scholarly journals In Vivo Imaging of Transport and Biocompatibility of Single Silver Nanoparticles in Early Development of Zebrafish Embryos

ACS Nano ◽  
2007 ◽  
Vol 1 (2) ◽  
pp. 133-143 ◽  
Author(s):  
Kerry J. Lee ◽  
Prakash D. Nallathamby ◽  
Lauren M. Browning ◽  
Christopher J. Osgood ◽  
Xiao-Hong Nancy Xu
2016 ◽  
Vol 8 (39) ◽  
pp. 25650-25653 ◽  
Author(s):  
Xin Zhang ◽  
Meinan Yao ◽  
Muhua Chen ◽  
Liqiang Li ◽  
Chengyan Dong ◽  
...  

2012 ◽  
Vol 25 (5) ◽  
pp. 1029-1046 ◽  
Author(s):  
Kerry J. Lee ◽  
Lauren M. Browning ◽  
Prakash D. Nallathamby ◽  
Tanvi Desai ◽  
Pavan K. Cherukuri ◽  
...  

2020 ◽  
Vol 21 (5) ◽  
pp. 1876
Author(s):  
Liyuan Qiang ◽  
Zeinab H. Arabeyyat ◽  
Qi Xin ◽  
Vesselin N. Paunov ◽  
Imogen J. F. Dale ◽  
...  

Silver nanoparticles (AgNPs) are widely used in commercial applications as antimicrobial agents, but there have recently been increasing concerns raised about their possible environmental and health impacts. In this study, zebrafish embryos were exposed to two sizes of AgNP, 4 and 10 nm, through a continuous exposure from 4 to 96 h post-fertilisation (hpf), to study their uptake, impact and molecular defense responses. Results showed that zebrafish embryos were significantly impacted by 72 hpf when continuously exposed to 4 nm AgNPs. At concentrations above 0.963 mg/L, significant in vivo uptake and delayed yolk sac absorption was evident; at 1.925 mg/L, significantly reduced body length was recorded compared to control embryos. Additionally, 4 nm AgNP treatment at the same concentration resulted in significantly upregulated hypoxia inducible factor 4 (HIF4) and peroxisomal membrane protein 2 (Pxmp2) mRNA expression in exposed embryos 96 hpf. In contrast, no significant differences in terms of larvae body length, yolk sac absorption or gene expression levels were observed following exposure to 10 nm AgNPs. These results demonstrated that S4 AgNPs are available for uptake, inducing developmental (measured as body length and yolk sac area) and transcriptional (specifically HIF4 and Pxmp2) perturbations in developing embryos. This study suggests the importance of particle size as one possible factor in determining the developmental toxicity of AgNPs in fish embryos.


2016 ◽  
Vol 18 (8) ◽  
Author(s):  
Dina A. Mosselhy ◽  
Wei He ◽  
Dan Li ◽  
Yaping Meng ◽  
Qingling Feng

Blood ◽  
2016 ◽  
Vol 128 (22) ◽  
pp. 4282-4282
Author(s):  
Ken-Hong Lim ◽  
Yu-Cheng Chang ◽  
Yi-Hao Chiang ◽  
Huan-Chau Lin ◽  
Chiao-Yi Chang ◽  
...  

Abstract Introduction: Calreticulin (CALR) is a 46-kDa highly conserved, multicompartmental and multifunctional protein. CALR acts as a Ca2+ binding chaperone protein and participates in ensuring proper protein and glycoprotein folding in the endoplasmic reticulum. CALR mutations have been identified in about 30% of JAK2 and MPL unmutated essential thrombocythemia and primary myelofibrosis. Although the expression of CALR mutants resulted in pathogenic thrombocytosis in adult mice, whether CALR mutants may disrupt normal hematopoiesis during early development remains unknown. Here we aimed to evaluate the effects of mutant CALR during embryonic hematopoietic development using the in vivo zebrafish model. Methods: Full-length CALR wild-type,and CALR-del52 and CALR-ins5 mutants cDNAs were subcloned in the pCS2+ vector and a bicistronic pSYC-102 T2A vector, respectively. Capped CALR mRNAs from the above vectors were micro-injected into 1-2 cells stage wild-type AB strain, Tg(cd41:GFP) and Tg(fli1:EGFP) zebrafish embryos, respectively. cd41+ thrombocytes were counted at 3 and 5 days post fertilization (dpf), respectively. Gene expression of hematopoietic lineage-specific and cytokine and cytokine receptor genes were evaluated by quantitative reverse-transcription and real-time polymerase chain reaction (Q-PCR) from 1 to 3 dpf. Morpholino (MO) was used to knock down cytokine receptor genes mpl, epor and csf3r. Results: The expression of CALR proteins from the injection of 100 pg mRNA was confirmed by CALR N-terminal and mutant specific antibodies, respectively. Expression of both CALR-del52 and CALR-ins5 mutant mRNA significantly increased the numbers of hematopoietic stem and progenitor cells in the caudal hematopoietic tissue when compared with CALR-wt mRNA at 3 dpf. No obvious changes in the angiogenesis were visualized in CALR-wt and mutant CALR expressing embryos at 3 dpf in the fli1:EGFP line when compared with uninjected control. Mutant CALR-del52 significantly increased the number of cd41+ thrombocytes at 5 dpf (mean 162.5±4.1 per embryo) when compared to CALR-wt (mean 117.1±3.1 per embryo, P<0.001), mutant CALR-ins5 (mean 128.3±6.1 per embryo, P<0.001) and uninjected control (mean 136.7±3.0 per embryo, P<0.001), respectively. At 5 dpf, the number of cd41+ thrombocytes significantly decreased upon mpl MO knockdown (mean 43.6±4.9 per embryo) when compared to the control MO group (mean 123.5±5.9 per embryo, P<0.001) and the mutant CALR-del52 group (P<0.001). Importantly, co-injection of CALR-del52 mutant mRNA (mean 73.7±5.1 per embryo) can only partially reverse the knockdown effect of mpl MO. In contrast, the numbers of cd41+ thrombocytes did not decrease significantly upon epor MO or csf3r MO knocked-down compared with the control MO group. When CALR-del52 mutant mRNA was co-injected with epor or csf3r MOs, the numbers of cd41+ thrombocytes were comparable to those of CALR-del52-injected embryos. In Q-PCR experiments, the expression of cmyb, runx1 and scl significantly increased in only CALR-ins5 mutant group at 3 dpf when compared to 2 dpf. The expression of αeHb and βeHb significantly decreased in both CALR-del52 and CALR-ins5 mutant groups at 2 dpf but the expression of gata1 remained unchange. The effects of CALR-del52 and CALR-ins5 mutant groups on the expression of cytokine and cytokine receptor genes included the upregulation of mpl at 1 dpf followed by progressive downregulation at 2 dpf and 3 dpf but relatively stable expression of tpo and epo during early development. In the group of genes related to thrombopoiesis, the expression of emilin1a and nbeal2 was significantly downregulated in CALR-del52 group at 3 dpf when compared to 2 dpf. Conclusions: In this study, we showed that the expression of mutant CALR causes thrombocytosis through an mpl-dependent mechanism and perturbs developmental hematopoiesis in zebrafish embryos. Disclosures No relevant conflicts of interest to declare.


2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light &gt;600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.


2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S588-S588
Author(s):  
Vladimir Kepe ◽  
Gregory M Cole ◽  
Jie Liu ◽  
Dorothy G Flood ◽  
Stephen P Trusko ◽  
...  

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