Impact of amino acid substitutions in domain 5 of high molecular weight kininogen on suppression of breast cancer cells invasion

Author(s):  
Han Xiao ◽  
An Liping ◽  
Xu Guangyu ◽  
Zhang Xiujuan ◽  
Du Peige
Oncogene ◽  
2019 ◽  
Vol 38 (22) ◽  
pp. 4297-4309 ◽  
Author(s):  
Yufang Zhao ◽  
Shupei Qiao ◽  
Xiaolu Hou ◽  
Hui Tian ◽  
Shuai Deng ◽  
...  

Soft Matter ◽  
2020 ◽  
Vol 16 (42) ◽  
pp. 9669-9673
Author(s):  
Dmitry V. Vishnevetskii ◽  
Arif R. Mekhtiev ◽  
Tatyana V. Perevozova ◽  
Dmitry V. Averkin ◽  
Alexandra I. Ivanova ◽  
...  

We present a method for the preparation of a new hydrogel based on low molecular weight gelators that exhibits selective toxicity towards MCF-7 human breast cancer cells.


Polymers ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 1094 ◽  
Author(s):  
Hsin-Ta Wang ◽  
Po-Chien Chou ◽  
Ping-Han Wu ◽  
Chi-Ming Lee ◽  
Kang-Hsin Fan ◽  
...  

Low-molecular-weight hyaluronic acid (LMWHA) was integrated with superparamagnetic Fe3O4 nanoparticles (Fe3O4 NPs). The size distribution, zeta potential, viscosity, thermogravimetric and paramagnetic properties of the LMWHA-Fe3O4 NPs were systematically examined. For cellular experiments, MCF7 breast cancer cell line was carried out. In addition, the cell targeting ability and characteristics of the LMWHA-Fe3O4 NPs for MCF7 breast cancer cells were analyzed using the thiocyanate method and time-of-flight secondary ion mass spectrometry (TOF-SIMS). The experimental results showed that the LMWHA-Fe3O4 NPs were not only easily injectable due to their low viscosity, but also exhibited a significant superparamagnetic property. Furthermore, the in vitro assay results showed that the NPs had negligible cytotoxicity and exhibited a good cancer cell targeting ability. Overall, the results therefore suggest that the LMWHA-Fe3O4 NPs have considerable potential as an injectable agent for enhanced magnetic resonance imaging (MRI) and/or hyperthermia treatment in breast cancer therapy.


1998 ◽  
Vol 180 (2) ◽  
pp. 395-399 ◽  
Author(s):  
Anke Becker ◽  
Alfred Pühler

ABSTRACT The production of the acidic exopolysaccharide succinoglycan (EPS I) by Rhizobium meliloti exoP* mutants expressing an ExoP protein lacking its C-terminal cytoplasmic domain and by mutants characterized by specific amino acid substitutions in the proline-rich motif (RX4PX2PX4SPKX9IXGXMXGXG) located from positions 443 to 476 of the ExoP protein was analyzed. The absence of the C-terminal cytoplasmic ExoP domain (positions 484 to 786) and the substitution of both arginine443 by isoleucine443 and proline457 by serine457 within the proline-rich motif resulted in enhanced production of low-molecular-weight (LMW) EPS I at the expense of high-molecular-weight (HMW) EPS I. The ratios of HMW to LMW EPS I of the wild type and mutant strains increased with osmolarity.


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