カルシウム結合タンパク質

WordNet

executed with proper legal authority; "a binding contract"
the protective covering on the front, back, and spine of a book; "the book had a leather binding" (同)book binding, cover, back
strip sewn over or along an edge for reinforcement or decoration
the capacity to attract and hold something
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
a white metallic element that burns with a brilliant light; the fifth most abundant element in the earths crust; an important component of most plants and animals (同)Ca, atomic number 20

PrepTutorEJDIC

義務的な,拘束力ある / 〈U〉しばること;〈C〉しばる物 / 〈C〉製本,装丁 / 〈U〉縁(‘ふち')取り材料
蛋白(たんばく)質
『カルシウム』(金属元素;化学記号は『Ca』)

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/10/29 21:05:51」(JST)

wiki en

Calcium-binding proteins are proteins that participate in calcium cell signalling pathways by binding to Ca²⁺, the calcium ion that plays an important role in many cellular processes. This calcium ion has unique specific domains that bind to Calcium binding proteins (CBP) and is known to be heterogenous. One of the functions of Calcium binding proteins is to regulate the amount of free (unbound) Ca²⁺ in the cytosol of the cell.^[1] Regulation of Ca(2+) is known as Calcium homeostasis.

Types

Many different calcium-binding proteins exist, with different cellular and tissue distribution and involvement in specific functions. Calcium binding proteins also serve an important physiological role for cells.^[2] The most ubiquitous Ca²⁺-sensing protein, found in all eukaryotic organisms including yeasts, is calmodulin. Intracellular storage and release of Ca²⁺ from the sarcoplasmic reticulum is associated with the high-capacity, low-affinity calcium-binding protein calsequestrin.^[3] Calretinin is another type of Calcium binding protein weighing 29kD. It is involved in cell signaling and shown to exist in neurons. This type of protein is also found in large quantities in malignant mesothelial cells, which can be easily differentiated from carcinomas. This differentiation is later applied for a diagnosis on ovarian stromal tumors.^[4] Also, another member of the EF-hand superfamily is the S100B protein, which regulates p53. P53 is known as a tumor suppressor protein and in this case acts as a transcriptional activator or repressor of numerous genes. S100B proteins are abundantly found in cancerous tumor cells causing them to be overexpressed, therefore making these proteins useful for classifying tumors. In addition, this explains why this protein can easily interact with p53 when transcriptional regulation takes place.^[5]

Ca(2+) binding proteins can be either intracellular and extracellular. Those that are intracellular can contain or lack a structural EF- hand domain. Extra cellular calcium binding proteins are classified into six groups.^[6] Since Ca (2+) is an important second messenger, it can act as an activator or inhibitor in gene transcription. Those that belong to the EF-hand superfamily such as Calmodulin and Calcineurin have been linked to transcription regulation. When levels of Ca(2+) increase in the cell, these members of the EF-hand superfamily regulate transcription indirectly by phosphorylating/dephosphorylating transcription factors.^[5]

Functions

With their role in signal transduction, calcium-binding proteins contribute to all aspects of the cell's functioning, from homeostasis to learning and memory. For example, the neuron-specific calexcitin has been found to have an excitatory effect on neurons, and interacts with proteins that control the firing state of neurons, such as the voltage-dependent potassium channel.^[7]

Compartmentalization of calcium binding proteins such as calretinin and calbindin-28 kDa has been noted within cells, suggesting that these proteins perform distinct functions in localized calcium signaling.^[8] It also indicates that in addition to freely diffusing through the cytoplasm to attain a homogeneous distribution, calcium binding proteins can bind to cellular structures through interactions that are likely important for their functions.^[8]

Calcium-binding protein modulators

Calcium Binding Protein Modulator Agonists

Calcium Binding Protein Modulator Antagonists

Calcium Binding Protein Modulator Inhibitors

Additional Calcium Binding Protein Modulators

References

^ Kinjo, Tashi G; Schnetkamp, Paul PM. Ca2+ Chemistry, Storage and Transport in Biologic Systems: An Overview. Madame Curie Bioscience Database [Internet]. Retrieved 2 May 2016.
^ Yáñez M, Gil-Longo J, Campos-Toimil M (2012). "Calcium binding proteins.". Adv Exp Med Biol. 740: 461–82. doi:10.1007/978-94-007-2888-2_19. PMID 22453954.
^ Siegel, George (Ed.). Basic neurochemistry: molecular, cellular and medical aspects. Lippincott Williams and Wilkins / 1999 ISBN 0-397-51820-X
^ http://www.nordiqc.org/Epitopes/calretinin/calretinin.htm
^ ^a ^b http://nmr.uhnres.utoronto.ca/ikura/publication/PDF%20Articles/2002/The%20role%20of%20calcium%20binding%20proteins.pdf
^ http://download.springer.com/static/pdf/28/chp%253A10.1007%252F978-94-007-2888-2_19.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Fchapter%2F10.1007%2F978-94-007-2888-2_19&token2=exp=1462396956~acl=%2Fstatic%2Fpdf%2F28%2Fchp%25253A10.1007%25252F978-94-007-2888-2_19.pdf%3ForiginUrl%3Dhttp%253A%252F%252Flink.springer.com%252Fchapter%252F10.1007%252F978-94-007-2888-2_19*~hmac=0838af8d5cc7a124739099b49a84211059c2f5d7df52548bd38371e2027ffada
^ Nelson T, Cavallaro S, Yi C, McPhie D, Schreurs B, Gusev P, Favit A, Zohar O, Kim J, Beushausen S, Ascoli G, Olds J, Neve R, Alkon D (1996). "Calexcitin: a signaling protein that binds calcium and GTP, inhibits potassium channels, and enhances membrane excitability". PNAS. 93 (24): 13808–13. doi:10.1073/pnas.93.24.13808. PMC 19433. PMID 8943017.
^ ^a ^b Mojumder DK, Wensel TG, Frishman LJ (Aug 2008). "Subcellular compartmentalization of two calcium binding proteins, calretinin and calbindin-28 kDa, in ganglion and amacrine cells of the rat retina". Molecular Vision. 14: 1600–1613. PMC 2528027. PMID 18769561.

External links

Calcium-Binding Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. Hypertrophic cardiomyopathy: Gene mutations and clinical genetic testing
2. 成人におけるカルシウム結石の危険因子 risk factors for calcium stones in adults
3. 幼児および小児における低カルシウム血症の病因 etiology of hypocalcemia in infants and children
4. 骨格の正常な発達および骨形成ならびに骨吸収の調節 normal skeletal development and regulation of bone formation and resorption
5. 思春期におけるカルシウムの所要量 calcium requirements in adolescents

English Journal

Advances in structure-function relationships of tyrosinase from Agaricus bisporus - Investigation on heat-induced conformational changes.

Ioniţă E1, Aprodu I2, Stănciuc N1, Râpeanu G1, Bahrim G3.Author information 1Dunarea de Jos University of Galati, Faculty of Food Science and Engineering, Domnească Street 111, 800201 Galati, Romania.2Dunarea de Jos University of Galati, Faculty of Food Science and Engineering, Domnească Street 111, 800201 Galati, Romania. Electronic address: iuliana.aprodu@ugal.ro.3Dunarea de Jos University of Galati, Faculty of Food Science and Engineering, Domnească Street 111, 800201 Galati, Romania. Electronic address: http://www.bioaliment.ugal.ro.AbstractA combination of fluorescence spectroscopic measurements, inactivation kinetics and in silico prediction was used in the present study to investigate the heat induced behaviour of tyrosinase from Agaricus bisporus. The phase diagram indicated the existence of at least two distinct species induced by the temperature increase up to 75°C. Regardless of calcium ion presence, the fluorescence intensity results suggest that tyrosinase tends to form aggregates after 10min at 75°C. The quenching experiments using acrylamide and iodide demonstrate a more flexible conformation of tyrosinase at higher temperature. Detailed insights into tyrosinase structure after performing molecular dynamics simulations, suggest important structural rearrangements of the protein with the temperature increase. The copper coordinating His(94) residue was predicted to be involved in salt bridge formation with Glu(98), therefore causing significant alteration of the substrate binding site with increasing temperature. These significant changes in tyrosinase structure at temperatures over 60°C might lead to enzyme inactivation.
Food chemistry.Food Chem.2014 Aug 1;156:129-36. doi: 10.1016/j.foodchem.2014.01.089. Epub 2014 Feb 5.
A combination of fluorescence spectroscopic measurements, inactivation kinetics and in silico prediction was used in the present study to investigate the heat induced behaviour of tyrosinase from Agaricus bisporus. The phase diagram indicated the existence of at least two distinct species induced by
PMID 24629948

l-Type lectin from the kuruma shrimp Marsupenaeus japonicus promotes hemocyte phagocytosis.

Xu S1, Wang L1, Wang XW1, Zhao YR1, Bi WJ1, Zhao XF1, Wang JX2.Author information 1MOE Key Laboratory of Plant Cell Engineering and Germplasm Innovation/Shandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Sciences, Shandong University, Jinan, Shandong 250100, China.2MOE Key Laboratory of Plant Cell Engineering and Germplasm Innovation/Shandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Sciences, Shandong University, Jinan, Shandong 250100, China. Electronic address: jxwang@sdu.edu.cn.Abstractl-Type lectins (LTLs) contain a luminal carbohydrate recognition domain, which exhibits homology to leguminous lectins. These type I membrane proteins are involved in the early secretory pathway of animals, and have functions in glycoprotein sorting, trafficking and targeting. Recent studies suggest that LTLs may be involved in immune responses in vertebrates, but no functional studies have been reported. This study reports an LTL, designated as MjLTL1, from the kuruma shrimp Marsupenaeus japonicus. MjLTL consists of a signal peptide, leguminous lectin domain, and transmembrane region. It was upregulated following challenge of shrimp with Vibrio anguillarum. MjLTL1 could agglutinate several bacteria with the presence of calcium, and bind to several Gram-positive and Gram-negative bacteria through lipopolysaccharide and peptidoglycan binding. MjLTL1 could enhance the clearance of V. anguillarum in vivo. MjLTL1 silencing by RNA interference could impair bacterial clearance ability. Further study suggested that MjLTL1 promoted hemocyte phagocytosis. To analyze the possible mechanism, a disintegrin and metalloprotease-like protein (MjADAM) mediating the proteolytic release of extracellular domains from the membrane-bound precursors was also studied in the shrimp. MjADAM exhibited similar tissue location and expression profiles to MjLTL1. After knockdown of MjADAM, the hemocyte phagocytosis rate also declined significantly. ADAM was reported to have an ectodomain shedding function to LTL and release the ectodomain of the lectin from cell membrane. Therefore, our results suggest that the extracellular domain of MjLTL1 might be released from the cell surface as a soluble protein by MjADAM, and function as an opsonin involved in the antibacterial immune responses in shrimp.
Developmental and comparative immunology.Dev Comp Immunol.2014 Jun;44(2):397-405. doi: 10.1016/j.dci.2014.01.016. Epub 2014 Feb 4.
l-Type lectins (LTLs) contain a luminal carbohydrate recognition domain, which exhibits homology to leguminous lectins. These type I membrane proteins are involved in the early secretory pathway of animals, and have functions in glycoprotein sorting, trafficking and targeting. Recent studies suggest
PMID 24508102

A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria.

Cammarata M1, Parisi MG2, Benenati G2, Vasta GR3, Parrinello N2.Author information 1Department of Biological, Chemical, Pharmaceutical Science and Technology, Marine Immunobiology Laboratory, University of Palermo, Via Archirafi 18, Palermo, Italy. Electronic address: matteo.cammarata@unipa.it.2Department of Biological, Chemical, Pharmaceutical Science and Technology, Marine Immunobiology Laboratory, University of Palermo, Via Archirafi 18, Palermo, Italy.3Department of Microbiology and Immunology, University of Maryland School of Medicine, UMB, IMET, Suite 236, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.AbstractThe discovery of rhamnose-binding lectins (RBLs) in teleost fish eggs led to the identification of a novel lectin family characterized by a unique sequence motif and a structural fold, and initially proposed to modulate fertilization. Further studies of the RBL tissue localization and gene organization were also suggestive of role(s) in innate immunity. Here we describe the purification, and biochemical and functional characterization of a novel RBL (DlRBL) from sea bass (Dicentrarchus labrax) serum. The purified DlRBL had electrophoretic mobilities corresponding to 24kDa and 100kDa under reducing and non-reducing conditions, respectively, suggesting that in plasma the DlRBL is present as a physiological homotetramer. DlRBL subunit transcripts revealed an open reading frame encoding 212 amino acid residues that included two tandemly-arrayed carbohydrate-recognition domains, and an 18-residue signal sequence at the N-terminus. The deduced size of 24.1kDa for the mature protein was in good agreement with the subunit size of the isolated lectin. Binding activity of DlRBL for rabbit erythrocytes could be inhibited in the presence of rhamnose or galactose, did not require calcium, and was optimal at around 20°C and within the pH 6.5-8.0 range. DlRBL agglutinated Gram positive and Gram negative bacteria, and exposure of formalin-killed Escherichia coli to DlRBL enhanced their phagocytosis by D. labrax peritoneal macrophages relative to the unexposed controls. Taken together, the results suggest that plasma DlRBL may play a role in immune recognition of microbial pathogens and facilitate their clearance by phagocytosis.
Developmental and comparative immunology.Dev Comp Immunol.2014 Jun;44(2):332-40. doi: 10.1016/j.dci.2014.01.019. Epub 2014 Jan 28.
The discovery of rhamnose-binding lectins (RBLs) in teleost fish eggs led to the identification of a novel lectin family characterized by a unique sequence motif and a structural fold, and initially proposed to modulate fertilization. Further studies of the RBL tissue localization and gene organizat
PMID 24486534

Japanese Journal

Recombinant gamma T305A fibrinogen indicates severely impaired fibrin polymerization due to the aberrant function of hole 'a' and calcium binding sites

Ikeda Minami,Kobayashi Tamaki,Arai Shinpei,Mukai Saki,Takezawa Yuka,Terasawa Fumiko,Okumura Nobuo
THROMBOSIS RESEARCH 134(2), 518-525, 2014-08
… We then functionally analyzed and compared with that of nearby recombinant γN308K fibrinogen.ResultsDNA sequence analysis revealed a heterozygous γT305A substitution (mature protein residue number). … The γT305A fibrinogen indicated markedly impaired thrombin-catalyzed fibrin polymerization both in the presence or absence of 1 mM calcium ion compared with that of γN308K fibrinogen. …
NAID 120005608309

Allograft inflammatory factor-1の免疫学的機能および役割について

山本相浩,川人豊
日本臨床免疫学会会誌 37(3), 139-145, 2014
Allograft inflammatory factor-1（AIF-1）は，ラットの異所性心移植モデルにおいて冠動脈周囲の浸潤したマクロファージにおいて発現が認められた蛋白である．主にマクロファージによって産生され，IFN-γにより制御される．AIF-1にはさまざまなsplicing valiantsが存在し，その機能も異なることが示されている．Ca結合に関わるEF handの立体構造を有 …
NAID 130004875925

Chemical alteration by tooth bleaching of human salivary proteins that infiltrated subsurface enamel lesions —Experimental study with bovine lesion model systems—

IIZUKA Junko,MUKAI Yoshiharu,TANIGUCHI Motoe,MIKUNI-TAKAGAKI Yuko,TEN CATE Jacob Martien,TERANAKA Toshio
Dental Materials Journal 33(5), 663-668, 2014
… Calcium-binding salivary proteins such as statherin hinder remineralization of these lesions. … SDS-PAGE of dialyzed extracts showed that specific salivary proteins bound to the lesions, while virtually no protein bands were detected if the specimens were bleached. …
NAID 130004696767

Related Pictures

★リンクテーブル★

リンク元	「カルシウム結合タンパク質」「CBP」
拡張検索	「vitamin D-dependent calcium-binding protein」
関連記事	「binding」「binding protein」「calcium」

「カルシウム結合タンパク質」

　　[★]

英: calcium-binding protein

[show details]

カルシウム結合タンパク質 : 約 89,500 件
カルシウム結合タンパク : 約 24,000 件
カルシウム結合蛋白質 : 約 56,800 件
カルシウム結合蛋白 : 約 35,700 件

「CBP」

　　[★]

「vitamin D-dependent calcium-binding protein」

　　[★]

ビタミンD依存性カルシウム結合タンパク質

「binding」

　　[★]

n.

結合、バインディング

adj.

結合性の

関: affinity、associate、bind、bond、bonding、combine、conjoin、conjugate、conjugation、conjunction、connect、connection、connective、connectivity、couple、dock、engage、engagement、join、ligate、linkage、symphysial、symphysic、union

「binding protein」

　　[★]

結合タンパク質、結合タンパク、結合蛋白質、結合蛋白

関: BP、carrier protein、transport protein

「calcium」

　　[★]

カルシウム Ca2+

[1] Kinjo, Tashi G; Schnetkamp, Paul PM. Ca2+ Chemistry, Storage and Transport in Biologic Systems: An Overview. Madame Curie Bioscience Database [Internet]. Retrieved 2 May 2016.

[pmid22453954-2] Yáñez M, Gil-Longo J, Campos-Toimil M (2012). "Calcium binding proteins.". Adv Exp Med Biol. 740: 461–82. doi:10.1007/978-94-007-2888-2_19. PMID 22453954.

[3] Siegel, George (Ed.). Basic neurochemistry: molecular, cellular and medical aspects. Lippincott Williams and Wilkins / 1999 ISBN 0-397-51820-X

[4] ttp://www.nordiqc.org/Epitopes/calretinin/calretinin.htm

[nmr.uhnres.utoronto.ca-5] ttp://nmr.uhnres.utoronto.ca/ikura/publication/PDF%20Articles/2002/The%20role%20of%20calcium%20binding%20proteins.pdf

[6] ttp://download.springer.com/static/pdf/28/chp%253A10.1007%252F978-94-007-2888-2_19.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Fchapter%2F10.1007%2F978-94-007-2888-2_19&token2=exp=1462396956~acl=%2Fstatic%2Fpdf%2F28%2Fchp%25253A10.1007%25252F978-94-007-2888-2_19.pdf%3ForiginUrl%3Dhttp%253A%252F%252Flink.springer.com%252Fchapter%252F10.1007%252F978-94-007-2888-2_19*~hmac=0838af8d5cc7a124739099b49a84211059c2f5d7df52548bd38371e2027ffada

[7] Nelson T, Cavallaro S, Yi C, McPhie D, Schreurs B, Gusev P, Favit A, Zohar O, Kim J, Beushausen S, Ascoli G, Olds J, Neve R, Alkon D (1996). "Calexcitin: a signaling protein that binds calcium and GTP, inhibits potassium channels, and enhances membrane excitability". PNAS. 93 (24): 13808–13. doi:10.1073/pnas.93.24.13808. PMC 19433. PMID 8943017.

[Mojumder2008-8] Mojumder DK, Wensel TG, Frishman LJ (Aug 2008). "Subcellular compartmentalization of two calcium binding proteins, calretinin and calbindin-28 kDa, in ganglion and amacrine cells of the rat retina". Molecular Vision. 14: 1600–1613. PMC 2528027. PMID 18769561.

v t e Proteins: carrier proteins

Fatty acid	FABP1 FABP2 FABP3 FABP4 FABP5 FABP6 FABP7

Hormone	peptide hormone: Follistatin Growth hormone binding protein Insulin-like growth factor binding protein IGFBP1 IGFBP2 IGFBP3 IGFBP4 IGFBP5 IGFBP6 IGFBP7 Neurophysins Neurophysin I II steroid hormone: Sex hormone binding globulin/Androgen binding protein Transcortin Thyroxine-binding globulin Transthyretin

Metal/element	calcium Calcium-binding protein Calmodulin-binding proteins copper Ceruloplasmin iron Iron-binding proteins Transferrin receptor

Vitamin	Retinol binding protein 1 2 3 4 Transcobalamin

Pigment	Plant Light-Harvesting Complex Orange Carotenoid Protein Phycobiliprotein Photosynthetic Reaction Centers Phytochrome Rhodopsin

Other	Acyl carrier protein Adaptor protein Cholesterylester transfer protein F-box protein GTP-binding protein Latent TGF-beta binding protein Major urinary proteins Membrane transport protein Odorant binding protein

匿名

検索

案内

案内

calcium-binding protein