Palladin is an actin binding protein that is specifically upregulated in metastatic cancer cells but also co-localizes with actin stress fibers in normal cells and is critical for embryonic development as well as wound healing. Of nine isoforms present in humans, only the 90 kDa isoform of palladin, comprising three immunoglobulin (Ig) domains and one proline-rich region, is ubiquitously expressed. Previous work has also established that the Ig3 domain of palladin is the minimal binding site for F-actin. In this work, we compare functions of the 90 kDa isoform of palladin to the isolated actin binding domain. To understand the mechanism of action for how palladin can influence actin assembly, we monitored F-actin binding and bundling as well as actin polymerization, depolymerization, and copolymerization. We also provide initial evidence that 90 kDa palladin exists in a closed conformation that prevents binding by the Ig3 domain to G-actin as compared to the isolated domain. Understanding the role of palladin in regulating the actin cytoskeleton may help us develop means to prevent cancer cells from reaching the metastatic stage of cancer progression.
The days of easy oil are going. The frontier of oil and gas exploitation continues to be pushed further as a result of oil price volatility, new technologies, and an ever dynamic political and economic atmosphere. Production by primary and secondary recovery have been known to only recover a limited fraction of the oil in place thus the need to look into more innovative ways to improve recovery especially in declining assets through suitable EOR methods. Several EOR techniques have been developed for improving oil recovery from reservoirs one of which is Water Alternating Gas (WAG) injection. In this work, WAG is presented as a potential candidate to increase oil productivity in the Niger delta. WAG involves the cyclic injection of water and gas into the reservoir so as to squeeze out more oil. By decreasing gas mobility and capillary forces, guaranteeing effective microscopic displacement due to gas flooding and reducing the mobility ratio thus improving the macroscopic sweep created by water injection, it combines the advantages of water flooding and gas injection in optimizing residual oil production. This study aims at investigating the possible increase in oil production and reserves from a Niger Delta field through the use of Immiscible WAG injection as an EOR process. In conducting this study, various development strategies such as Gas Injection, Water Injection and Immiscible WAG were proposed in exploiting the reservoir. Using a conventional 3-D numerical simulator to mimic the process, comparison was then made between the various strategies where results such as field oil recovery, cumulative oil recovery and production rate were analysed. With Immiscible WAG injection, an increase in recovery above the very popular gas injection or water injection was observed. Parameters critical to the success of a WAG enhanced oil recovery process such as three-phase flow, hysteresis effect, WAG cycle, WAG ratio, and Injection rates and their effects was also studied.
Palladin is an actin binding protein that is specifically upregulated in metastatic cancer cells but also colocalizes with actin stress fibers in normal cells and is critical for embryonic development as well as wound healing. Of nine isoforms present in humans, only the 90 kDa isoform of palladin, comprising three immunoglobulin (Ig) domains and one proline‐rich region, is ubiquitously expressed. Previous work has established that the Ig3 domain of palladin is the minimal binding site for F‐actin. In this work, we compare functions of the 90 kDa isoform of palladin to the isolated actin binding domain. To understand the mechanism of action for how palladin can influence actin assembly, we monitored F‐actin binding and bundling as well as actin polymerization, depolymerization, and copolymerization. Together, these results demonstrate that there are key differences between the Ig3 domain and full‐length palladin in actin binding stoichiometry, polymerization, and interactions with G‐actin. Understanding the role of palladin in regulating the actin cytoskeleton may help us develop means to prevent cancer cells from reaching the metastatic stage of cancer progression.
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