scholarly journals 1004 THE DUAL ROLE OF MANNITOL AS OSMOPROTECTANT AND PHOTOASSIMILATE IN CELERY

HortScience ◽  
1994 ◽  
Vol 29 (5) ◽  
pp. 573d-573
Author(s):  
D.M. Pharr ◽  
J.M.H. Stoop ◽  
M.E. Studer Feusi ◽  
J.D. Williamson ◽  
M.O. Massel ◽  
...  

Mannitol, a six carbon sugar alcohol, is widely distributed in nature and is a major phloem-translocated photoassimilate in celery. II may also function as a compatible osmolyte providing stress tolerance. Until recently, little was known about the route of mannitol catabolism in sink tissues of higher plants. An enzyme. mannitol dehydrogenase. (MDH) that oxidizes mannitol to mannose utilizing NAD as the electron acceptor was discovered (Arch. Biochem. Biophys. 1991. 298:612-619) in “sink” tissues of celery and celeriac plants. The activity of the enzyme is inversely related to tissue mannitol concentration in various parts of celery plants suggesting a role for the enzyme in mannitol catabolism. In osmostressed celery plants, the activity of the enzyme in sink tissues decreases as mannitol accumulates. Celery cells growing heterotrophically in suspension culture utilize either sucrose or mannitol as the sole carbon source and grow equally well on either carbohydrate. Mannitol-grown cells contain more MDI-I activity than sucrose-grown cells, and the activity of the enzyme is correlated with the rate of depletion of mannitol from the culture medium. Cells growing on mannitol contain an internal pool of mannitol but little sugar. Cells growing on sucrose contain internal sugar pools but no mannitol. Mannitol-grown cells are also more salt tolerant than cells grown on sucrose. Our laboratory is involved in studies of the physiological role of the mannitol oxidizing enzyme in regulating mannitol utilization and the role of the enzyme in regulating mannitol pool size during salt and osmostress in both celery plants and celery suspension cultures. Current studies on the molecular control of expression of the enzyme will be discussed.

2012 ◽  
Vol 30 (1) ◽  
pp. 100
Author(s):  
Wei HUANG ◽  
Shi-Bao ZHANG ◽  
Kun-Fang CAO

Amino Acids ◽  
1990 ◽  
pp. 1040-1051
Author(s):  
Fumio Ikegami ◽  
Fernand Lambein ◽  
Leslie Fowden ◽  
Isamu Murakoshi

2011 ◽  
Vol 1 (1) ◽  
pp. 44-50 ◽  
Author(s):  
S. S. Sangaev ◽  
A. V. Kochetov ◽  
S. S. Ibragimova ◽  
B. A. Levenko ◽  
V. K. Shumny

2001 ◽  
Vol 48 (1) ◽  
pp. 145-155 ◽  
Author(s):  
W Jarmuszkiewicz

Uncoupling proteins, members of the mitochondrial carrier family, are present in mitochondrial inner membrane and mediate free fatty acid-activated, purine-nucleotide-inhibited H+ re-uptake. Since 1995, it has been shown that the uncoupling protein is present in many higher plants and some microorganisms like non-photosynthetic amoeboid protozoon, Acanthamoeba castellanii and non-fermentative yeast Candida parapsilosis. In mitochondria of these organisms, uncoupling protein activity is revealed not only by stimulation of state 4 respiration by free fatty acids accompanied by decrease in membrane potential (these effects being partially released by ATP and GTP) but mainly by lowering ADP/O ratio during state 3 respiration. Plant and microorganism uncoupling proteins are able to divert very efficiently energy from oxidative phosphorylation, competing for deltamicroH+ with ATP synthase. Functional connection and physiological role of uncoupling protein and alternative oxidase, two main energy-dissipating systems in plant-type mitochondria, are discussed.


Zygote ◽  
2013 ◽  
Vol 22 (3) ◽  
pp. 395-403 ◽  
Author(s):  
Peng Wang ◽  
Yi Zheng ◽  
Ying Li ◽  
Hua Shang ◽  
Guang-Xuan Li ◽  
...  

SummarySpermatogenesis is a process in adult male mammals supported by spermatogonial stem cells (SSCs). The cultivation of SSCs has potential value, for example for the treatment of male infertility or spermatogonial transplantation. Testicular interstitial fluid was added to culture medium to a final concentration of 5, 10, 20, 30 or 40%, in order to investigate its effects on proliferation of mouse SSCs in vitro, Alkaline phosphatase (AKP) assay, reverse transcription polymerase chain reaction (RT-PCR) analysis and indirect immunofluorescence of cells were performed to identify SSCs, and the proliferation rate and diameters of the SSCs colonies were measured. The results showed that the optimal addition of testicular interstitial fluid to culture medium was 30%. When medium supplemented with 30% testicular interstitial fluid was used to culture mouse SSCs, the optimum proliferation rate and diameter of the cell colonies were 72.53% and 249 μm, respectively, after 8 days in culture, values that were significant higher than those found for other groups (P < 0.05). In conclusion, proliferation of mouse SSCs could be promoted significantly by supplementation of the culture medium with 30% testicular interstitial fluid. More research is needed to evaluate and understand the precise physiological role of testicular interstitial fluid during cultivation of SSCs.


2018 ◽  
Vol 38 (4) ◽  
Author(s):  
Jeanette Flores-Bautista ◽  
José Navarrete-Perea ◽  
Gladis Fragoso ◽  
Ana Flisser ◽  
Xavier Soberón ◽  
...  

During the study of host–parasite relationships in taeniid parasite diseases, including cysticercosis and hydatidosis, reports have described the presence of host proteins in the cyst fluid and tissue of metacestodes. However, the fate or role of host elements inside the parasite remains barely explored. After the publication of genomes of four cestode species, it became clear that these organisms possess a limited biosynthetic capability. The initial goal of the present study was to determine if uptaken host proteins could be a source of essential amino acids for cysticerci. To track the utilization of uptaken proteins, we added metabolically labeled IgG-3H and GFP-3H to the culture medium of Taenia crassiceps cysticerci. Incorporation of labeled amino acid was evaluated by fluorography in cysticerci extracts. Our results showed that the use of uptaken proteins by cysticerci as a source of amino acids appeared negligible. Exploring alternative fates for the host proteins, proteomic analysis of the protein matrix in calcareous corpuscles was carried out. Since T. crassiceps does not contain calcareous corpuscles, proteomic analyses were performed in corpuscles of Taenia solium cysticerci. Our results demonstrated that host proteins represented approximately 70% of protein content in the calcareous corpuscles. The presence of the two major uptaken host proteins, namely albumin and IgG, was also demonstrated by Western blot in the matrix of corpuscles. Our findings strongly suggested that the uptake and disposal of host proteins involve calcareous corpuscles, expanding the physiological role of these mineral concretions to a far more important level than previously proposed.


2004 ◽  
Vol 287 (5) ◽  
pp. G967-G973 ◽  
Author(s):  
Jun Wu ◽  
Fuli Liu ◽  
Åke Nilsson ◽  
Rui-Dong Duan

Sphingomyelin (SM) hydrolysis in the gut has implications in colonic tumorigenesis and cholesterol absorption. It is triggered by intestinal alkaline sphingomyelinase (Alk-SMase) that is present in the intestinal mucosa and content. The mechanism by which the enzyme is released into the lumen is not clear. We studied whether trypsin can dissociate Alk-SMase from the mucosa and affect its activity. During luminal perfusion of rat intestine, addition of trypsin to the buffer increased Alk-SMase activity in the perfusate output by about threefold. Treating COS-7 cells transfected with Alk-SMase cDNA with trypsin increased the SMase activity in the medium and reduced that in the cell lysate dose dependently. The appearance of Alk-SMase in the perfusate and culture medium was confirmed by Western blot analysis. The effect of trypsin was blocked by trypsin inhibitor, and neither chymotrypsin nor elastase had a similar effect. We also expressed the full length and COOH-terminal truncated Alk-SMase in COS-7 cells and found that the activity of the full-length enzyme is mainly in the cells, whereas that of the truncated form is mainly in the medium. Both forms were active, but only the activity of the full-length Alk-SMase was enhanced by trypsin. By linking a poly-His tag to the constructed cDNA, we found that the first tryptic site Arg440 upstream of the signal anchor was attacked by trypsin. In conclusion, trypsin cleaves the Alk-SMase at the COOH terminal, releases it from mucosa, and meanwhile enhances its activity. The findings indicate a physiological role of trypsin in SM digestion.


1982 ◽  
Vol 682 (3) ◽  
pp. 436-445 ◽  
Author(s):  
Christa Critchley ◽  
Ion C. Baianu ◽  
Govindjee ◽  
H.S. Gutowsky

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