9-amino acid cyclic peptide-decorated sorafenib polymeric nanoparticles for the efficient in vitro nursing care analysis of hepatocellular carcinoma

2021 ◽  
Vol 100 ◽  
pp. 140-148
Author(s):  
Yue Hu ◽  
Dan Yu ◽  
Xiaoxia Zhang
Keyword(s):  
Hepatocellular Carcinoma ◽  
Amino Acid ◽  
Nursing Care ◽  
Cyclic Peptide ◽  
Polymeric Nanoparticles

scholarly journals In vitro display evolution of the PURE system-expressed TNFα-binding unnatural cyclic peptide containing an N-methyl-d-amino acid

2021 ◽  
Vol 534 ◽  
pp. 519-525 ◽  
Author(s):  
Keita Tsukamoto ◽  
Takehiro Ando ◽  
Daisuke Fuji ◽  
Takumi Yokoyama ◽  
Yukio Takamori ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cyclic Peptide ◽  
Pure System

scholarly journals An Engineered Arginase FC Protein Inhibits Tumor GrowthIn VitroandIn Vivo

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Lihua Li ◽  
Yan Wang ◽  
Jun Chen ◽  
Bi Cheng ◽  
Jiehua Hu ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Cell Proliferation ◽  
Amino Acid ◽  
Fusion Protein ◽  
Genetically Engineered ◽  
Arginine Deiminase ◽  
Cellular Migration ◽  
Fc Fusion Protein

Arginine is a semiessential amino acid required for the growth of melanoma and hepatocellular carcinoma, and the enzymatic removal of arginine by pegylated arginine deiminase (ADI) or arginase is being tested clinically. Here, we report a genetically engineered arginase FC fusion protein exhibiting a prolonged half-life and enhanced efficacy. The use of this enzyme to treat different tumor lines both inhibited cell proliferation and impaired cellular migrationin vitroandin vivo. Our data reinforce the hypothesis that nutritional depletion is a key strategy for cancer treatment.

scholarly journals Selective Targeting of αvβ5 Integrin in HepG2 Cell Line by RGDechi15D Peptide

Molecules ◽  
2020 ◽  
Vol 25 (18) ◽  
pp. 4298
Author(s):  
Domenica Capasso ◽  
Annarita Del Gatto ◽  
Daniela Comegna ◽  
Luigi Russo ◽  
Roberto Fattorusso ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Cell Proliferation ◽  
Cyclic Peptide ◽  
Pi3k Pathway ◽  
Physiological Processes ◽  
Tumor Dissemination ◽  
Selective Targeting ◽  
Vitro Model ◽  
Adhesion And Invasion

Recently, the research community has become increasingly concerned with the receptor αvβ5, a member of the well-known integrin family. Different ongoing studies have evidenced that αvβ5 integrin regulates not only physiological processes but also a wide array of pathological events, suggesting the receptor as a valuable biomarker to specifically target for therapeutic/diagnostic purposes. Remarkably, in some tumors the involvement of the receptor in cell proliferation, tumor dissemination and angiogenesis is well-documented. In this scenario, the availability of a selective αvβ5 antagonist without ‘off-target’ protein effects may improve survival rate in patients with highly aggressive tumors, such as hepatocellular carcinoma. We recently reported a cyclic peptide, RGDechi15D, obtained by structure-activity studies. To our knowledge it represents the first peptide-based molecule reported in the literature able to specifically bind αvβ5 integrin and not cross react with αvβ3. Here we demonstrated the ability of the peptide to diminish both adhesion and invasion of HepG2 cells, an in vitro model system for hepatocellular carcinoma, to reduce the cell proliferation through an apoptotic process, and to interfere with the PI3K pathway. The peptide, also decreases the formation of new vessels in endothelial cells. Taken together these results indicate that the peptide can be considered a promising molecule with properties suited to be assessed in the future for its validation as a selective therapeutic/diagnostic weapon in hepatocarcinoma.

Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

1986 ◽  
Vol 44 ◽  
pp. 134-135
Author(s):  
A. J. Tousimis
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Epithelial Cells ◽  
Elemental Composition ◽  
Isotope Labeling ◽  
Structural Components ◽  
X Ray ◽  
Human Small Intestine ◽  
Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

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