scholarly journals Molecular Characterization of Ca2+/Calmodulin-Dependent Protein Kinase II Isoforms in Three Rice Planthoppers—Nilaparvata lugens, Laodelphax striatellus, and Sogatella furcifera

2019 ◽  
Vol 20 (12) ◽  
pp. 3014
Author(s):  
Wei-Xia Wang ◽  
Feng-Xiang Lai ◽  
Pin-Jun Wan ◽  
Qiang Fu ◽  
Ting-Heng Zhu
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Variable Region ◽  
Nilaparvata Lugens ◽  
Laodelphax Striatellus ◽  
Sogatella Furcifera ◽  
Dependent Protein Kinase ◽  
Rice Planthoppers ◽  
Protein Kinase Ii ◽  
Dependent Protein

This study reports the identification of splice variants for the calcium/calmodulin-dependent protein kinase II (CaMKII) gene from Nilaparvata lugens, Laodelphax striatellus, and Sogatella furcifera. CaMKII is a multifunctional serine/threonine protein kinase that transduces Ca2+ signals in cells to control a range of cellular processes in the nervous system and muscular tissue. Sequence analysis showed that CaMKII was 99.0% identical at the amino acid level among three rice planthoppers, with the exception of a variable region located in the association domain. Four kinds of 20–81 amino acid “inserts” were found in the variable region. The phylogenetic tree of the deduced amino acid sequences showed that the NlCaMKII isoforms were more closely related to the LsCaMKII isoforms and were slightly distinct from SfCaMKII. CaMKII-E was the dominant type among the five main isoforms. CaMKII genes were constitutively expressed in various nymphal and adult stages and in tested tissues with the predominant transcription occurring in the head. There was no major tissue specificity of isoform expression, but the expression pattern and relative abundance of isoforms varied when compared with the RT-PCR between tissues. In addition, RNAi in N. lugens with dsRNA at a concentration of 200 ng nymph−1 induced a mortality of 77.7% on the 10th day and a reduction in the mRNA expression level of 67.2%. Unlike the holometabolous insect Helicoverpa armigera, the knockdown of NlCaMKII did not suppress the expression of 20E response genes, such as ECR, USP1, and HR3, in N. lugens. These results indicate that the role of CaMKII in hemimetabolous insects may be different from that in holometabolous insects.

scholarly journals The amino acid sequence of a hinge region in the regulatory subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase II

FEBS Letters ◽  
1980 ◽  
Vol 114 (1) ◽  
pp. 83-88 ◽  
Author(s):  
Koji Takio ◽  
Kenneth A. Walsh ◽  
Hans Neurath ◽  
Stephen B. Smith ◽  
Edwin G. Krebs ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Amino Acid Sequence ◽  
Cardiac Muscle ◽  
Hinge Region ◽  
Regulatory Subunit ◽  
Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein

scholarly journals Phosphorylation of the C-terminal domain of the Na+/H+ exchanger by Ca2+/calmodulin-dependent protein kinase II

1992 ◽  
Vol 282 (1) ◽  
pp. 139-145 ◽  
Author(s):  
L Fliegel ◽  
M P Walsh ◽  
D Singh ◽  
C Wong ◽  
A Barr
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Fusion Protein ◽  
Dependent Protein Kinase ◽  
Terminal Domain ◽  
Kinase C ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Beta Galactosidase

The Na+/H+ exchanger is a pH-regulatory protein that extrudes one H+ ion in exchange for one Na+ ion when intracellular pH declines. A number of studies have shown phorbol ester stimulation of activity in intact cells, leading to the idea that the exchanger is regulated by protein kinase C-mediated phosphorylation in vivo. cDNA encoding the protein has been cloned, and a recent model suggests a large internal cytoplasmic C-terminal domain that may be a site of regulation of the exchanger [Sardet, Franchi & Pouyssegur (1989) Cell 56, 271-280]. We examined this region of the protein using a rabbit cardiac Na+/H+ exchanger cDNA clone. cDNA of the Na+/H+ exchanger, coding for the C-terminal 178 amino acid residues, was cloned into the expression vector pEX-1 and expressed as a fusion protein with beta-galactosidase. The fusion protein reacted with an antibody produced against a synthetic peptide of the C-terminal 13 amino acid residues of the Na+/H+ exchanger, confirming the identity of the expressed protein. Control and experimental pEX-1-Na+/H+ exchanger protein was purified on a p-aminophenyl beta-D-thiogalactopyranoside-agarose column. Purified Ca2+/calmodulin-dependent protein kinase II readily phosphorylated the Na+/H+ exchanger protein in a Ca(2+)- and calmodulin-dependent manner in vitro, but this region of the protein was not a substrate for purified protein kinase C or for the catalytic subunit of cyclic AMP-dependent protein kinase. Control-expressed beta-galactosidase was phosphorylated to a maximal level of 0.77 +/- 0.17 mol of Pi/mol (mean +/- S.E.M., n = 6) whereas the fusion protein was phosphorylated to a maximal level of 4.09 +/- 0.39 mol of Pi/mol (n = 6), suggesting one site of phosphorylation in beta-galactosidase and three in the C-terminal domain of the Na+/H+ exchanger. Examination of the deduced amino acid sequence of this part of the exchanger reveals three consensus sequences for Ca2+/calmodulin-dependent protein kinase II. These results suggest that the exchanger may be directly regulated in vivo by calmodulin-dependent protein kinase II but not by protein kinase C or cyclic AMP-dependent protein kinase.

scholarly journals Critical amino acid residues of AIP, a highly specific inhibitory peptide of calmodulin-dependent protein kinase II

FEBS Letters ◽  
1998 ◽  
Vol 427 (1) ◽  
pp. 115-118 ◽  
Author(s):  
Atsuhiko Ishida ◽  
Yasushi Shigeri ◽  
Yoshiro Tatsu ◽  
Koichi Uegaki ◽  
Isamu Kameshita ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Residues ◽  
Inhibitory Peptide ◽  
Dependent Protein Kinase ◽  
Critical Amino Acid ◽  
Protein Kinase Ii ◽  
Dependent Protein

scholarly journals Characterization of Ca2+/calmodulin-dependent protein kinase II from smooth muscle

1995 ◽  
Vol 310 (2) ◽  
pp. 517-525 ◽  
Author(s):  
Z H L Zhou ◽  
S Ando ◽  
D Furutsuka ◽  
M Ikebe
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Variable Region ◽  
Serine Phosphorylation ◽  
Active Enzyme ◽  
Dependent Protein Kinase ◽  
Rapid Phase ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Constitutively Active

We have characterized chicken gizzard smooth muscle Ca2+/calmodulin-dependent protein kinase II (CaM-PKII) with particular focus on its autophosphorylation. The autophosphorylation of smooth muscle CaMPKII produced a partially constitutively active enzyme, as occurs with the alpha- and beta-isoforms of this enzyme, but the autophosphorylation kinetics were significantly slower. Phosphorylation during the initial rapid phase coincided with the production of constitutively active enzyme. The phosphorylation was on both serine and threonine residues, which is distinct from the brain enzyme where threonine phosphorylation is much faster and more prevalent than serine phosphorylation. The major autophosphorylation sites identified were different from the known autophosphorylation sites of the alpha- and beta-isoforms. During the initial autophosphorylation phase Ser-319, Ser-352 and a Thr residue within residues 345-368 were found to be phosphorylated. During the subsequent gradual phase two serine residues in the variable region and Ser-280 were phosphorylated, but Thr-286 and Thr-305, which are the known major autophosphorylation sites for the alpha- and beta-isoforms, were not detected as the major autophosphorylation sites of smooth muscle CaMPKII. By comparing the phosphopeptide sequence with the known sequences of various isoforms, we concluded that isoform gamma-b, which contains a unique insertion and two deletions at the C-terminal side of the calmodulin binding domain, is the dominant CaMPKII isoform in smooth muscle. The molecular mass of smooth muscle CaMPKII was estimated to be 240 kDa which would comprise four subunits, fewer than in the alpha- and beta-isoforms. The results show that smooth muscle CaMPKII is functionally distinct from the alpha- and beta-isoforms of this enzyme, which might be crucial for its physiological relevance.

scholarly journals New isoforms of Ca2+/calmodulin-dependent protein kinase II in smooth muscle

1994 ◽  
Vol 299 (2) ◽  
pp. 489-495 ◽  
Author(s):  
Z L Zhou ◽  
M Ikebe
Keyword(s):  
Smooth Muscle ◽  
Alternative Splicing ◽  
Protein Kinase ◽  
Variable Region ◽  
Rat Aorta ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein

Four novel isoforms of Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) were found in rat aorta smooth muscle. Two of them were related to gamma-isoform of brain CaM kinase II (gamma-a). Differences in the primary structure of these isoforms were located in the variable region. One of them (gamma-b) contained 23 unique amino acid residues, whereas the other (gamma-c) did not contain this sequence. Both isoforms lacked the two segments (Val-316 to Gln-337 and Lys-353 to Leu-362) present in gamma-a. The DNA sequence of these gamma-isoforms except the variable region was exactly the same, suggesting that they are produced by alternative splicing. Another two isoforms were related to the delta-isoform of brain CaM kinase II (delta-a). delta-b contained a unique 11-residue sequence in the variable region whereas delta-c did not. As found for gamma-isoforms, the sequence analysis suggested that the three delta-isoforms are also produced by alternative splicing. Analysis of RNA by reverse transcription PCR confirmed the existence of specific messages for gamma-b, delta-a and delta-b. The variety of isoforms of CaM kinase II suggest that each isoform may play a specialized role in cell regulation.

Scutellarin Mitigates Cancer-Induced Bone Pain by Suppressing CaMKII/CREB Pathway in Rat Models

2019 ◽  
Vol 17 (3) ◽  
pp. 249-253
Author(s):  
Liu Chenglong ◽  
Liu Haihua ◽  
Zhang Fei ◽  
Zheng Jie ◽  
Wei Fang
Keyword(s):  
Protein Kinase ◽  
Bone Pain ◽  
Binding Protein ◽  
Camp Response Element Binding ◽  
Camp Response Element ◽  
Dependent Protein Kinase ◽  
Response Element ◽  
Protein Kinase Ii ◽  
Element Binding Protein ◽  
Dependent Protein

Cancer-induced bone pain is a severe and complex pain caused by metastases to bone in cancer patients. The aim of this study was to investigate the analgesic effect of scutellarin on cancer-induced bone pain in rat models by intrathecal injection of Walker 256 carcinoma cells. Mechanical allodynia was determined by paw withdrawal threshold in response to mechanical stimulus, and thermal hyperalgesia was indicated by paw withdrawal latency in response to noxious thermal stimulus. The paw withdrawal threshold and paw withdrawal latencies were significantly decreased after inoculation of tumor cells, whereas administration of scutellarin significantly attenuated tumor cell inoculation-induced mechanical and heat hyperalgesia. Tumor cell inoculation-induced tumor growth was also significantly abrogated by scutellarin. Ca2+/calmodulin-dependent protein kinase II is a multifunctional kinase with up-regulated activity in bone pain models. The activation of Ca2+/calmodulin-dependent protein kinase II triggers phosphorylation of cAMP-response element binding protein. Scutellarin significantly reduced the expression of phosphorylated-Ca2+/calmodulin-dependent protein kinase II and phosphorylated-cAMP-response element binding protein in cancer-induced bone pain rats. Collectively, our study demonstrated that scutellarin attenuated tumor cell inoculation-induced bone pain by down-regulating the expression of phosphorylated-Ca2+/calmodulin-dependent protein kinase II and phosphorylated-cAMP-response element binding protein. The suppressive effect of scutellarin on phosphorylated-Ca2+/calmodulin-dependent protein kinase II/phosphorylated-cAMP-response element binding protein activation may serve as a novel therapeutic strategy for CIBP management.

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