Role of Aquaporin 1 Signalling in Cancer Development and Progression

Tomita, Yoko; Dorward, Hilary; Yool, Andrea J.; Smith, Eric; Townsend, Amanda; Price, Tim; Hardingham, Jennifer E.

doi:10.3390/ijms18020299

Cited by 95 publications

(96 citation statements)

References 116 publications

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“…Aquaporins (AQP) are widely distributed in tissues and cells, with AQP1 an integrative membrane protein in human erythrocytes responsible for maintaining cell permeability. Urine proteome analysis to identify disease biomarkers for prostate cancer, renal cell carcinoma, bladder cancer, urothelial carcinoma, and renal Fanconi syndrome suggested as a possible marker AQP1 (Morrissey, et al, 2015;Morrissey, et al, 2014;Rodrigues, et al, 2017;Rubenwolf, et al, 2009;Tomita, et al, 2017).…”

Section: Prostate Cancer Associated Network Analysismentioning

confidence: 99%

Disease associated protein-protein interaction network reconstruction based on comprehensive influence analysis

Zhu

Ling

et al. 2019

Preprint

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Proteins and their interactions are fundamental to biological system. With the scientific paradigm shifting to systems biology, functional study of proteins from a network viewpoint to get a deep understanding of their roles in human life and diseases being increasingly essential. Although several methods already existed for protein-protein interaction (PPI) network building, the precise reconstruction of disease associated PPI network remains a challenge. In this paper we introduce a novel concept of comprehensive influence of proteins in network, in which direct and indirect connections are adopted for the calculation of influential effects of a protein with different weights. With the optimized weights, we calculate and select the important proteins and their interactions to reconstruct the PPI network for further validation and confirmation. To evaluate the performance of the method, we compared our model with the six existed ones by using five standard data sets. The results indicated that our method outperforms the existed ones. We then applied our model to prostate cancer and Parkinson's disease to predict novel disease associated proteins for the future experimental validation. Author SummaryThe diverse protein-protein interaction networks have dramatic effects on biological system. The disease associated PPI networks are generally reconstructed from experimental data with computational models but with limited accuracy. We developed a novel concept of comprehensive influence of proteins in network for reconstructing the PPI network. Our model outperforms the state-of-the-art ones and we then applied our model to identify novel interactions for further validation. / 21experimental methods and the complexity of biomedical systems, the experimental results often present high false-positive and false-negative rates (Cheng, et al., 2016). Moreover, experimental verification of the PPI network is time consuming and expensive. Therefore, rapid and accurate computational methods represent useful alternative for predicting protein interactions, with such results providing guidance for experiments, including determination of unknown relationships between disease-causing genes and protein interactions (Zhu, et al., 2015). Such knowledge can be useful to the understanding of protein structure and evolution, as well as the overall function of the network and its associated dynamic processes (Cowen, et al., 2017;Hoeng, et al., 2014).The unknown interaction between proteins can be predicted by the theory of complex network. PPI network consists of nodes and edges, with the nodes representing proteins and the edges representing associations or interactions between the two proteins (Gani, et al., 2015). Libennowell et al. considered the influence of common neighbor nodes in the network and introduced similarity indices to include common neighbors (Libennowell and Kleinberg, 2007). Pujari et al. suggested that each attribute of a pair of connected proteins represents different information (Pujari and Kanawati, 2012), and L...

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Section: Prostate Cancer Associated Network Analysismentioning

confidence: 99%

Disease associated protein-protein interaction network reconstruction based on comprehensive influence analysis

Zhu

Ling

et al. 2019

Preprint

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“…has been associated with many types of carcinoma as a distinctive clinical prognostic factor. This has prompted researchers to evaluate the link between AQP1 and cancer biology [18]. AQP1 is overexpressed in multiple human cancers including that of biliary duct, bladder, brain, breast, cervix, colon, lung, nasopharynx and prostate.…”

Section: H180a/ R195vmentioning

confidence: 99%

Aquaporin–graphene interface: relevance to point-of-care device for renal cell carcinoma and desalination

et al. 2018

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Aquaporins superfamily of hydrophobic integral membrane proteins constitute water channels essential to the movement of water across the cell membrane maintaining homeostatic equilibrium. During the passage of water between the extracellular and intracellular sides of the cell, aquaporins act as ultra-sensitive filters. Due to their hydrophobic nature, aquaporins self-assemble in phospholipids and if a proper choice of lipids are made then the aquaporin biomimetic membrane can be used in the design of artificial kidney. In combination with graphene, aquaporin biomimetic membrane finds practical application in desalination and water recycling using mostly E.coli AqpZ. Recently, human aquaporin 1 has emerged as an important biomarker in renal cell carcinoma. At present the ultrasensitive sensing of renal cell carcinoma is cumbersome and hence we are discussing usage of epitopes from monoclonal antibody as a probe for Point-ofCare device for sensing renal cell carcinoma by immobilizing the antibody on the surface of a single layer graphene as a microfluidic device for sensing renal cell carcinoma which is pursued in our laboratories.

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“…AQP-1 is a transmembrane channel protein that facilitates the flux of water across the plasma membrane (Agre et al, 1993) and is one member of a family of at least 13 aquaporins (Ishibashi et al, 2011). AQP-1 has been detected in several aggressive human cancers and its expression correlates with poor disease prognosis (Tomita et al, 2017; De leso and Yool, 2018). However, the mechanistic basis of AQP-1 function is still unclear since studies have been limited to analyzing cell behaviors using in vitro assays.…”

Section: Introductionmentioning

confidence: 99%

Neural crest cells bulldoze through the microenvironment using Aquaporin-1 to stabilize filopodia

McLennan

McKinney

Teddy

et al. 2019

Preprint

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2Neural crest migration requires cells to move through an environment filled with dense 3 extracellular matrix and mesoderm to reach targets throughout the vertebrate embryo. 4 Here, we use high-resolution microscopy, computational modeling, and in vitro and in 5 vivo cell invasion assays to investigate the function of Aquaporin-1 (AQP-1) signaling. 6 We find that migrating lead cranial neural crest cells express AQP-1 mRNA and protein, 7 implicating a biological role for water channel protein function during invasion. 8 Differential AQP-1 levels affect neural crest cell speed, direction, and the length and 9 stability of cell filopodia. Further, AQP-1 enhances matrix metalloprotease (MMP) 10 activity and colocalizes with phosphorylated focal adhesion kinases (pFAK). Co-11 localization of AQP-1 expression with EphB guidance receptors in the same migrating 12 neural crest cells raises novel implications for the concept of guided bulldozing by lead 13 cells during migration. 14 15 3 1 INTRODUCTION 2 Cell migration is essential during embryogenesis to gastrulate, elongate the vertebrate 3 axis, and distribute cells into the periphery to contribute to organ development. Despite 4 the importance of cell migration to human development and disease, it is still unclear 5 what mechanisms enable cells to invade the dense ECM, mesoderm and other cell 6 types characteristic of the embryonic microenvironment. The complexity of the 7 embryonic microenvironment means that invading cells must rapidly change cell shape 8 and volume, form and sustain protrusions that penetrate different sized gaps, and attach 9 to and remodel the ECM. Thus, there is a tremendous need to identify and test the 10 function of molecules critical to embryonic cell migration and better understand their 11 mechanistic basis.12 13 Neural crest cell migration is one of the most prevalent examples of how cells efficiently 14 distribute throughout the growing vertebrate embryo to precise targets. In the head, 15 cranial neural crest cells must invade through dense ECM, loosely connected 16 mesoderm, and migrating endothelial cells. Yet, it has remained unclear how the 17 migrating neural crest cells that first encounter the embryonic microenvironment 18 penetrate small gaps between mesodermal cells and degrade the ECM to move in a 19 directed manner to peripheral targets. By combining dynamic in vivo imaging and super 20 resolution microscopy with gain-and loss-of-function experiments, we are poised to 21 examine the function of genes presumed critical to neural crest cell migration. Thus, the 22 embryonic neural crest is an attractive in vivo model to study the function of cell 23 invasion genes in mechanistic detail. 4 1 Using single cell RT-qPCR and transcriptome profiling, we discovered the enhanced 2 expression of several genes in the most invasive chick cranial neural crest cells, 3 including AQP-1 (McLennan et al., 2015a; Morrison et al., 2017a). AQP-1 is a 4 transmembrane channel protein that facilitates the flux of water across the plasma 5 5 ...

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Role of Aquaporin 1 Signalling in Cancer Development and Progression

Cited by 95 publications

References 116 publications

Disease associated protein-protein interaction network reconstruction based on comprehensive influence analysis

Disease associated protein-protein interaction network reconstruction based on comprehensive influence analysis

Aquaporin–graphene interface: relevance to point-of-care device for renal cell carcinoma and desalination

Neural crest cells bulldoze through the microenvironment using Aquaporin-1 to stabilize filopodia

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