein expression and enzyme activity remain unchanged. These data indicate that, although this hepatocyte IEG is transcriptionally regulated, the physiologically important level of regulation is posttranscriptional. This highlights the importance of correlating gene expression of IEG with protein expression and physiological function.

scholarly journals Sesamin Modulates Tyrosine Hydroxylase, Superoxide Dismutase, Catalase, Inducible No Synthase and Interleukin-6 Expression in Dopaminergic Cells Under Mpp+-Induced Oxidative Stress

2008 ◽  
Vol 1 (1) ◽  
pp. 54-62 ◽  
Author(s):  
Vicky Lahaie-Collins ◽  
Julie Bournival ◽  
Marilyn Plouffe ◽  
Julie Carange ◽  
Maria-Grazia Martinoli
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Tyrosine Hydroxylase ◽  
Protein Expression ◽  
Pc12 Cells ◽  
Interleukin 6 ◽  
Estrogen Receptor Alpha ◽  
Strong Increase ◽  
Mrna Levels ◽  
Neuronal Pc12 Cells

Oxidative stress is regarded as a mediator of nerve cell death in several neurodegenerative disorders, such as Parkinson's disease. Sesamin, a lignan mainly found in sesame oil, is currently under study for its anti-oxidative and possible neuroprotective properties. We used 1-methyl-4-phenyl-pyridine (MPP+) ion, the active metabolite of the potent parkinsonism-causing toxin 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine, to produce oxidative stress and neurodegeneration in neuronal PC12 cells, which express dopamine, as well as neurofilaments. Our results show that picomolar doses of sesamin protected neuronal PC12 cells from MPP+-induced cellular death, as revealed by colorimetric measurements and production of reactive oxygen species. We also demonstrated that sesamin acted by rescuing tyrosine hydroxylase levels from MPP+-induced depletion. Sesamin, however, did not modulate dopamine transporter levels, and estrogen receptor-alpha and -beta protein expression. By examining several parameters of cell distress, we found that sesamin also elicited a strong increase in superoxide dismutase activity as well as protein expression and decreased catalase activity and the MPP+stimulated inducible nitric oxide synthase protein expression, in neuronal PC12 cells. Finally, sesamin possessed significant anti-inflammatory properties, as disclosed by its potential to reduce MPP+-induced interleukin-6 mRNA levels in microglia. From these studies, we determined the importance of the lignan sesamin as a neuroprotective molecule and its possible role in complementary and/or preventive therapies of neurodegenerative diseases.

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