• Title/Summary/Keyword: calcium binding protein

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RELATIONSHIPS BETWEEN EGGSHELL QUALITY AND BIOCHEMICAL PARAMETERS OF CALCIUM METABOLISM

  • Kang, C.W.;Nam, K.T.;Olson, O.E.;Carlson, C.W.
    • Asian-Australasian Journal of Animal Sciences
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    • v.9 no.6
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    • pp.715-722
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    • 1996
  • To determine relationships of biochemical parameters involved in Ca metabolism with eggshell quality, serum Ca level, duodenal and uterine calcium binding protein (CaBP) and uterine carbonic anhydrase (CA) activities were measured using 102-week old hens. Three groups of chickens were selected, those showing high quality (HQ) and low quality (LQ) eggshells and non-laying activity (NE). NE hens exhibited significantly (p < 0.05) lower serum Ca levels than laying hens. HQ and LQ hens were not different in the Ca level, indicating that serum Ca level was not good indicator of hen's ability to produce different quality eggshells. Duodenal CaBPs was highest in HQ and lowest in NE (p < 0.10). Uterine CaBPs of LQ and NE were not different and lower significantly (p<0.10) than that of HQ, suggesting that CaBP played an important role in determining eggshell quality. Uterine CA activities of the three groups were significantly different (p < 0.01) ; highest in HQ and lowest in NE, suggesting intimate relationship between CA and Eggshell quality.

A Proteomic Screen for Presynaptic Terminal N-type Calcium Channel (CaV2.2) Binding Partners

  • Khanna, Rajesh;Zougman, Alexandre;Stanley, Elise F.
    • BMB Reports
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    • v.40 no.3
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    • pp.302-314
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    • 2007
  • N type calcium channels (CaV2.2) play a key role in the gating of transmitter release at presynaptic nerve terminals. These channels are generally regarded as parts of a multimolecular complex that can modulate their open probability and ensure their location near the vesicle docking and fusion sites. However, the proteins that comprise this component remain poorly characterized. We have carried out the first open screen of presynaptic CaV2.2 complex members by an antibody-mediated capture of the channel from purified rat brain synaptosome lysate followed by mass spectroscopy. 589 unique peptides resulted in a high confidence match of 104 total proteins and 40 synaptosome proteome proteins. This screen identified several known CaV2.2 interacting proteins including syntaxin 1, VAMP, protein phosphatase 2A, $G_{o\alpha}$, G$\beta$ and spectrin and also a number of novel proteins, including clathrin, adaptin, dynamin, dynein, NSF and actin. The unexpected proteins were classified within a number of functional classes that include exocytosis, endocytosis, cytoplasmic matrix, modulators, chaperones, and cell-signaling molecules and this list was contrasted to previous reports that catalogue the synaptosome proteome. The failure to detect any postsynaptic density proteins suggests that the channel itself does not exhibit stable trans-synaptic attachments. Our results suggest that the channel is anchored to a cytoplasmic matrix related to the previously described particle web.

Effects of Calcium on Nitric oxide (NO)-induced Adventitious Rooting Process in Radish (Raphanus sativus L.) Cotyledons (무 (Raphanus sativus L.) 자엽에서 산화질소 (Nitric oxide)에 의해 유도된 부정근 형성과정에 대한 칼슘의 효과)

  • Jin, Chang-Duck
    • Journal of Plant Biotechnology
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    • v.34 no.3
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    • pp.213-221
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    • 2007
  • The treatment of radish cotyledons with a nitric oxide (NO)-releasing substance, sodium nitroprusside (SNP) resulted in an increased adventitious root development in a dose-dependent manner. However, this NO-mediated enhancement effect was reversed when either 0.5 mM EGTA (an extracellular $Ca^{2+}$ chelator) or 0.1 mM $LaCl_3$ (a calcium channel blocker) was applied with $50\;{\mu}M$ SNP. Our results also showed that guaiacol peroxidase (GPX) and syringaldazine peroxidase (SPX) activities, which are known to play a key role in rooting, were more largely increased during adventitious root induction in the cotyledons treated with SNP. However, the treatment of cotyledons with SNP plus $LaCl_3$ inhibited the SNP-induced increases in the activities of both GPX and SPX. Trifluoperazine (TFP), an antagonist of calmodulin (a specific calcium-binding protein), also delayed adventitious root formation and significantly reduced the root length and number of the SNP-treated cotyledons as well as the deactivation of GPX and SPX enzymes. In conclusion, our results suggest that calcium is involved in the NO response leading to induction of adventitious root through a regulation of GPX and SPX.

Relationships between in-vitro virulence-associated characteristics, plasmid-bearing and production of Outer Membrane Protein(OMP) of Yersinia enterocolitica isolated from pigs (Yersinia enterocolitica의 시험관내 병원성 성상, plasmid 보유 및 외막 단백질(OMP) 생산간의 관계)

  • Park, Seog-gee;Choi, Chul-soon;Jeon, Yun-seong
    • Korean Journal of Veterinary Research
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    • v.32 no.2
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    • pp.181-194
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    • 1992
  • Two hundred and eighty nine strains of Yersinia enterocolitica isolated from healthy pigs were tested for the presence of 40~50 Megadalton virulence-associated plasmids and plasmidmediated in vitro virulence-associated properties, i.e., congo red uptake, calcium dependency, autoagglutination, CRMOX reaction, crystal violet binding and pyrazinamidase reaction. The correlationships between in vitro virulence-associated properties and the presence of 220 Kdalton outer membrane protein(OMP) were examined in strains with or without virulence-associated plasmids. The correlationships between the presence of plasmids on the production of the OMP and the expression of in vitro virulence-associated properties were studied with $CRMOX^+$ strains and acridine orangecured $CRMOX^-$ mutants. The results were as follows : 1. Of the in vitro virulence-associated tests with 289 strains of Y enterocolitica, 275 strains (95.2%) were positive for pyrazinamidase test, and followed by in order of crystal violet binding test, 226 (79.2% ) ; CRMOX test, 190 (65.7%) ; autoagglutination test, 1.85(64.0%) : calcium dependency test, 86 (29.8%) and congo red uptake test, 47(16.3%). 2. The correlationship between autoagglutination and CRMOX test(r=0.90) was highly significant (p<0.01). 3. In 190 strains(65.7%) bearing the virulence-associated plasmids(MW 40~50 Mdalton), the correlation between the presence of plasmids and their in vitro virulence-associated properties were highest with CRMOX test(r=0.93) and followed by in orders of AAG test(0.81), CV test(0.46), PYZ test(0.37) and CD test(0.18), but no correlationship between the presence of plasmids and CR test(-0.11). 4. The $CRMOX^+$ strains produced the 220 Kdalton OMP when they were cultured at $37^{\circ}C$, but not at $26^{\circ}C$. The presence of 220 Kdalton OMP was correlated significantly with in vitro virulence properties and the presence of virulence-associated plasmid, respectively. 5. In the isogenic $CRMOX^-$ mutant strains, of which plasmid were cured by treatment with acridine orange not only in vitro virulence-associated properties(CR 100%, CD 100%, AAG 82.6%, CV 58.3%) disappeared but also 220 Kdalton OMP(100%) was not produced. These results indicate that the positive CRMOX reaction is plasmid-mediated and the CRMOX test is potential as an in vitro virulence tests with Y enterocolitica.

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Functional Mechanism of Calmodulin for Cellular Responses in Plants (식물의 세포반응에 대한 칼모듈린의 functional 작용기작 연구)

  • Cho, Eun-Kyung;Choi, Young-Ju
    • Journal of Life Science
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    • v.19 no.1
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    • pp.129-137
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    • 2009
  • Calcium ($Ca^{2+}$) plays pivotal roles as an intracellular second messenger in response to a variety of stimuli, including light, abiotic. and biotic stresses and hormones. $Ca^{2+}$ sensor is $Ca^{2+}$-binding protein known to function in transducing signals by activating specific targets and pathways. Among $Ca^{2+}$-binding proteins, calmodulin (CaM) has been well reported to regulate the activity of down-stream target proteins in plants and animals. Especially plants possess multiple CaM genes and many CaM target proteins, including unique protein kinases and transcription factors. Thus, plants are possible to perceive different signals from their surroundings and adapt to the changing environment. However, the function of most of CaM or CaM-related proteins have been remained uncharacterized and unknown. Hence, a better understanding of the function of these proteins will help in deciphering their roles in plant growth, development and response to environmental stimuli. This review focuses on $Ca^{2+}$-CaM messenger system, CaM-associated proteins and their role in responses to external stimuli of both abiotic and biotic stresses in plants.

Protein Kinase (PKC)-ε Interacts with the Serotonin Transporter (SERT) C-Terminal Region (Protein kinase (PKC)-ε와 serotonin transporter (SERT)의 C-말단과의 결합)

  • Moon, Il-Soo;Seog, Dae-Hyun
    • Journal of Life Science
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    • v.20 no.10
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    • pp.1451-1457
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    • 2010
  • Serotonin (5-hydroxytryptamine, 5-HT) is an important mediator of cell-cell signaling in neuronal systems. The serotonin transporter (SERT) on the plasma membrane controls the extracellular 5-HT level by reuptake of released 5-HT from the synaptic cleft, but the underlying regulation mechanism is unclear. Here, we used the yeast two-hybrid system to identify the specific binding protein(s) that interacts with the carboxyl (C)-terminal region of SERT and found a specific interaction with protein kinase C-$\varepsilon$ (PKC-$\varepsilon$), a PKC isotype that is characterized as a calcium-independent and phorbol ester/diacylglycerol-sensitive serine/threonine kinase. PKC-$\varepsilon$ bound to the tail region of SERT but not to other members of the $Na^+/Cl^-$ dependent SLC6 gene family in the yeast two-hybrid assay. The C-terminal region of PKC-$\varepsilon$ is essential for interaction with SERT. In addition, these proteins showed specific interactions in the glutathione S-transferase (GST) pull-down assay. PKC-$\varepsilon$ phosphorylated the peptide of the SERT amino (N)-terminus in vitro. These results suggest that the phosphorylation of SERT by PKC-$\varepsilon$ may regulate SERT activity in plasma membrane.

Stage specific transcriptome profiles at cardiac lineage commitment during cardiomyocyte differentiation from mouse and human pluripotent stem cells

  • Cho, Sung Woo;Kim, Hyoung Kyu;Sung, Ji Hee;Han, Jin
    • BMB Reports
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    • v.54 no.9
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    • pp.464-469
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    • 2021
  • Cardiomyocyte differentiation occurs through complex and finely regulated processes including cardiac lineage commitment and maturation from pluripotent stem cells (PSCs). To gain some insight into the genome-wide characteristics of cardiac lineage commitment, we performed transcriptome analysis on both mouse embryonic stem cells (mESCs) and human induced PSCs (hiPSCs) at specific stages of cardiomyocyte differentiation. Specifically, the gene expression profiles and the protein-protein interaction networks of the mESC-derived platelet-derived growth factor receptor-alpha (PDGFRα)+ cardiac lineage-committed cells (CLCs) and hiPSC-derived kinase insert domain receptor (KDR)+ and PDGFRα+ cardiac progenitor cells (CPCs) at cardiac lineage commitment were compared with those of mesodermal cells and differentiated cardiomyocytes. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes pathway analyses revealed that the genes significantly upregulated at cardiac lineage commitment were associated with responses to organic substances and external stimuli, extracellular and myocardial contractile components, receptor binding, gated channel activity, PI3K-AKT signaling, and cardiac hypertrophy and dilation pathways. Protein-protein interaction network analysis revealed that the expression levels of genes that regulate cardiac maturation, heart contraction, and calcium handling showed a consistent increase during cardiac differentiation; however, the expression levels of genes that regulate cell differentiation and multicellular organism development decreased at the cardiac maturation stage following lineage commitment. Additionally, we identified for the first time the protein-protein interaction network connecting cardiac development, the immune system, and metabolism during cardiac lineage commitment in both mESC-derived PDGFRα+ CLCs and hiPSC-derived KDR+PDGFRα+ CPCs. These findings shed light on the regulation of cardiac lineage commitment and the pathogenesis of cardiometabolic diseases.

Molecular and Functional Characterization of Mouse Cardiac Junctate

  • Hong, Chang-Soo;Cho, Myeong-Chan;Kwak, Yong-Geun;Chae, Soo-Wan;Kim, Do-Han
    • Proceedings of the Korean Biophysical Society Conference
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    • 2002.06b
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    • pp.57-57
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    • 2002
  • Junctate is a newly identified integral endo(sarco)plasmic reticulum membrane calcium binding protein, which is an alternative splicing form of the same gene generating aspartyl-hydroxylase and junctin. Screening a mouse heart cDNA library using canine junctin cDNA as a probe yielded 3 complete mouse heart cDNAs.(omitted)

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cDNA Cloning and Tissue Distribution of Two Parvalbumin Isoforms from the Hermaphrodite fish Rivulus marmoratus(Cyprinodontiformes, Rivulidae)

  • Lee, Jae-Seong;Lee, Young-Mi;Jung, Sang-Oun;Lee, Chang-Joo
    • Journal of Aquaculture
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    • v.18 no.2
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    • pp.81-85
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    • 2005
  • We isolated two parvalbumin cDNAS by expressed sequence tag analysis (1,577 ESTs in total) from the self-fertilizing fish Rivulus marmoratus (Cyprinodontiformes, Rivulidae). Two isoforms of parvalbumin genes showed high similarity to those of carp at 88% and 91% amino acid residues identity, respectively, and showed 79.8% similarity between two parvalbumin isoforms. Of 1,577 ESTs from R. marmroatus sequenced, parvalbumin 1 gene was most abundant. This gene was strongly expressed in the order of muscle, eye, and brain, while it was expressed slightly in other tissues. In this paper, we discussed on the R. marmoratus parvalbumin genes on its sequence and basic characteristics.