scholarly journals Molecular interconversion of cold-sensitive cytosolic 3,3′,5-tri-iodo-l-thyronine-binding proteins from human erythrocytes: effect of cold, heat and pH treatments

1993 ◽  
Vol 290 (2) ◽  
pp. 579-582 ◽  
Author(s):  
A N Fanjul ◽  
R N Farías
Keyword(s):  
Blood Cells ◽  
Low Temperatures ◽  
Binding Proteins ◽  
Cold Treatment ◽  
Rapid Loss ◽  
Polymeric Form ◽  
Human Red Blood Cells ◽  
Similar Association ◽  
Cold Sensitive ◽  
Inactive Monomer

Cytosolic 3,3′,5-tri-iodo-L-thyronine-binding proteins (CTBP I, II and IV species) from human red blood cells undergo rapid loss of activity at low temperatures. Cold treatment of CTBPs was accompanied by dissociation of the polymeric protein to the 60 kDa inactive monomer. Re-activation of the cold-inactivated CTBP IV by warming resulted in association of the monomer to the active polymeric form. A similar association-dissociation phenomenon was also obtained isothermically, though pH changes. We conclude that CTBP I and CTBP II are polymeric forms of CTBP IV.

scholarly journals iTRAQ-based quantitative proteomics analysis of cantaloupe (Cucumis melo var. saccharinus) after cold storage

2020 ◽  
Author(s):  
Wen Song ◽  
Fengxian Tang ◽  
Wenchao Cai ◽  
Qin Zhang ◽  
Fake Zhou ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cold Tolerance ◽  
Low Temperatures ◽  
Proteomic Analysis ◽  
Molecular Mechanisms ◽  
Chilling Injury ◽  
Cold Treatment ◽  
Metabolic Analysis ◽  
Itraq Analysis ◽  
Cold Sensitive

Abstract Background: Cantaloupe is susceptible to cold stress when it is stored at low temperatures, resulting in the loss of edible and commercial quality. To ascertain the molecular mechanisms of low temperatures resistance in cantaloupe, a cold-sensitive cultivar, Golden Empress-308 (GE) and a cold-tolerant cultivar, Jia Shi-310 (JS), were selected in parallel for iTRAQ quantitative proteomic analysis. Results: The two kinds of commercial cultivars were exposed to a temperature of 0.5℃ for 0, 12 and 24 days. We found that the cold-sensitive cultivar (GE) suffered more severe damage as the length of the cold treatment increased. Proteomic analysis of both cultivars indicated that the number of differentially expressed proteins (DEPs) changed remarkably during the chilly treatment. JS expressed cold-responsive proteins more rapidly and mobilized more groups of proteins than GE. Furthermore, metabolic analysis revealed that more amino acids were up-regulated in JS during the early phases of low temperatures stress. The DEPs we found were mainly related to carbohydrate and energy metabolism, structural proteins, reactive oxygen species scavenging, amino acids metabolism and signal transduction. The consequences of phenotype assays, metabolic analysis and q-PCR validation confirm the findings of the iTRAQ analysis. Conclusion: We found that the prompt response and mobilization of proteins in JS allowed it to maintain a higher level of cold tolerance than GE, and that the slower cold responses in GE may be a vital reason for the severe chilling injury commonly found in this cultivar. The candidate proteins we identified will form the basis of future studies and may improve our understanding of the mechanisms of cold tolerance in cantaloupe.

Scanning and Transmission Electron Microscopy of Human Red Blood Cells

1969 ◽  
Vol 27 ◽  
pp. 44-45
Author(s):  
A.J. Tousimis ◽  
T.R. Padden
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Blood Cells ◽  
Room Temperature ◽  
Type Specimen ◽  
New Combination ◽  
Human Red Blood Cells ◽  
Transmission Electron ◽  
Microscope Slides ◽  
Scanning Electron

The size, shape and surface morphology of human erythrocytes (RBC) were examined by scanning electron microscopy (SEM), of the fixed material directly and by transmission electron microscopy (TEM) of surface replicas to compare the relative merits of these two observational procedures for this type specimen.A sample of human blood was fixed in glutaraldehyde and washed in distilled water by centrifugation. The washed RBC's were spread on freshly cleaved mica and on aluminum coated microscope slides and then air dried at room temperature. The SEM specimens were rotary coated with 150Å of 60:40- gold:palladium alloy in a vacuum evaporator using a new combination spinning and tilting device. The TEM specimens were preshadowed with platinum and then rotary coated with carbon in the same device. After stripping the RBC-Pt-C composite film, the RBC's were dissolved in 2.5N HNO3 followed by 0.2N NaOH leaving the preshadowed surface replicas showing positive topography.

scholarly journals Transbilayer distribution and mobility of phosphatidylinositol in human red blood cells.

1990 ◽  
Vol 265 (27) ◽  
pp. 16035-16038 ◽  
Author(s):  
P Bütikofer ◽  
Z W Lin ◽  
D T Chiu ◽  
B Lubin ◽  
F A Kuypers
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Human Red Blood Cells

scholarly journals Rhythmic glucose metabolism regulates the redox circadian clockwork in human red blood cells

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Ratnasekhar Ch ◽  
Guillaume Rey ◽  
Sandipan Ray ◽  
Pawan K. Jha ◽  
Paul C. Driscoll ◽  
...  
Keyword(s):  
Glucose Metabolism ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Mammalian Cells ◽  
Metabolic Flux ◽  
Pentose Phosphate ◽  
Human Red Blood Cells ◽  
Integral Process ◽  
Metabolic Oscillations ◽  
Human Rbcs

AbstractCircadian clocks coordinate mammalian behavior and physiology enabling organisms to anticipate 24-hour cycles. Transcription-translation feedback loops are thought to drive these clocks in most of mammalian cells. However, red blood cells (RBCs), which do not contain a nucleus, and cannot perform transcription or translation, nonetheless exhibit circadian redox rhythms. Here we show human RBCs display circadian regulation of glucose metabolism, which is required to sustain daily redox oscillations. We found daily rhythms of metabolite levels and flux through glycolysis and the pentose phosphate pathway (PPP). We show that inhibition of critical enzymes in either pathway abolished 24-hour rhythms in metabolic flux and redox oscillations, and determined that metabolic oscillations are necessary for redox rhythmicity. Furthermore, metabolic flux rhythms also occur in nucleated cells, and persist when the core transcriptional circadian clockwork is absent in Bmal1 knockouts. Thus, we propose that rhythmic glucose metabolism is an integral process in circadian rhythms.

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