関: apohemoglobin、beta-globin、gamma-globin

WordNet

a colorless protein obtained by removing heme from hemoglobin; the oxygen carrying compound in red blood cells (同)hematohiston, haematohiston

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(液体の)小滴,しずく / (粘土・クリームなどの)球形の固まり

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/06/18 19:50:37」(JST)

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The globins are a family of globular proteins, which are thought to share a common ancestor. These proteins all incorporate the globin fold, a series of eight alpha helical segments. Two prominent members of this family include myoglobin and hemoglobin, which both bind the heme (also haem) prosthetic group. Both of these proteins are reversible oxygen binders.

Globins are haem-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family that is widely distributed in many organisms.^[2]

Types

Globins evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric globins, flavohaemoglobins and globin-coupled sensors. Bacteria have all three types of globins, while archaea lack flavohaemoglobins, and eukaryotes lack globin-coupled sensors.^[3] Several functionally different haemoglobins can coexist in the same species.

Eight globins are known to occur in vertebrates: androglobin, cytoglobin, globin E, globin X, globin Y, haemoglobin, myoglobin and neuroglobin.

Subfamilies

Leghaemoglobin IPR001032
Myoglobin IPR002335
Erythrocruorin IPR002336
Haemoglobin, beta IPR002337
Haemoglobin, alpha IPR002338
Myoglobin, trematode type IPR011406
Globin, nematode IPR012085
Globin, lamprey/hagfish type IPR013314
Globin, annelid-type IPR013316
Haemoglobin, extracellular IPR014610

Examples

Human genes encoding globin proteins include:

CYGB
HBA1, HBA2, HBB, HBD, HBE1, HBG1, HBG2, HBM, HBQ1, HBZ, MB

The globins include:

Haemoglobin (Hb)

Myoglobin (Mb)

Neuroglobin: a myoglobin-like haemprotein expressed in vertebrate brain and retina, where it is involved in neuroprotection from damage due to hypoxia or ischemia.^[4] Neuroglobin belongs to a branch of the globin family that diverged early in evolution.

Cytoglobin: an oxygen sensor expressed in multiple tissues. Related to neuroglobin.^[5]

Erythrocruorin: highly cooperative extracellular respiratory proteins found in annelids and arthropods that are assembled from as many as 180 subunit into hexagonal bilayers.^[6]

Leghaemoglobin (legHb or symbiotic Hb): occurs in the root nodules of leguminous plants, where it facilitates the diffusion of oxygen to symbiotic bacteriods in order to promote nitrogen fixation.

Non-symbiotic haemoglobin (NsHb): occurs in non-leguminous plants, and can be over-expressed in stressed plants .

Flavohaemoglobins (FHb): chimeric, with an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD/FAD-binding domain. FHb provides protection against nitric oxide via its C-terminal domain, which transfers electrons to haem in the globin.^[7]

Globin E: a globin responsible for storing and delivering oxygen to the retina in birds^[8]

Globin-coupled sensors: chimeric, with an N-terminal myoglobin-like domain and a C-terminal domain that resembles the cytoplasmic signalling domain of bacterial chemoreceptors. They bind oxygen, and act to initiate an aerotactic response or regulate gene expression.^[9]^[10]

Protoglobin: a single domain globin found in archaea that is related to the N-terminal domain of globin-coupled sensors.^[11]

Truncated 2/2 globin: lack the first helix, giving them a 2-over-2 instead of the canonical 3-over-3 alpha-helical sandwich fold. Can be divided into three main groups (I, II and II) based on structural features.

HbN (or GlbN): a truncated haemoglobin-like protein that binds oxygen cooperatively with a very high affinity and a slow dissociation rate, which may exclude it from oxygen transport. It appears to be involved in bacterial nitric oxide detoxification and in nitrosative stress.^[12]

Cyanoglobin (or GlbN): a truncated haemoprotein found in cyanobacteria that has high oxygen affinity, and which appears to serve as part of a terminal oxidase, rather than as a respiratory pigment.^[13]

HbO (or GlbO): a truncated haemoglobin-like protein with a lower oxygen affinity than HbN. HbO associates with the bacterial cell membrane, where it significantly increases oxygen uptake over membranes lacking this protein. HbO appears to interact with a terminal oxidase, and could participate in an oxygen/electron-transfer process that facilitates oxygen transfer during aerobic metabolism.^[14]

Glb3: a nuclear-encoded truncated haemoglobin from plants that appears more closely related to HbO than HbN. Glb3 from Arabidopsis thaliana (Mouse-ear cress) exhibits an unusual concentration-independent binding of oxygen and carbon dioxide.^[15]

References

^ Kavanaugh JS, Rogers PH, Case DA, Arnone A (April 1992). "High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp----Arg: a mutation that creates an intersubunit chloride-binding site". Biochemistry 31 (16): 4111–21. doi:10.1021/bi00131a030. PMID 1567857.
^ Vinogradov SN, Hoogewijs D, Bailly X, Mizuguchi K, Dewilde S, Moens L, Vanfleteren JR (August 2007). "A model of globin evolution". Gene 398 (1-2): 132â42. doi:10.1016/j.gene.2007.02.041. PMID 17540514.
^ Vinogradov SN, Hoogewijs D, Bailly X, Arredondo-Peter R, Gough J, Dewilde S, Moens L, Vanfleteren JR (2006). "A phylogenomic profile of globins". BMC Evol. Biol. 6: 31. doi:10.1186/1471-2148-6-31. PMC 1457004. PMID 16600051.
^ Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M (September 2003). "Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity". Structure 11 (9): 1087â95. doi:10.1016/S0969-2126(03)00166-7. PMID 12962627.
^ Fago A, Hundahl C, Malte H, Weber RE (2004). "Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins". IUBMB Life 56 (11-12): 689â96. doi:10.1080/15216540500037299. PMID 15804833.
^ Royer WE, Omartian MN, Knapp JE (January 2007). "Low resolution crystal structure of Arenicola erythrocruorin: influence of coiled coils on the architecture of a megadalton respiratory protein". J. Mol. Biol. 365 (1): 226â36. doi:10.1016/j.jmb.2006.10.016. PMC 1847385. PMID 17084861.
^ Mukai M, Mills CE, Poole RK, Yeh SR (March 2001). "Flavohemoglobin, a globin with a peroxidase-like catalytic site". J. Biol. Chem. 276 (10): 7272â7. doi:10.1074/jbc.M009280200. PMID 11092893.
^ Blank M, Kiger L, Thielebein A, Gerlach F, Hankeln T, Marden MC, Burmeister T (2011). "Oxygen supply from the bird's eye perspective: Globin E is a respiratory protein in the chicken retina". J. Biol. Chem. 286 (30): 26507–15. doi:10.1074/jbc.M111.224634. PMC 3143615. PMID 21622558.
^ Hou S, Freitas T, Larsen RW, Piatibratov M, Sivozhelezov V, Yamamoto A, Meleshkevitch EA, Zimmer M, Ordal GW, Alam M (July 2001). "Globin-coupled sensors: a class of heme-containing sensors in Archaea and Bacteria". Proc. Natl. Acad. Sci. U.S.A. 98 (16): 9353â8. doi:10.1073/pnas.161185598. PMC 55424. PMID 11481493.
^ Freitas TA, Saito JA, Hou S, Alam M (January 2005). "Globin-coupled sensors, protoglobins, and the last universal common ancestor". J. Inorg. Biochem. 99 (1): 23â33. doi:10.1016/j.jinorgbio.2004.10.024. PMID 15598488.
^ Freitas TA, Hou S, Dioum EM, Saito JA, Newhouse J, Gonzalez G, Gilles-Gonzalez MA, Alam M (April 2004). "Ancestral hemoglobins in Archaea". Proc. Natl. Acad. Sci. U.S.A. 101 (17): 6675â80. doi:10.1073/pnas.0308657101. PMC 404104. PMID 15096613.
^ Lama A, Pawaria S, Dikshit KL (July 2006). "Oxygen binding and NO scavenging properties of truncated hemoglobin, HbN, of Mycobacterium smegmatis". FEBS Lett. 580 (17): 4031â41. doi:10.1016/j.febslet.2006.06.037. PMID 16814781.
^ Yeh DC, Thorsteinsson MV, Bevan DR, Potts M, La Mar GN (February 2000). "Solution 1H NMR study of the heme cavity and folding topology of the abbreviated chain 118-residue globin from the cyanobacterium Nostoc commune". Biochemistry 39 (6): 1389â99. doi:10.1021/bi992081l. PMID 10684619.
^ Pathania R, Navani NK, Rajamohan G, Dikshit KL (May 2002). "Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli". J. Biol. Chem. 277 (18): 15293â302. doi:10.1074/jbc.M111478200. PMID 11796724.
^ Watts RA, Hunt PW, Hvitved AN, Hargrove MS, Peacock WJ, Dennis ES (August 2001). "A hemoglobin from plants homologous to truncated hemoglobins of microorganisms". Proc. Natl. Acad. Sci. U.S.A. 98 (18): 10119â24. doi:10.1073/pnas.191349198. PMC 56925. PMID 11526234.

This article incorporates text from the public domain Pfam and InterPro IPR001486

UpToDate Contents

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1. サラセミア症候群の分子病理 molecular pathology of the thalassemic syndromes
2. 異常ヘモグロビン症の検査室診断 laboratory diagnosis of the hemoglobinopathies
3. αサラセミアの病態生理 pathophysiology of alpha thalassemia
4. 正常ヒトヘモグロビンの構造および機能 structure and function of normal human hemoglobins
5. βサラセミアの病態生理 pathophysiology of beta thalassemia

English Journal

Effect of hypoxia on lung gene expression and proteomic profile: Insights into the pulmonary surfactant response.

Olmeda B1, Umstead TM2, Silveyra P2, Pascual A3, López-Barneo J3, Phelps DS2, Floros J2, Pérez-Gil J4.Author information 1Dept. Bioquímica, Fac. Biología, Universidad Complutense, Madrid, Spain.2Center for Host Defense, Inflammation, and Lung Disease (CHILD), Department of Pediatrics, The Pennsylvania State University College of Medicine, Hershey, PA, USA.3Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, Sevilla, Spain.4Dept. Bioquímica, Fac. Biología, Universidad Complutense, Madrid, Spain. Electronic address: jperezgil@bio.ucm.es.AbstractExposure of lung to hypoxia has been previously reported to be associated with significant alterations in the protein content of bronchoalveolar lavage (BAL) and lung tissue. In the present work we have used a proteomic approach to describe the changes in protein complement induced by moderate long-term hypoxia (rats exposed to 10% O2 for 72h) in BAL and lung tissue, with a special focus on the proteins associated with pulmonary surfactant, which could indicate adaptation of this system to limited oxygen availability. The analysis of the general proteomic profile indicates a hypoxia-induced increase in proteins associated with inflammation both in lavage and lung tissue. Analysis at mRNA and protein levels revealed no significant changes induced by hypoxia on the content in surfactant proteins or their apparent oligomeric state. In contrast, we detected a hypoxia-induced significant increase in the expression and accumulation of hemoglobin in lung tissue, at both mRNA and protein levels, as well as an accumulation of hemoglobin both in BAL and associated with surface-active membranes of the pulmonary surfactant complex. Evaluation of pulmonary surfactant surface activity from hypoxic rats showed no alterations in its spreading ability, ruling out inhibition by increased levels of serum or inflammatory proteins.
Journal of proteomics.J Proteomics.2014 Apr 14;101:179-91. doi: 10.1016/j.jprot.2014.02.019. Epub 2014 Feb 24.
Exposure of lung to hypoxia has been previously reported to be associated with significant alterations in the protein content of bronchoalveolar lavage (BAL) and lung tissue. In the present work we have used a proteomic approach to describe the changes in protein complement induced by moderate long-
PMID 24576641

Multiple physical stresses induce γ-globin gene expression and fetal hemoglobin production in erythroid cells.

Schaeffer EK1, West RJ1, Conine SJ1, Lowrey CH2.Author information 1Department of Medicine, Geisel School of Medicine, Dartmouth College, Hanover, NH 03755, USA; Department of Pharmacology and Toxicology, Geisel School of Medicine, Dartmouth College, Hanover, NH 03755, USA; Program in Experimental and Molecular Medicine, Geisel School of Medicine, Dartmouth College, Hanover, NH 03755, USA; Norris Cotton Cancer Center, Dartmouth-Hitchcock Medical Center, Lebanon, NH 03756, USA.2Department of Medicine, Geisel School of Medicine, Dartmouth College, Hanover, NH 03755, USA; Department of Pharmacology and Toxicology, Geisel School of Medicine, Dartmouth College, Hanover, NH 03755, USA; Program in Experimental and Molecular Medicine, Geisel School of Medicine, Dartmouth College, Hanover, NH 03755, USA; Norris Cotton Cancer Center, Dartmouth-Hitchcock Medical Center, Lebanon, NH 03756, USA. Electronic address: Christopher.H.Lowrey@dartmouth.edu.AbstractIncreased fetal hemoglobin (HbF) expression is beneficial for β-hemoglobinopathy patients; however, current inducing agents do not possess the ideal combination of efficacy, safety and ease of use. Better understanding the mechanisms involved in γ-globin gene induction is critical for designing improved therapies, as no complete mechanism for any inducing agent has been identified. Given the cytotoxic nature of most known inducing drugs, we hypothesized that γ-globin is a cell stress response gene, and that induction occurs via activation of cell stress signaling pathways. We tested this hypothesis by investigating the ability of physical stresses including heat-shock (HS), UV- and X-irradiation and osmotic shock to increase γ-globin gene expression in erythroid cells. Experiments in K562 and KU812 cells showed that each of these stresses increased steady-state γ-globin mRNA levels, but only after 3-5days of treatments. HS and UV also increased γ-globin mRNA and HbF levels in differentiating primary human erythroid cells. Mechanistic studies showed that HS affects γ-globin mRNA at multiple levels, including nascent transcription and transcript stability, and that induction is dependent on neither the master regulator of the canonical HS response, HSF1, nor p38 MAPK. Inhibitor panel testing identified PI3K inhibitor LY294002 as a novel inducing agent and revealed potential roles for NFκB and VEGFR/PDGFR/Raf kinases in HS-mediated γ-globin gene induction. These findings suggest that cell stress signaling pathways play an important role in γ-globin gene induction and may provide novel targets for the pharmacologic induction of fetal hemoglobin.
Blood cells, molecules & diseases.Blood Cells Mol Dis.2014 Apr;52(4):214-24. doi: 10.1016/j.bcmd.2013.10.007. Epub 2013 Dec 5.
Increased fetal hemoglobin (HbF) expression is beneficial for β-hemoglobinopathy patients; however, current inducing agents do not possess the ideal combination of efficacy, safety and ease of use. Better understanding the mechanisms involved in γ-globin gene induction is critical for designing im
PMID 24314748

The diagnosis and molecular analysis of a novel 21.9kb deletion (Qinzhou type deletion) causing α(+) thalassemia.

Long J1, Yan S2, Lao K2, Pang W2, Ye X2, Sun L2.Author information 1Laboratory of Medical Genetics, Qinzhou Maternal and Child Health Care Hospital, Guangxi 535099, PR China. Electronic address: lab@longju.net.2Laboratory of Medical Genetics, Qinzhou Maternal and Child Health Care Hospital, Guangxi 535099, PR China.Abstractα-Thalassemia is a common single-gene genetic disease that can cause Hb Bart's hydrops fetalis and Hb H disease in tropical and subtropical regions. When examining conventional thalassemia genes, an only detected --(SEA) genotype sample needs further analysis. In doing so, we found a novel 21.9kb deletion (Qinzhou type deletion). The deletion position of the novel 21.9kb deletion is from 14373bp to 36299bp of the α-globin gene cluster (NG_000006.1); thus, there exists a 21927bp sequence deletion, into which a 29bp sequence is added. After sequence analysis, a group of Gap-PCR primers were synthesized to diagnose this novel thalassemia genotype. Through pedigree analysis, we deduced that the propositus obtained the novel alleles from her mother. The genotype of this propositus is --(SEA)/-α(21.9) and its phenotype conforms to the characteristics of Hb H disease, establishing that the combination between -α(21.9) genotype and α(0) genotype can lead to Hb H disease. By molecular analysis, we established that this case fits the characteristic of an α(+) thalassemia genotype.
Blood cells, molecules & diseases.Blood Cells Mol Dis.2014 Apr;52(4):225-9. doi: 10.1016/j.bcmd.2013.10.005. Epub 2013 Nov 10.
α-Thalassemia is a common single-gene genetic disease that can cause Hb Bart's hydrops fetalis and Hb H disease in tropical and subtropical regions. When examining conventional thalassemia genes, an only detected --(SEA) genotype sample needs further analysis. In doing so, we found a novel 21.9kb d
PMID 24225490

Japanese Journal

A high concentration of triiodothyronine attenuates the stimulatory effect on hemin-induced erythroid differentiation of human erythroleukemia K562 cells

, , , , , ,
Endocrine Journal 62(5), 431-440, 2015
… Lower concentrations of T3 had a stimulatory effect on hemin-induced hemoglobin production (1 and 10 nM), CD71 expression (0.1 nM), and α-globin mRNA expression (1 nM), while a higher concentration of T3 (100 nM) abrogated the stimulatory effect on these parameters. …
NAID 130005071801

Possible production of arsenic hemoglobin adducts via exposure to arsine

, , [他], , , , ,
Journal of Occupational Health 57(2), 161-168, 2015
… Results: In the exposed samples, the arsenic concentration in the fraction containing immunocomplexes was higher when immunoprecipitation was conducted with an anti-globin antibody. … Conclusions: Globin forms an adduct with arsenic after both in vitro and in vivo exposure to arsine. …
NAID 130005066086

HbA1cが偽性高値を示したために経口血糖降下薬の投与を受けた非糖尿病異常ヘモグロビンの2例

清水彩洋子,平良暁子,畑﨑聖弘,馬屋原豊,平良真人,古賀正史
糖尿病 58(2), 121-127, 2015
HbA1cは血糖コントロール指標として広く用いられているが，貧血や異常ヘモグロビンを有する患者のHbA1cは血糖コントロールを正しく反映しない．今回，HbA1cが偽性高値を示したために，経口血糖降下薬の投与を受けた非糖尿病異常ヘモグロビンの2例を経験した．2例とも高血糖は認めなかったが，免疫法で測定したHbA1cが高値を示した．1例はスルホニルウレア薬の投与で低血糖をきたしたが，他の1例はDPP4 …
NAID 130004905477

Related Pictures

★リンクテーブル★

リンク元	「グロビン」「apohemoglobin」「beta-globin」「gamma-globin」
拡張検索	「SLS hemoglobin」「hemoglobin/oxygen binding」「hemoglobin Alc」「myoglobin salting out method」

「グロビン」

Bac_globin
	crystal structure of "truncated" hemoglobin n (hbn) from mycobacterium tuberculosis, soaked with xe atoms
Identifiers
Symbol	Bac_globin
Pfam	PF01152
Pfam clan	CL0090
InterPro	IPR001486
PROSITE	PDOC00933
SCOP	1dlw
SUPERFAMILY	1dlw
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Globin family
	Structure of deoxyhemoglobin Rothschild 37 beta Trp----Arg: a mutation that creates an intersubunit chloride-binding site.
Identifiers
Symbol	Goblin
Pfam	PF00042
Pfam clan	CL0090
InterPro	IPR000971
PROSITE	PS01033
SCOP	1hba
SUPERFAMILY	1hba
CDD	cd01067
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary