Knowledge base, research front and hot spot analysis of Cu-Zn superoxide dismutase

doi:10.3969/j.issn.2095-4344.2015.42.025

Abstract

Abstract:

BACKGROUND: Studies have found that Cu-Zn superoxide dismutase (SOD1) is associated with familial amyotrophic lateral sclerosis, opening up a new way of studying molecular genetics. So far more than 100 kinds of SOD1 gene mutations have been found.

OBJECTIVE: To analyze the hot spot, research front and knowledge base of amyotrophic lateral sclerosis visually.

METHODS: Totally 4 693 relevant articles published from 2005 to 2014 were retrieved from Web of Science in ISI with “Cu-Zn superoxide dismutase” or “SOD1” as search keywords. With the aid of CiteSpace III software, the visualization mapping of the network in co-cited articles and keywords was drawn to reveal knowledge base, hot spots and research front of SOD1. The parameters include the number of published papers and citations within 10 years, distribution of research countries and institutions, main source journals, research area of highly cited papers, keywords with high-frequency and emerging keywords with high-frequency in recent 5 years.

RESULTS AND CONCLUSION: The number of published papers and citations in a year showed a trend of sustained growth. United State, China and Japan rank the top three in this area, in which Chinese Academy of Sciences has a great influence among the research institutions. The research fields of SOD1 focus on neurosciences and neurology, biochemistry and molecular biology and so on. The high impact factors of journals with a large number of articles reflect the importance and innovation of this research. Ten high-cited articles consist of the knowledge base on SOD1, directing to the finding of different sites of SOD1 mutation and the measurement of protein concentrations and activity of SOD. The hot spots of SOD1 mainly focus on oxidative stress, familial amyotrophic lateral sclerosis caused by SOD1 mutation and different types of transgenic animal models. The research fronts mainly focus on the finding of pathogenesis in amyotrophic lateral sclerosis, such as the aggregation of TDP-43, the interaction between astrocytes and motor neurons, optineurin and the inhibitor of nuclear factor-κB, hexanucleotide repeat expansion in C9ORF72 and autophagy.
中国组织工程研究杂志出版内容重点：组织构建；骨细胞；软骨细胞；细胞培养；成纤维细胞；血管内皮细胞；骨质疏松；组织工程

Key words: Copper, Zinc, Superoxide Dismutase, Amyotrophic Lateral Sclerosis

Zou Yu, Li Yan-jun Yang Shuang, Zhang Qing-wen. Knowledge base, research front and hot spot analysis of Cu-Zn superoxide dismutase[J]. Chinese Journal of Tissue Engineering Research, 2015, 19(42): 6861-6867.

Figures/Tables 8

References

[1] Mccord JM,Fridovich I.Superoxide Dismutase-An Enzymic Function for Erythrocuprein (Hemocuprein). J Biol chem.1969; 244:6049.
[2] Rosen DR, Siddique T,Patterson D, et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis.Nature. 1993;362(6415):59-62.
[3] Persson O.The intellectual base and research fronts of JASIS 1986-1990. Journal of the American society for information science.1994;45(1):31-38.
[4] Gurney ME, Pu H, Chiu AY, et al.Motor-neuron degeneration in mice that express a human Cu,Zn superoxide-dismutase mutation. Science.1994;264(5166):1772-1775.
[5] Bruijn LI, Miller TM, Cleveland DW.Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci.2004;27:723-749.
[6] Cleveland DW, Rothstein JD.From charcot to lou gehrig: deciphering selective motor neuron death in als. Nat Rev Neurosci.2001;2(11):806-819.
[7] Bradford MM.A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248-254.
[8] Wong PC, Pardo CA, Borchelt DR.et al.An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron.1995;14(6):1105-1116.
[9] Bruijn LI, Miller TM, Cleveland DW.Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci, 2004;27:723-749.
[10] Boillée S, Yamanaka K, Lobsiger CS.Onset and progression in inherited ALS determined by motor neurons and microglia. Science.2006;312(5778):1389-1392.
[11] Beaucham C, Fridovich I.Superoxide dismutase:Improved assays and an assay applicable to acrylamide gels. Anal Biochem.1971;44(1):276-287.
[12] Cvorovic J, Tramer F, Granzotto M,et al.Oxidative stress-based cytotoxicity of delphinidin and cyanidin in colon cancer cells. Arch Biochem Biophys. 2010;501(1):151-157.
[13] Shibata N, Nagai R, Miyata S.et al.Nonoxidative protein glycation is implicated in familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutation. Acta Neuropathol, 2000;100(3):275-284.
[14] Durand J, Amendola J, Bories C, et al.Early abnormalities in transgenic mouse models of amyotrophic lateral sclerosis.J Physiol Paris.2006;99(2-3):211-220.
[15] Furukawa Y, Fu R, Deng HX.et al. Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice. Proc Natl Acad Sci U S A.2006;103(18):7148-7153.
[16] Gurney ME.Transgenic-mouse model of amyotrophic lateral sclerosis. N Engl J Med.1994;331(25):1721-1722.
[17] Avossa D, Grandolfo M, Mazzarol F.et al.Early signs of motoneuron vulnerability in a disease model system: Characterization of transverse slice cultures of spinal cord isolated from embryonic ALS mice. Neuroscience. 2006; 138(4):1179-1194.
[18] Kikuchi H, Almer G, Yamashita S.et al.Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model. Proc Natl Acad Sci U S A.2006;103(15):6025-6030.
[19] Sies H. Oxidative stress: Oxidants and antioxidants. Experimental physiology.1997;82(2): 291-295.
[20] Ho YS, Magnenat JL, Gargano M, Cao J.The nature of antioxidant defense mechanisms: a lesson from transgenic studies. Environ Health Perspect.1998;106 (Suppl 5):1219-1228.
[21] Neumann M, Sampathu DM, Kwong LK,et al.Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.Science. 2006;314(5796):130-133.
[22] Higashi S, Tsuchiya Y, Araki T,et al.TDP-43 physically interacts with amyotrophic lateral sclerosis-linked mutant CuZn superoxide dismutase. Neurochem Int.2010;57(8):906-913.
[23] Van Den Bosch L, Robberecht W.Crosstalk between astrocytes and motor neurons: what is the message? Exp Neurol. 2008; 211(1):1-6.
[24] Maruyama H, Morino H, Ito H.et al.Mutations of optineurin in amyotrophic lateral sclerosis. Nature.2010;465(7295):223-226.
[25] DeJesus-Hernandez M,Mackenzie IR,Boeve BF,et al.Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALS. Neuron.2011;72(2):245-256.
[26] Renton AE, Majounie E, Waite A,et al.A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD. Neuron.2011;72(2):257-268.
[27] Kabuta T, Suzuki Y, Wada K. Degradation of amyotrophic lateral sclerosis-linked mutant Cu, Znsuperoxide dismutase proteins by macroautophagy and the proteasome. J Biol Chem.2006;281:30524-30533.
[28] Ohi T, Nabeshima K, Kato S.et al.Familial amyotrophic lateral sclerosis with His46Arg mutation in Cu/Zn superoxide dismutase presenting characteristic clinical features and Lewy body-like hyaline inclusions. J Neurol Sci.2004;225(1-2):19-25.
[29] Ivanova MI,Sievers SA, Guenther EL.et al. Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS. Proc Natl Acad Sci USA, 2014; 111(1):197-201.