Protein profile of MCF-7 breast cancer cell line treated with lectin delivered by CaCO3NPs revealed changes in molecular chaperones, cytoskeleton, and membrane-associated proteins
| Autor: | Amal Kh. Abbass, Rana I. Mahmood, Nurhanani Razali, Ali Z. Al-Saffar, Jameel R. Al-Obaidi |
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| Rok vydání: | 2021 |
| Předmět: |
0303 health sciences
biology Chemistry Endoplasmic reticulum 02 engineering and technology General Medicine 021001 nanoscience & nanotechnology Biochemistry Tropomyosin 03 medical and health sciences MCF-7 Structural Biology Cytoplasm Heat shock protein Chaperone (protein) Unfolded protein response biology.protein 0210 nano-technology Molecular Biology Annexin A2 030304 developmental biology |
| Zdroj: | International Journal of Biological Macromolecules. 184:636-647 |
| ISSN: | 0141-8130 |
| Popis: | The second most predominant cancer in the world and the first among women is breast cancer. We aimed to study the protein abundance profiles induced by lectin purified from the Agaricus bisporus mushroom (ABL) and conjugated with CaCO3NPs in the MCF-7 breast cancer cell line. Two-dimensional electrophoresis (2-DE) and orbitrap mass spectrometry techniques were used to reveal the protein abundance pattern induced by lectin. Flow cytometric analysis showed the accumulation of ABL-CaCO3NPs treated cells in the G1 phase than the positive control. Thirteen proteins were found different in their abundance in breast cancer cells after 24 h exposure to lectin conjugated with CaCO3NPs. Most of the identified proteins were showing a low abundance in ABL-CaCO3NPs treated cells in comparison to the positive and negative controls, including V-set and immunoglobulin domain, serum albumin, actin cytoplasmic 1, triosephosphate isomerase, tropomyosin alpha-4 chain, and endoplasmic reticulum chaperone BiP. Hornerin, tropomyosin alpha-1 chain, annexin A2, and protein disulfide-isomerase were up-regulated in comparison to the positive. Bioinformatic analyses revealed the regulation changes of these proteins mainly affected the pathways of ‘Bcl-2-associated athanogene 2 signalling pathway’, ‘Unfolded protein response’, ‘Caveolar-mediated endocytosis signalling’, ‘Clathrin-mediated endocytosis signalling’, ‘Calcium signalling’ and ‘Sucrose degradation V’, which are associated with breast cancer. We concluded that lectin altered the abundance in molecular chaperones/heat shock proteins, cytoskeletal, and metabolic proteins. Additionally, lectin induced a low abundance of MCF-7 cancer cell proteins in comparison to the positive and negative controls, including; V-set and immunoglobulin domain, serum albumin, actin cytoplasmic 1, triosephosphate isomerase, tropomyosin alpha-4 chain, and endoplasmic reticulum chaperone BiP. |
| Databáze: | OpenAIRE |
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