scholarly journals Role of Changes in State of Bound Water and Tissue Stiffness in Development of Age-Related Diseases

Polymers ◽  
2020 ◽  
Vol 12 (6) ◽  
pp. 1362
Author(s):  
Garry Kerch

An essential effect of environmental stiffness on biological processes in cells at present is generally accepted. An increase in arterial stiffness with advanced age has been reported in many publications. The aim of the present review is to summarize current information about possible chemical reactions and physical processes that lead to tissue stiffening and result in age-related diseases in order to find methods that can prevent or retard time-dependent tissue stiffening. The analysis of published data shows that bound water acts as a plasticizer of biological tissues, a decrease in bound water content results in an increase in biological tissue stiffness, and increased tissue stiffness leads to NF-kB activation and triggered actin polymerization—NF-kB activation is associated with age-related diseases. It can be suggested that changes in bound water content through changing tissue stiffness can affect cellular processes and the development of pathologies related to aging. Both age-related diseases and COVID-19 may be associated with tight-junction disruption and increased tissue stiffness and permeability.

1996 ◽  
Vol 34 (3-4) ◽  
pp. 443-448 ◽  
Author(s):  
G. W. Chen ◽  
W. W. Lin ◽  
D. J. Lee

The feasibility of employment of capillary suction time (CST) for characterizing the dewaterability of excess activated sludges was examined. The CST was shown as a good index for sludge filterability, if only the product of solid concentration and average specific resistance is of interest. On the other hand, the bound water content cannot be directly evaluated from the CST data.


1938 ◽  
Vol 36 (1) ◽  
pp. 99-105 ◽  
Author(s):  
C. A. Friedman ◽  
B. S. Henry

2012 ◽  
Vol 38 (3) ◽  
pp. 197-200
Author(s):  
Khee-Hwan Choi ◽  
Myung-Jin Ann ◽  
Hong-Ha Son ◽  
Kyong-Seub Kim ◽  
Sang-Min Lee ◽  
...  

1988 ◽  
Vol 123 ◽  
pp. 153-161 ◽  
Author(s):  
Tatauko Hatakeyama ◽  
Kunio Nakamura ◽  
Hyoe Hatakeyama

2009 ◽  
Vol 20 (6) ◽  
pp. 1618-1628 ◽  
Author(s):  
Alastair S. Robertson ◽  
Ellen G. Allwood ◽  
Adam P.C. Smith ◽  
Fiona C. Gardiner ◽  
Rosaria Costa ◽  
...  

Actin plays an essential role in many eukaryotic cellular processes, including motility, generation of polarity, and membrane trafficking. Actin function in these roles is regulated by association with proteins that affect its polymerization state, dynamics, and organization. Numerous proteins have been shown to localize with cortical patches of yeast actin during endocytosis, but the role of many of these proteins remains poorly understood. Here, we reveal that the yeast protein Ysc84 represents a new class of actin-binding proteins, conserved from yeast to humans. It contains a novel N-terminal actin-binding domain termed Ysc84 actin binding (YAB), which can bind and bundle actin filaments. Intriguingly, full-length Ysc84 alone does not bind to actin, but binding can be activated by a specific motif within the polyproline region of the yeast WASP homologue Las17. We also identify a new monomeric actin-binding site on Las17. Together, the polyproline region of Las17 and Ysc84 can promote actin polymerization. Using live cell imaging, kinetics of assembly and disassembly of proteins at the endocytic site were analyzed and reveal that loss of Ysc84 and its homologue Lsb3 decrease inward movement of vesicles consistent with a role in actin polymerization during endocytosis.


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