The Experts below are selected from a list of 252 Experts worldwide ranked by ideXlab platform
Leyu Wang - One of the best experts on this subject based on the ideXlab platform.
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a biosynthesized gold nanoparticle from staphylococcus aureus as a Functional Factor in muscle tissue engineering
Applied Materials Today, 2021Co-Authors: Renjie Qiu, Weirong Xiong, Wenxi Hua, Xiaomin Sun, Malcolm Xing, Leyu WangAbstract:Abstract Nano-biosynthesis for gold nanoparticle (AuNP) using bacteria can produce the tailored Functional AuNP because of the different bioactive molecules coating on the AuNP derived from different bacteria. However, the biosynthesis for the biocompatible AuNP from the harmful bacteria is still challenging, and the extensive application of the bacteria-derived AuNP in tissue repair is lacking. In this study, without other auxiliary chemical molecules, the gradient centrifugation was used to successfully remove the toxic part of the pristine AuNPs biosynthesized from Staphylococcus aureus (S. aureus). The purified S. aureus-derived AuNPs were proved to be beneficial for the muscle cells’ viability and could even protect the cells against the cardiotoxin damages. Furthermore, the S. aureus-derived AuNPs were assembled into an elastic scaffold to form the AuNPs-incorporated cardiac patch. The in vivo study in rat myocardial infarction (MI) models demonstrated that these S. aureus-derived AuNPs could be taken as a Functional Factor in the cardiac patch to promote MI repair, through decreasing the infarct area and improving the cardiac function of the infarct heart. This study provides a Functional S. aureus-derived AuNP with tissue repair potential, which can be extensively applied in muscle tissue engineering.
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A biosynthesized gold nanoparticle from Staphylococcus aureus – as a Functional Factor in muscle tissue engineering
Applied Materials Today, 1Co-Authors: Renjie Qiu, Weirong Xiong, Wenxi Hua, Xiaomin Sun, Malcolm Xing, Leyu WangAbstract:Abstract Nano-biosynthesis for gold nanoparticle (AuNP) using bacteria can produce the tailored Functional AuNP because of the different bioactive molecules coating on the AuNP derived from different bacteria. However, the biosynthesis for the biocompatible AuNP from the harmful bacteria is still challenging, and the extensive application of the bacteria-derived AuNP in tissue repair is lacking. In this study, without other auxiliary chemical molecules, the gradient centrifugation was used to successfully remove the toxic part of the pristine AuNPs biosynthesized from Staphylococcus aureus (S. aureus). The purified S. aureus-derived AuNPs were proved to be beneficial for the muscle cells’ viability and could even protect the cells against the cardiotoxin damages. Furthermore, the S. aureus-derived AuNPs were assembled into an elastic scaffold to form the AuNPs-incorporated cardiac patch. The in vivo study in rat myocardial infarction (MI) models demonstrated that these S. aureus-derived AuNPs could be taken as a Functional Factor in the cardiac patch to promote MI repair, through decreasing the infarct area and improving the cardiac function of the infarct heart. This study provides a Functional S. aureus-derived AuNP with tissue repair potential, which can be extensively applied in muscle tissue engineering.
Randal J. Kaufman - One of the best experts on this subject based on the ideXlab platform.
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atp dependent dissociation of non disulfide linked aggregates of coagulation Factor viii is a rate limiting step for secretion
Biochemistry, 2000Co-Authors: Luigina Tagliavacca, Qingcai Wang, Randal J. KaufmanAbstract:Deficiency in coagulation Factor VIII leads to the bleeding disorder hemophilia A. Previous studies demonstrated that Factor VIII secretion is limited due to an ATP-requiring step early in the secretory pathway. In this report, we identified that this ATP-dependent rate-limiting step involves the dissociation of non-disulfide-linked aggregates within the endoplasmic reticulum (ER). In contrast to the numerous examples of interchain disulfide-linked aggregates, Factor VIII is the first protein characterized to form non-disulfide-linked high molecular weight aggregates within the ER. Approximately a third of newly synthesized Factor VIII was detected in high molecular weight aggregates. These aggregates disappeared over time as Functional Factor VIII appeared in the medium. The aggregated complexes did not require proteasomal degradation for clearance. Aggregate formation was enhanced by ATP depletion, and upon restoration of metabolic energy, these aggregates were dissociated and secreted. With the coexpre...
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Post-translational requirements for Functional Factor V and Factor VIII secretion in mammalian cells.
The Journal of biological chemistry, 1994Co-Authors: D D Pittman, K N Tomkinson, Randal J. KaufmanAbstract:Coagulation Factors V and VIII are homologous glycosylated plasma proteins that provide essential functions for hemostasis. Factor V is secreted as a single chain polypeptide, whereas Factor VIII is processed intracellularly to yield a metal-ion-associated heterodimer that is stabilized through interaction with von Willebrand Factor. In transfected mammalian cells, Factor V is more efficiently secreted than Factor VIII. To provide insight into the different secretion efficiencies, we compared the post-translational processing requirements for Factor V and Factor VIII expressed in mammalian cells. In contrast to Factor VIII, Factor V was not detected in association with the immunoglobulin-binding protein (BiP), a chaperonin protein of the endoplasmic reticulum (ER). Depletion of intracellular ATP levels by treatment of cells with low concentrations of carbonyl cyanide 3-chlorophenylhydrazone (CCCP), protonophore that uncouples oxidative phosphorylation, inhibited secretion of Factor VIII but had no effect on the secretion of Factor V. Inhibition of N-linked oligosaccharide addition by treatment with tunicamycin prevented secretion of both Factor V and Factor VIII, whereas treatment with an inhibitor of complex oligosaccharide addition, deoxymannojirimycin, did not affect secretion, although the specific activities of both Factor V and Factor VIII were slightly increased. Thus, complex oligosaccharide addition was not required for secretion or Functional activity of either Factor V or Factor VIII. Depletion of intralumenal calcium with the ionophore A23187 did not affect secretion of either Factor V or Factor VIII. In the presence of A23187, the secreted Factor V was fully Functional, whereas the Factor VIII heavy and light chains were not associated and the secreted molecule was inactive. In addition, A23187 treatment inhibited addition of serine/threonine (O)-linked oligosaccharides to Factor V and Factor VIII. The differences between Factor V and Factor VIII were further evaluated by characterization of a single chain mutant Factor VIII. The single chain Factor VIII was secreted with an efficiency similar to wild-type Factor VIII and also required von Willebrand Factor for stabilization. In addition, the activity of single chain Factor VIII was also inhibited by A23187 treatment, suggesting a unique metal-ion requirement within the secretory pathway for Functional Factor VIII folding. The differences identified in BiP association, ATP requirements, and metal-ion dependence for effective Functional secretion of these two molecules may underlie mechanisms accounting for their different secretion efficiencies.
J A Van Mourik - One of the best experts on this subject based on the ideXlab platform.
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The pro-polypeptide of von Willebrand Factor is required for the formation of a Functional Factor VIII-binding site on mature von Willebrand Factor.
The Biochemical journal, 1991Co-Authors: A Leyte, J Voorberg, H B Van Schijndel, B Duim, H Pannekoek, J A Van MourikAbstract:We have established that a recombinant von Willebrand Factor (vWF) mutant (vWFdelpro) that lacks the propolypeptide, in contrast with mature wild-type vWF, with which it is identical in terms of primary amino acid sequence, is not able to form a complex with Factor VIII. Wild-type vWF (flvWF) and vWFdelpro were expressed in AtT-20 cells. Under the culture conditions employed, completely processed multimerized flvWF and dimeric vWFdelpro were secreted into the medium. FlvWF and vWFdelpro were compared for their Factor VIII-binding properties in two distinct assay systems. In a direct binding assay, purified human Factor VIII was shown to bind to flvWF that had been immobilized on the surface of microtitre wells by using an anti-vWF monoclonal antibody. In contrast, Factor VIII did not bind to immobilized vWFdelpro. In a competition assay, fluid-phase flvWF appeared to inhibit efficiently the binding of Factor VIII to immobilized vWF isolated from plasma, whereas vWFdelpro did not influence Factor VIII binding. From these observations, it is argued that the pro-polypeptide serves an essential role in the post-translational processes that lead to the expression of a Functional Factor VIII-binding site on the mature vWF subunit.
Renjie Qiu - One of the best experts on this subject based on the ideXlab platform.
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a biosynthesized gold nanoparticle from staphylococcus aureus as a Functional Factor in muscle tissue engineering
Applied Materials Today, 2021Co-Authors: Renjie Qiu, Weirong Xiong, Wenxi Hua, Xiaomin Sun, Malcolm Xing, Leyu WangAbstract:Abstract Nano-biosynthesis for gold nanoparticle (AuNP) using bacteria can produce the tailored Functional AuNP because of the different bioactive molecules coating on the AuNP derived from different bacteria. However, the biosynthesis for the biocompatible AuNP from the harmful bacteria is still challenging, and the extensive application of the bacteria-derived AuNP in tissue repair is lacking. In this study, without other auxiliary chemical molecules, the gradient centrifugation was used to successfully remove the toxic part of the pristine AuNPs biosynthesized from Staphylococcus aureus (S. aureus). The purified S. aureus-derived AuNPs were proved to be beneficial for the muscle cells’ viability and could even protect the cells against the cardiotoxin damages. Furthermore, the S. aureus-derived AuNPs were assembled into an elastic scaffold to form the AuNPs-incorporated cardiac patch. The in vivo study in rat myocardial infarction (MI) models demonstrated that these S. aureus-derived AuNPs could be taken as a Functional Factor in the cardiac patch to promote MI repair, through decreasing the infarct area and improving the cardiac function of the infarct heart. This study provides a Functional S. aureus-derived AuNP with tissue repair potential, which can be extensively applied in muscle tissue engineering.
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A biosynthesized gold nanoparticle from Staphylococcus aureus – as a Functional Factor in muscle tissue engineering
Applied Materials Today, 1Co-Authors: Renjie Qiu, Weirong Xiong, Wenxi Hua, Xiaomin Sun, Malcolm Xing, Leyu WangAbstract:Abstract Nano-biosynthesis for gold nanoparticle (AuNP) using bacteria can produce the tailored Functional AuNP because of the different bioactive molecules coating on the AuNP derived from different bacteria. However, the biosynthesis for the biocompatible AuNP from the harmful bacteria is still challenging, and the extensive application of the bacteria-derived AuNP in tissue repair is lacking. In this study, without other auxiliary chemical molecules, the gradient centrifugation was used to successfully remove the toxic part of the pristine AuNPs biosynthesized from Staphylococcus aureus (S. aureus). The purified S. aureus-derived AuNPs were proved to be beneficial for the muscle cells’ viability and could even protect the cells against the cardiotoxin damages. Furthermore, the S. aureus-derived AuNPs were assembled into an elastic scaffold to form the AuNPs-incorporated cardiac patch. The in vivo study in rat myocardial infarction (MI) models demonstrated that these S. aureus-derived AuNPs could be taken as a Functional Factor in the cardiac patch to promote MI repair, through decreasing the infarct area and improving the cardiac function of the infarct heart. This study provides a Functional S. aureus-derived AuNP with tissue repair potential, which can be extensively applied in muscle tissue engineering.
Guanghua Zhao - One of the best experts on this subject based on the ideXlab platform.
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Structure, Function, and Nutrition of Ferritin from Foodstuffs
Mineral Containing Proteins, 2017Co-Authors: Taro Masuda, Hai Chen, Guanghua ZhaoAbstract:Iron deficiency anemia (IDA) is the most common and widespread nutritional disorder in the world, so it is crucial to explore a safe and efficient Functional Factor for iron supplement. Fortunately, ferritin as a class of naturally occurring iron storage proteins can accommodate 4500 iron atoms within its inner cavity. Thus, it seems to be a suitable candidate as novel, utilizable forms of iron supplementary for populations with a low iron status. Additionally, ferritin also can be used as a vehicle for bioactive compounds delivery after the remove of the iron. This chapter focuses on recent progress in structure, function, and nutrition of ferritin.
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Structure, function, and nutrition of phytoferritin: a newly Functional Factor for iron supplement.
Critical reviews in food science and nutrition, 2014Co-Authors: Xiayun Liao, Shaojun Yun, Guanghua ZhaoAbstract:Ferritins are members of the superfamily of iron storage and detoxification proteins present in all living organisms and play important roles in controlling cellular iron homeostasis. In contrast to animal ferritin, relatively little information is available on the structure and function of phytoferritin. Phytoferritin is observed in plastids whereas animal ferritins are largely found in the cytoplasm of cell. Compared to animal ferritin, phytoferritin exhibits two major distinctive features in structure. First, phytoferritin contains a specific extension peptide (EP) at the N-terminal while animal ferritin lacks it. The EP is located on the exterior surface of protein, which recently has been found to act as a second ferroxidase center for iron-binding and oxidation, and regulate iron release during the germination and early growth of seedlings. Second, only H-type subunit has been identified in phytoferritin, which is usually a heteropolymer consisting of two different subunits, H-1 and H-2, sharing ~80% amino acid sequence identity. These two subunits in phytoferritin play a positively cooperative role in iron oxidative deposition in protein. Iron deficiency anemia (IDA) is the most common and widespread nutritional disorder in the world, so it is crucial to explore a safe and efficient Functional Factor for iron supplement. Fortunately, phytoferritin seems to be a suitable candidate. In legume seeds, more than 90% of iron is stored in the form of ferritin in amyloplasts. Recently, some studies at different levels have demonstrated that plant ferritin could be used as novel, utilizable, plant-based forms of iron for populations with a low iron status. This review focuses on recent progress in structure, function, and nutrition of phytoferritin.
