Differences in tissue concentrations of hydrogen peroxide in the roots and cotyledons of annual and perennial species of flax (Linum)

Botany ◽  
2012 ◽  
Vol 90 (10) ◽  
pp. 1015-1027 ◽  
Author(s):  
Jason C.L. Brown ◽  
Katie E. Marshall ◽  
James F. Staples

Short-lived annuals should allocate more resources towards reproduction, whereas long-lived perennials should allocate more resources towards tissue maintenance. Although ecological data support this hypothesis, no studies have examined the physiological basis for lifespan differences between annuals and perennials. Based on the oxidative theory of aging, hydrogen peroxide (H2O2) levels should be lower in perennating tissues (e.g., basal roots) — but not nonperennating tissues (e.g., cotyledons) — from perennials compared with annuals. We tested this prediction using two annual and two perennial species of flax ( Linum ). As predicted, H2O2 concentrations were lower in roots from perennials than from annuals, reflecting higher catalase activity in roots from perennials. In cotyledons, contrary to our predictions, H2O2 concentrations were actually higher in perennials than in annuals, despite higher catalase activity in perennials as well, likely reflecting higher H2O2 production via peroxisomes and chloroplasts. Therefore, we propose that, consistent with the oxidative theory of aging, perennial flax species have a lower oxidative burden in their roots, but this comes at the cost of a greater oxidative burden in their shoots. As we demonstrate, perenniality is ancestral in Linum, and so derivation of the annual condition likely involved a physiological shift towards a more equitable oxidative burden between roots and shoots.

2012 ◽  
Vol 56 (1) ◽  
pp. 48-55 ◽  
Author(s):  
Keisuke Nakamura ◽  
Taro Kanno ◽  
Takayuki Mokudai ◽  
Atsuo Iwasawa ◽  
Yoshimi Niwano ◽  
...  

2016 ◽  
Vol 8 (36) ◽  
pp. 6625-6630 ◽  
Author(s):  
Lili Zhao ◽  
Julia Wiebe ◽  
Rabia Zahoor ◽  
Sladjana Slavkovic ◽  
Brian Malile ◽  
...  

The sensitivity of the formation of plasmonic silver nanoprisms to hydrogen peroxide is explored for the colorimetric detection of catalase activity in bacteria.


In haemolysates of non-nucleated erythrocytes there is an inverse proportion between catalase activity and rate of choleglobin formation on addition of ascorbic acid. In the intact erythrocytes catalase protects haemoglobin against oxidation and further destruction by the hydrogen peroxide generated by the D-amino-acid oxidase system or by physiological concentrations of ascorbic acid and glutathione. Acid destromatization of haemolyzed horse erythrocytes causes a small decrease in the catalase activity and an increased rate of inactivation of the remaining catalase by ascorbic acid. The liberation of copper from haemocuprein is quantitatively insufficient to explain the decreased stability of the catalase. Exposing duck oxyhaemoglobin, but not reduced haemoglobin, to a pH of 5⋅5 to 5⋅8, causes an alteration which is apparent from the increase of the rate of choleglobin formation. The mechanism of this alteration is discussed. It partly explains the 'stroma effect', at least in duck erythrocytes. In addition, in the latter, there is a true stroma effect. Choleglobin formation in the presence of ascorbic acid is accelerated by a variety of substances. Some of these perturb haemoglobin, while others increase the formation of hydrogen peroxide from ascorbic acid. The implications of our findings on the mechanism of choleglobin formation and on the role of catalase in the erythrocyte are discussed.


2016 ◽  
Vol 61 (3) ◽  
Author(s):  
Crystal L. Jones ◽  
Shweta S. Singh ◽  
Yonas Alamneh ◽  
Leila G. Casella ◽  
Robert K. Ernst ◽  
...  

ABSTRACT The loss of fitness in colistin-resistant (CR) Acinetobacter baumannii was investigated using longitudinal isolates from the same patient. Early CR isolates were outcompeted by late CR isolates for growth in broth and survival in the lungs of mice. Fitness loss was associated with an increased susceptibility to oxidative stress since early CR strains had reduced in vitro survival in the presence of hydrogen peroxide and decreased catalase activity compared to that of late CR and colistin-susceptible (CS) strains.


Blood ◽  
2007 ◽  
Vol 110 (11) ◽  
pp. 5139-5139
Author(s):  
Michael W. Epperly ◽  
J. Andres Melendez ◽  
Xichen Zhang ◽  
Darcy Franicola ◽  
Tracy Smith ◽  
...  

Abstract Mitochondrial localization of the radioprotective MnSOD transgene in hematopoietic cells dismutates irradiation induced superoxide to hydrogen peroxide which is converted to water and oxygen by catalase or glutathione peroxide. Increased concentration of hydrogen peroxide can be toxic. We hypothesized, that increased mitochondrial localized catalase to remove hydrogen peroxide would further increase radioresistance. The human catalase transgene was cloned into a pSVZeo plasmid. To localize the transgene product catalase to the mitochondria, the mitochondrial localization sequence of MnSOD was cloned and attached to the catalase transgene (mt-catalase), then cloned into a pSVZeo plasmid. The plasmids were electroporated into murine hematopoietic cell line 32Dcl3 and 32Dcl3 MnSOD transgene overexpressing clonal cell line 2C6 and subclones of each expressing the non-targeted catalase or mt-catalase selected by growing the cells in zeomycin. The clonal cell lines were shown to express either catalase or mt-catalase by RT-PCR using specific primers. Catalase biochemical activity was determined and 32D-cat and 32D-mt-cat cells had increased catalase activity (595.7 ± 15.3 or 603.3 ± 3.0 μM, respectively) compared to 539.7 ± 3.7 μM (p = 0.0288 or 0.0002, respectively) for 32Dcl3. Compared to the 32Dcl3 cells, 2C6 cells had decreased catalase activity of 205.0 ± 10.0 compared to 539.7 ± 3.7 (p < 0.0001). Catalase activity was increased in 2C6-cat and 2C6-mt-cat (333.3 ± 12.7 and 467.0 ± 1.0, respectively) compared to 205.0 ± 1.0 for 2C6 (p <0.001). Western analysis confirmed the differences in catalase activity. Cells from 32Dcl3, 32D-cat, 32D-mt-catalase, and subclones of 2C6 cells were irradiated to doses ranging from 0 to 8 Gy, plated in methylcellulose, incubated at 37° C for seven days, and colonies of greater that 50 cells counted. The data was analyzed by linear quadratic and single-hit, multi-target models. The 32D-mt-cat cells were more radioresistant than 32D-cat cells by an increased shoulder on the survival curve (n = 10.3 ± 0.5 or 5.9 ± 0.2, respectively, p = 0.0025). Both 32D-mt-cat and 32D-cat were more resistant compared to 32Dcl3 cells (n = 2.9 ± 1.1, p = 0.0196 or 0.0479). Cells from the 2C6 transfected with mt-catalase, but not catalase, showed increased radioresistance increasing the Do from 0.979 ± 0.1Gy for 2C6 to 1.171 ± 0.1 Gy for 2C6-mCat cells. To determine if increased catalase activity altered antioxidant status, levels of glutathione (GSH) and glutathione peroxidase (GPX) were measured. There was no significant change in GSH between cell lines. However, there were increased levels of GPX in 32D-cat and 32D-mt-cat of 260.4 ± 24.6 or 257.1 ± 17.1 μM, respectively, compared to 105.5 ± 1.6 μM (p = 0.0005 or 0.0134, respectively). Cells from 2C6, 2C6-cat or 2C6-mt-cat had decreased GPX activity to 46.7 ± 1.3, 39.1 ± 0.9 or 44.1 ± 1.5μM, respectively, compared to 105.5 ± 1.6μM for 32Dcl3 (p<0.0001). Thus, overexpression of both MnSOD and mt-catalase transgene provides superior radioprotection compared to one alone.


2001 ◽  
Vol 47 (3) ◽  
pp. 222-228 ◽  
Author(s):  
Anne J Anderson ◽  
Charles D Miller

Peracetic acid is used as a sterilant in several industrial settings. Cells of a plant-colonizing bacterium, Pseudomonas putida in liquid suspension, were more sensitive to killing by peracetic acid when they lacked a major catalase activity, catalase A. Low doses of peracetic acid induced promoter activity of the gene encoding catalase A and increased total catalase specific activity in cell extracts. Microbes present in native agricultural soils rapidly degraded the active oxygen species present in peracetic acid. The simultaneous release of oxygen was consistent with a role for catalase in degrading the hydrogen peroxide that is part of the peracetic acid-equilibrium mixture. Amendment of sterilized soils with wild-type P. putida restored the rate of degradation of peracetic acid to a higher level than was observed in the soils amended with the catalase A-deficient mutant. The association of the bacteria with the plant roots resulted in protection of the wild-type as well as the catalase-deficient mutant from killing by peracetic acid. No differential recovery of the wild-type and catalase A mutant of P. putida was observed from roots after the growth matrix containing the plants was flushed with peracetic acid.Key words: Pseudomonas putida (Pp), activated oxygen species (AOS), hydrogen peroxide, luciferase, colonization.


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