Mitochondrial STAT3 and reactive oxygen species: a fulcrum of adipogenesis?
- Kramer, Adam H, Kadye, Rose, Houseman, Pascalene S, Prinsloo, Earl
- Authors: Kramer, Adam H , Kadye, Rose , Houseman, Pascalene S , Prinsloo, Earl
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/431674 , vital:72795 , xlink:href="https://doi.org/10.1080/21623996.2015.1084084"
- Description: The balance between cellular lineages can be controlled by reactive oxygen species (ROS). Cellular differentiation into adipocytes is highly dependent on the production of ROS to initiate the process through activation of multiple interlinked factors that stimulate mitotic clonal expansion and cellular maturation. The signal transducer and activator of transcription family of signaling proteins have accepted roles in adipogenesis and associated lipogenesis. Non-canonical mitochondrial localization of STAT3 and other members of the STAT family however opens up new avenues for investigation of its role in the aforementioned processes. Following recent observations of differences in mitochondrially localized serine 727 phosphorylated STAT3 (mtSTAT3-pS727) in preadipocytes and adipocytes, here, we hypothesize and speculate further on the role of mitochondrial STAT3 in adipogenesis.
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- Authors: Kramer, Adam H , Kadye, Rose , Houseman, Pascalene S , Prinsloo, Earl
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/431674 , vital:72795 , xlink:href="https://doi.org/10.1080/21623996.2015.1084084"
- Description: The balance between cellular lineages can be controlled by reactive oxygen species (ROS). Cellular differentiation into adipocytes is highly dependent on the production of ROS to initiate the process through activation of multiple interlinked factors that stimulate mitotic clonal expansion and cellular maturation. The signal transducer and activator of transcription family of signaling proteins have accepted roles in adipogenesis and associated lipogenesis. Non-canonical mitochondrial localization of STAT3 and other members of the STAT family however opens up new avenues for investigation of its role in the aforementioned processes. Following recent observations of differences in mitochondrially localized serine 727 phosphorylated STAT3 (mtSTAT3-pS727) in preadipocytes and adipocytes, here, we hypothesize and speculate further on the role of mitochondrial STAT3 in adipogenesis.
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Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) Protein
- Zininga, Tawanda, Achilonu, Ikechukwu, Hoppe, Heinrich, Prinsloo, Earl, Dirr, Heinrich W, Shonhai, Addmore
- Authors: Zininga, Tawanda , Achilonu, Ikechukwu , Hoppe, Heinrich , Prinsloo, Earl , Dirr, Heinrich W , Shonhai, Addmore
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/431719 , vital:72799 , xlink:href="https://doi.org/10.1371/journal.pone.0129445"
- Description: Six Hsp70-like genes are represented on the genome of Plasmodium falciparum. Of these two occur in the cytosol: P. falciparum Hsp70-z (PfHsp70-z) and PfHsp70-1. PfHsp70-1 is a well characterised canonical Hsp70 that facilitates protein quality control and is crucial for the development of malaria parasites. There is very little known about PfHsp70-z. However, PfHsp70-z is known to be essential and is implicated in suppressing aggregation of asparagine-rich proteins of P. falciparum. In addition, its expression at the clinical stage of malaria correlates with disease prognosis. Based on structural evidence PfHsp70-z belongs to the Hsp110 family of proteins. Since Hsp110 proteins have been described as nucleotide exchange factors (NEFs) of their canonical Hsp70 counterparts, it has been speculated that PfHsp70-z may serve as a NEF of PfHsp70-1. In the current study, P. falciparum cells cultured in vitro were subjected to heat stress, triggering the enhanced expression of PfHsp70-z. Biochemical assays conducted using recombinant PfHsp70-z protein demonstrated that the protein is heat stable and possesses ATPase activity. Furthermore, we observed that PfHsp70-z is capable of self-association. The structural-functional features of PfHsp70-z provide further evidence for its role as a chaperone and possible nucleotide exchange factor of PfHsp70-1.
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- Authors: Zininga, Tawanda , Achilonu, Ikechukwu , Hoppe, Heinrich , Prinsloo, Earl , Dirr, Heinrich W , Shonhai, Addmore
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/431719 , vital:72799 , xlink:href="https://doi.org/10.1371/journal.pone.0129445"
- Description: Six Hsp70-like genes are represented on the genome of Plasmodium falciparum. Of these two occur in the cytosol: P. falciparum Hsp70-z (PfHsp70-z) and PfHsp70-1. PfHsp70-1 is a well characterised canonical Hsp70 that facilitates protein quality control and is crucial for the development of malaria parasites. There is very little known about PfHsp70-z. However, PfHsp70-z is known to be essential and is implicated in suppressing aggregation of asparagine-rich proteins of P. falciparum. In addition, its expression at the clinical stage of malaria correlates with disease prognosis. Based on structural evidence PfHsp70-z belongs to the Hsp110 family of proteins. Since Hsp110 proteins have been described as nucleotide exchange factors (NEFs) of their canonical Hsp70 counterparts, it has been speculated that PfHsp70-z may serve as a NEF of PfHsp70-1. In the current study, P. falciparum cells cultured in vitro were subjected to heat stress, triggering the enhanced expression of PfHsp70-z. Biochemical assays conducted using recombinant PfHsp70-z protein demonstrated that the protein is heat stable and possesses ATPase activity. Furthermore, we observed that PfHsp70-z is capable of self-association. The structural-functional features of PfHsp70-z provide further evidence for its role as a chaperone and possible nucleotide exchange factor of PfHsp70-1.
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Photophysical properties and photodynamic therapy effect of zinc phthalocyanine-spermine-single walled carbon nanotube conjugate on MCF-7 breast cancer cell line
- Ogbodu, Rachael O, Limson, Janice L, Prinsloo, Earl, Nyokong, Tebello
- Authors: Ogbodu, Rachael O , Limson, Janice L , Prinsloo, Earl , Nyokong, Tebello
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/189493 , vital:44851 , xlink:href="https://doi.org/10.1016/j.synthmet.2015.03.011"
- Description: The present study shows improved photodynamic therapy (PDT) effect of zinc mono carboxy phenoxy phthalocyanine (ZnMCPPc (1)) upon conjugation to spermine (via amide bond) as a targeting molecule on MCF-7 breast cancer cells. The ZnMCPPc-spermine (2) conjugate was adsorbed onto single walled carbon nanotubes (represented as ZnMCPPc-spermine-SWCNT (3)). There was no change in the fluorescence quantum yield of complex 1 following formation of 2 or 3. Complexes 2 and 3 showed improved photophysical properties; with over 50% increases in triplet and singlet oxygen quantum yields compared to 1. Complexes 1, 2 and 3 were relatively not toxic to MCF-7 cancer cells when incubated with 5–40 μM of each complex for 24 h in the dark. The PDT results showed that at 40 μM complex 1 resulted in only 64% decrease in cell viability, while 2 and 3 improved the PDT effect of 1 to 97% and 95% decrease in cell viability at 40 μM respectively.
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- Authors: Ogbodu, Rachael O , Limson, Janice L , Prinsloo, Earl , Nyokong, Tebello
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/189493 , vital:44851 , xlink:href="https://doi.org/10.1016/j.synthmet.2015.03.011"
- Description: The present study shows improved photodynamic therapy (PDT) effect of zinc mono carboxy phenoxy phthalocyanine (ZnMCPPc (1)) upon conjugation to spermine (via amide bond) as a targeting molecule on MCF-7 breast cancer cells. The ZnMCPPc-spermine (2) conjugate was adsorbed onto single walled carbon nanotubes (represented as ZnMCPPc-spermine-SWCNT (3)). There was no change in the fluorescence quantum yield of complex 1 following formation of 2 or 3. Complexes 2 and 3 showed improved photophysical properties; with over 50% increases in triplet and singlet oxygen quantum yields compared to 1. Complexes 1, 2 and 3 were relatively not toxic to MCF-7 cancer cells when incubated with 5–40 μM of each complex for 24 h in the dark. The PDT results showed that at 40 μM complex 1 resulted in only 64% decrease in cell viability, while 2 and 3 improved the PDT effect of 1 to 97% and 95% decrease in cell viability at 40 μM respectively.
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Photophysicochemical properties and in vitro cytotoxicity of zinc tetracarboxyphenoxy phthalocyanine–quantum dot nanocomposites
- Oluwole, David O, Tilbury, Chelsea M, Prinsloo, Earl, Limson, Janice L, Nyokong, Tebello
- Authors: Oluwole, David O , Tilbury, Chelsea M , Prinsloo, Earl , Limson, Janice L , Nyokong, Tebello
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/240846 , vital:50878 , xlink:href="https://doi.org/10.1016/j.poly.2015.12.060"
- Description: Cadmium based quantum dots (QDs) capped with two different ligands (thioglycolic acid, TGA, and glutathione, GSH) were synthesized. The QDs are: CdTe, CdTe/ZnO, CdTeSe, CdTeSe/ZnO and CdSe/ZnS (the last one for TGA only). Cytotoxicity of the QDs against MCF-7 epithelial breast cancer was evaluated. The TGA capped core QDs were found to be highly cytotoxic to the cell lines when compared to GSH capped ones. The glutathione capped QDs were covalently linked to zinc tetracarboxyphenoxy phthalocyanine (ZnTCPPc). Cytotoxicity and photophysicochemical properties of the conjugates were investigated. The toxicity of the core QDs was reduced in the presence of ZnTCPPc. Enhanced triplet quantum yields and long triplet lifetimes were obtained for ZnTCPPc in the presence of all QDs.
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- Authors: Oluwole, David O , Tilbury, Chelsea M , Prinsloo, Earl , Limson, Janice L , Nyokong, Tebello
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/240846 , vital:50878 , xlink:href="https://doi.org/10.1016/j.poly.2015.12.060"
- Description: Cadmium based quantum dots (QDs) capped with two different ligands (thioglycolic acid, TGA, and glutathione, GSH) were synthesized. The QDs are: CdTe, CdTe/ZnO, CdTeSe, CdTeSe/ZnO and CdSe/ZnS (the last one for TGA only). Cytotoxicity of the QDs against MCF-7 epithelial breast cancer was evaluated. The TGA capped core QDs were found to be highly cytotoxic to the cell lines when compared to GSH capped ones. The glutathione capped QDs were covalently linked to zinc tetracarboxyphenoxy phthalocyanine (ZnTCPPc). Cytotoxicity and photophysicochemical properties of the conjugates were investigated. The toxicity of the core QDs was reduced in the presence of ZnTCPPc. Enhanced triplet quantum yields and long triplet lifetimes were obtained for ZnTCPPc in the presence of all QDs.
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Plasmodium falciparum Hop (PfHop) interacts with the Hsp70 chaperone in a nucleotide-dependent fashion and exhibits ligand selectivity
- Zininga, Tawanda, Makumire, Stanley, Gitau, Grace W, Njunge, James M, Pooe, Ofentse J, Klimek, Hanna, Scheurr, Robina, Raifer, Hartmann, Prinsloo, Earl, Przyborski, Jude M, Hoppe, Heinrich, Shonhai, Addmore
- Authors: Zininga, Tawanda , Makumire, Stanley , Gitau, Grace W , Njunge, James M , Pooe, Ofentse J , Klimek, Hanna , Scheurr, Robina , Raifer, Hartmann , Prinsloo, Earl , Przyborski, Jude M , Hoppe, Heinrich , Shonhai, Addmore
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/431752 , vital:72801 , xlink:href=" https://doi.org/10.1371/journal.pone.0135326"
- Description: Heat shock proteins (Hsps) play an important role in the development and pathogenicity of malaria parasites. One of the most prominent functions of Hsps is to facilitate the folding of other proteins. Hsps are thought to play a crucial role when malaria parasites invade their host cells and during their subsequent development in hepatocytes and red blood cells. It is thought that Hsps maintain proteostasis under the unfavourable conditions that malaria parasites encounter in the host environment. Although heat shock protein 70 (Hsp70) is capable of independent folding of some proteins, its functional cooperation with heat shock protein 90 (Hsp90) facilitates folding of some proteins such as kinases and steroid hormone receptors into their fully functional forms. The cooperation of Hsp70 and Hsp90 occurs through an adaptor protein called Hsp70-Hsp90 organising protein (Hop). We previously characterised the Hop protein from Plasmodium falciparum (PfHop). We observed that the protein co-localised with the cytosol-localised chaperones, PfHsp70-1 and PfHsp90 at the blood stages of the malaria parasite. In the current study, we demonstrated that PfHop is a stress-inducible protein. We further explored the direct interaction between PfHop and PfHsp70-1 using far Western and surface plasmon resonance (SPR) analyses.
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- Authors: Zininga, Tawanda , Makumire, Stanley , Gitau, Grace W , Njunge, James M , Pooe, Ofentse J , Klimek, Hanna , Scheurr, Robina , Raifer, Hartmann , Prinsloo, Earl , Przyborski, Jude M , Hoppe, Heinrich , Shonhai, Addmore
- Date: 2015
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/431752 , vital:72801 , xlink:href=" https://doi.org/10.1371/journal.pone.0135326"
- Description: Heat shock proteins (Hsps) play an important role in the development and pathogenicity of malaria parasites. One of the most prominent functions of Hsps is to facilitate the folding of other proteins. Hsps are thought to play a crucial role when malaria parasites invade their host cells and during their subsequent development in hepatocytes and red blood cells. It is thought that Hsps maintain proteostasis under the unfavourable conditions that malaria parasites encounter in the host environment. Although heat shock protein 70 (Hsp70) is capable of independent folding of some proteins, its functional cooperation with heat shock protein 90 (Hsp90) facilitates folding of some proteins such as kinases and steroid hormone receptors into their fully functional forms. The cooperation of Hsp70 and Hsp90 occurs through an adaptor protein called Hsp70-Hsp90 organising protein (Hop). We previously characterised the Hop protein from Plasmodium falciparum (PfHop). We observed that the protein co-localised with the cytosol-localised chaperones, PfHsp70-1 and PfHsp90 at the blood stages of the malaria parasite. In the current study, we demonstrated that PfHop is a stress-inducible protein. We further explored the direct interaction between PfHop and PfHsp70-1 using far Western and surface plasmon resonance (SPR) analyses.
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