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The nuclear transport of the internalised naER is influenced by a 58 kDa protein, p58, that appears to recognize the nuclear localization signals on the naER. At the nuclear pore complex the naER-p58 complex binds to a 62 kDa protein, p62; p58 recognizes p62 in this interaction. It is further observed that p62 gets 'docked' at a 66 kDa nuclear pore complex protein, npcp66. The nuclear entry of naER is an ATP-dependent process. An ATP-dependent biphasic nuclear entry of naER, has been observed. It is possible that the docking of p58-naER complex at the nuclear pore complex and the eventual nuclear entry of naER following its dissociation from the p58 are influenced by two different ranges in the concentration of ATP. In this process, it appears that, the nuclear entry requires an additional quantum of energy, provided by the hydrolysed ATP, in contrast to the energy requirement associated with, the nuclear 'docking' event. 相似文献
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Stephanie Zobrist Marcelo Brito Eduardo Garbin Wuelton M. Monteiro Suellen Clementino Freitas Marcela Macedo Aline Soares Moura Nicole Advani Maria Kahn Sampa Pal Emily Gerth-Guyette Pooja Bansil Gonzalo J. Domingo Dhelio Pereira Marcus VG Lacerda 《PLoS neglected tropical diseases》2021,15(8)
BackgroundGlucose-6-phosphate dehydrogenase (G6PD) deficiency is a common enzyme deficiency, prevalent in many malaria-endemic countries. G6PD-deficient individuals are susceptible to hemolysis during oxidative stress, which can occur from exposure to certain medications, including 8-aminoquinolines used to treat Plasmodium vivax malaria. Accordingly, access to point-of-care (POC) G6PD testing in Brazil is critical for safe treatment of P. vivax malaria.Methodology/Principal findingsThis study evaluated the performance of the semi-quantitative, POC STANDARD G6PD Test (SD Biosensor, Republic of Korea). Participants were recruited at clinics and through an enriched sample in Manaus and Porto Velho, Brazil. G6PD and hemoglobin measurements were obtained from capillary samples at the POC using the STANDARD and HemoCue 201+ (HemoCue AB, Sweden) tests. A thick blood slide was prepared for malaria microscopy. At the laboratories, the STANDARD and HemoCue tests were repeated on venous samples and a quantitative spectrophotometric G6PD reference assay was performed (Pointe Scientific, Canton, MI). G6PD was also assessed by fluorescent spot test. In Manaus, a complete blood count was performed.Samples were analyzed from 1,736 participants. In comparison to spectrophotometry, the STANDARD G6PD Test performed equivalently in determining G6PD status in venous and capillary specimens under varied operating temperatures. Using the manufacturer-recommended reference value thresholds, the test’s sensitivity at the <30% threshold on both specimen types was 100% (95% confidence interval [CI] venous 93.6%–100.0%; capillary 93.8%–100.0%). Specificity was 98.6% on venous specimens (95% CI 97.9%–99.1%) and 97.8% on capillary (95% CI 97.0%–98.5%). At the 70% threshold, the test’s sensitivity was 96.9% on venous specimens (95% CI 83.8%–99.9%) and 94.3% on capillary (95% CI 80.8%–99.3%). Specificity was 96.5% (95% CI 95.0%–97.6%) and 92.3% (95% CI 90.3%–94.0%) on venous and capillary specimens, respectively.Conclusion/SignificanceThe STANDARD G6PD Test is a promising tool to aid in POC detection of G6PD deficiency in Brazil.Trial registrationThis study was registered with ClinicalTrials.gov (identifier: ). NCT04033640相似文献
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There is a wealth of information regarding the import and export of nuclear proteins in general. Nevertheless, the available data that deals with the nucleocytoplasmic movement of steroid hormone receptors remains highly limited. Some research findings reported during the past five years have succeeded in identifying proteins related to the movement of estrogen receptor alpha from the cytoplasm to the nucleus. What is striking in these findings is the facilitatory role of estradiol in the transport process. A similar conclusion has been drawn from the studies on the plasma membrane-to nucleus movement of the alternative form of estrogen receptor, the non-activated estrogen receptor (naER). The internalization of naER from the plasma membrane takes place only in the presence of estradiol. While the gene regulatory functions of ER alpha appear to get terminated following its ubiquitinization within the nucleus, the naER, through its deglycosylated form, the nuclear estrogen receptor II (nER II) continues to remain functional even beyond its existence within the nucleus. Recent studies have indicated the possibility that the estrogen receptor that regulates the nucleo cytoplasmic transport of m RNP is the nERII. This appears to be the result of the interaction between nERII and three proteins belonging to a group of small nuclear ribonucleo proteins (snRNP). The interaction of nERII with two of this protein appears to activate the inherent Mg2+ ATPase activity of the complex, which leads to the exit of the RNP through the nuclear pore complex. 相似文献
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Elizabeth M. Haynes Sreeja B. Asokan Samantha J. King Heath E. Johnson Jason M. Haugh James E. Bear 《The Journal of cell biology》2015,209(6):803-812
The lamellipodium is an important structure for cell migration containing branched actin nucleated via the Arp2/3 complex. The formation of branched actin is relatively well studied, but less is known about its disassembly and how this influences migration. GMF is implicated in both Arp2/3 debranching and inhibition of Arp2/3 activation. Modulation of GMFβ, a ubiquitous GMF isoform, by depletion or overexpression resulted in changes in lamellipodial dynamics, branched actin content, and migration. Acute pharmacological inhibition of Arp2/3 by CK-666, coupled to quantitative live-cell imaging of the complex, showed that depletion of GMFβ decreased the rate of branched actin disassembly. These data, along with mutagenesis studies, suggest that debranching (not inhibition of Arp2/3 activation) is a primary activity of GMFβ in vivo. Furthermore, depletion or overexpression of GMFβ disrupted the ability of cells to directionally migrate to a gradient of fibronectin (haptotaxis). These data suggest that debranching by GMFβ plays an important role in branched actin regulation, lamellipodial dynamics, and directional migration. 相似文献
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R. Sreeja S. Balaji L. Arul A. Nirmala Kumari J. R. Kannan Bapu A. Subramanian 《Molecular breeding : new strategies in plant improvement》2016,36(11):149
To understand the lodging behavior in kodo millet (Paspalum scrobiculatum L.) at morphological, biochemical, and molecular levels, 22 germplasm accessions selected based on previous trials were characterized for culm strength-related morphological traits such as pulling force, culm weight per unit length, culm diameter, recovery angle after bending and degree of lodging, and biochemical traits such as cellulose, hemicellulose, and lignin content of the culm. Correlation among traits and path analysis with degree of lodging showed that only lignin content per unit length of the culm had a very high negative effect on degree of lodging, followed by culm diameter, which means that higher the lignin content and culm diameter, the lesser will be the degree of lodging. Hence, it was concluded that any improvement for lodging resistance in kodo millet can be achieved through improving the lignin content (mg/cm of the dry culm) and culm diameter. Gene expression studies in kodo millet for FLEXIBLE CULM 1 (FC1), a gene implicated in lignin biosynthetic pathway and lodging resistance in rice, suggests the role of FC1 gene ortholog in lignin accumulation in kodo millet as well. Accordingly, the highest gene expression was recorded in strong culm line “Adari” a land race and the lowest expression in “Aamo 10,” a weak culm line. 相似文献
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C. Jasmin Sreeja Chellappan Rajeev K. Sukumaran K. K. Elyas Sarita G. Bhat M. Chandrasekaran 《World journal of microbiology & biotechnology》2010,26(7):1269-1279
An alkaline protease gene (Eap) was isolated for the first time from a marine fungus, Engyodontium album. Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular
mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology
model of the Engyodontium album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate
specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to
have two disulfide bonds and more than two Ca2+ binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein. 相似文献
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