scholarly journals Cold acclimation of Trogoderma granarium Everts is tightly linked to regulation of enzyme activity, energy content and ion concentration

2018 ◽  
Author(s):  
Mozhgan Mohammadzadeh ◽  
Hamzeh Izadi
Keyword(s):  
Molecular Weight ◽  
Protein Kinase ◽  
Cold Acclimation ◽  
Cold Tolerance ◽  
Exposure Time ◽  
Protein Phosphatase ◽  
Cold Hardiness ◽  
Glycogen Content ◽  
Thermal Reaction ◽  
Low Molecular Weight

ABSTRACTIn this study, cold hardiness and some physiological characteristics of T. granarium larvae were investigated under different thermal regimes, i.e. warm-acclimated (WA), cold-acclimated (CA), fluctuating-acclimated (FA) and rapid cold-hardened (RCH). In all regimes, the survival rate of the larvae decreased with a decrease in temperature and raise in exposure time. Cold acclimated larvae showed the highest cold hardiness in -15 and -20 ºC. Control larvae had the highest glycogen content (34.4 ± 2.3 µg/gdw). In contrast, cold acclimation larvae had the lowest glycogen content (23.0 ± 1.6 µg/gdw). Change in trehalose content was reversely proportional to change in glycogen content. The greatest myo-inositol and glucose contents were detected in larvae cold acclimation treatment (10.7 ± 0.4 µg/gdw) and control (0.49 ± 0.03 µg/gdw), respectively. In control and treated larvae, the concentration of Na+ decreased, though the concentration of K+ rose, with rising the exposure time. The shape of the thermal reaction of AMP-depended protein kinase and protein phosphatase IIC followed the same norm, which is different from protein phosphatase I and protein phosphatase IIA. Protein phosphatase IIA and IIC showed a complete difference in thermal reaction norms. In did, thermal fluctuation caused the highest changes in the activity of the enzymes, whereas the RCH showed the lowest changes in the activity of the enzyme. Our results showed a significant enhancement of larval cold tolerance under CA regime that is related to the level of low molecular weight carbohydrates, protein kinase, and phosphatases activity, and hemolymph ions concentration.SUMMARY STATEMENTIn Trogoderma granarium, cold acclimation enhances the larval cold tolerance that is related to change in the level of low molecular weight carbohydrates, protein kinase, and phosphatases activity, and hemolymph ions concentration.

scholarly journals Low‐molecular‐weight phosphotyrosyl protein phosphatase expression in brain of chicken and some lower vertebrates

2002 ◽  
Vol 69 (2) ◽  
pp. 97-102
Author(s):  
Livia Lucentini ◽  
Antonella Angiolillo ◽  
Emanuela Varasano ◽  
Fausto Panara
Keyword(s):  
Molecular Weight ◽  
Protein Phosphatase ◽  
Low Molecular Weight ◽  
Lower Vertebrates

scholarly journals Abundance of Low Molecular Weight Phosphotyrosine Protein Phosphatase in the Nerve-Ending Fraction in the Brain.

1999 ◽  
Vol 22 (8) ◽  
pp. 794-798 ◽  
Author(s):  
Hiroko TANINO ◽  
Jun-ichi YOSHIDA ◽  
Ryoji YAMAMOTO ◽  
Yumi KOBAYASHI ◽  
Shun SHIMOHAMA ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Nerve Ending ◽  
Protein Phosphatase ◽  
Low Molecular Weight ◽  
Phosphotyrosine Protein Phosphatase ◽  
The Brain

scholarly journals The effect of cold acclimation on the low molecular weight carbohydrate composition of safflower

Heliyon ◽  
2017 ◽  
Vol 3 (9) ◽  
pp. e00402 ◽  
Author(s):  
Erik J. Landry ◽  
Sam J. Fuchs ◽  
Vicki L. Bradley ◽  
R.C. Johnson
Keyword(s):  
Molecular Weight ◽  
Cold Acclimation ◽  
Low Molecular Weight ◽  
Carbohydrate Composition

Small GTPase-regulated phospholipase D in granulocytes

1996 ◽  
Vol 74 (4) ◽  
pp. 459-467 ◽  
Author(s):  
Martin G. Houle ◽  
Sylvain Bourgoin
Keyword(s):  
Molecular Weight ◽  
Protein Kinase ◽  
Phospholipase D ◽  
Tyrosine Kinases ◽  
Binding Proteins ◽  
Active Role ◽  
Small Gtpase ◽  
Low Molecular Weight ◽  
Gtp Binding Proteins ◽  
Gtp Binding

This review examines the functional role of phospholipase D in the neutrophil. Phospholipase D is emerging as an important component in the signal transduction pathways leading to granulocyte activation. Through the second messenger it produces, phosphatidic acid, phospholipase D plays an active role in the regulation of granulocyte NADPH oxidase activation and granular secretion. Many factors from both the cytosol and the membrane are necessary for maximal phospholipase D activation. This paper will focus on the regulation of phospholipase D by low molecular weight GTP-binding proteins, tyrosine kinases, and protein kinase C.Key words: phospholipase D, low molecular weight GTP-binding proteins, tyrosine kinases, protein kinase C, granulocytes.

scholarly journals Low molecular weight fibroblast growth factor-2 signals via protein kinase C and myofibrillar proteins to protect against postischemic cardiac dysfunction

2013 ◽  
Vol 304 (10) ◽  
pp. H1382-H1396 ◽  
Author(s):  
Janet R. Manning ◽  
Sarah O. Perkins ◽  
Elizabeth A. Sinclair ◽  
Xiaoqian Gao ◽  
Yu Zhang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Fibroblast Growth Factor ◽  
Cardiac Dysfunction ◽  
Fibroblast Growth Factor 2 ◽  
Low Molecular Weight ◽  
Fibroblast Growth ◽  
Kinase C

Among its many biological roles, fibroblast growth factor-2 (FGF2) acutely protects the heart from dysfunction associated with ischemia/reperfusion (I/R) injury. Our laboratory has demonstrated that this is due to the activity of the low molecular weight (LMW) isoform of FGF2 and that FGF2-mediated cardioprotection relies on the activity of protein kinase C (PKC); however, which PKC isoforms are responsible for LMW FGF2-mediated cardioprotection, and their downstream targets, remain to be elucidated. To identify the PKC pathway(s) that contributes to postischemic cardiac recovery by LMW FGF2, mouse hearts expressing only LMW FGF2 (HMWKO) were bred to mouse hearts not expressing PKCα (PKCαKO) or subjected to a selective PKCε inhibitor (εV1–2) before and during I/R. Hearts only expressing LMW FGF2 showed significantly improved postischemic recovery of cardiac function following I/R ( P < 0.05), which was significantly abrogated in the absence of PKCα ( P < 0.05) or presence of PKCε inhibition ( P < 0.05). Hearts only expressing LMW FGF2 demonstrated differences in actomyosin ATPase activity as well as increases in the phosphorylation of troponin I and T during I/R compared with wild-type hearts; several of these effects were dependent on PKCα activity. This evidence indicates that both PKCα and PKCε play a role in LMW FGF2-mediated protection from cardiac dysfunction and that PKCα signaling to the contractile apparatus is a key step in the mechanism of LMW FGF2-mediated protection against myocardial dysfunction.

Modulation of Ceramide-Activated Protein Phosphatase 2A Activity by Low Molecular Weight Aromatic Compounds

1998 ◽  
Vol 55 (7) ◽  
pp. 1105-1111 ◽  
Author(s):  
Lorenzo M. Leoni ◽  
Hsien C. Shih ◽  
Lynn Deng ◽  
Chuck Tuey ◽  
Gernot Walter ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Aromatic Compounds ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Low Molecular Weight ◽  
Phosphatase 2A
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