Sandbox Reserved 1454
From Proteopedia
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Abrus precatorius (or rosary peas) contain the protein abrin. Rosary peas are red and oval-shaped with a black edge towards one end. In some cultures, they are used to make beaded jewelry. Abrin can exhibit beneficial uses for medical research, but it can also be destructive if it directly enters an organism’s body because of its toxic properties. | Abrus precatorius (or rosary peas) contain the protein abrin. Rosary peas are red and oval-shaped with a black edge towards one end. In some cultures, they are used to make beaded jewelry. Abrin can exhibit beneficial uses for medical research, but it can also be destructive if it directly enters an organism’s body because of its toxic properties. | ||
== Structure == | == Structure == | ||
| - | Abrin is referred to as a ribosome-inactivating protein (RIP). The protein contains two chains: A and B which are connected by a disulfide bond. The <scene name='77/778334/Alpha_a/1'>A chain</scene> is known as an N-glycosidase allowing it modify adenine in ribosomes by deleting cyanide. This causes the ribosome to be incompetent when trying to connect to an elongation factor [3]. The B chain is composed of Ile-Val-Glu-Lys-Ser-Lys-Ile-Ser-Ser-Ser-Arg-Tyr-Glu-Pro-Thr amino acids which attach to carbohydrate receptors of the cell. With these abilities, cells are very susceptible to abrin. | + | Abrin is referred to as a ribosome-inactivating protein (RIP). The protein contains two chains: A and B which are connected by a disulfide bond. The <scene name='77/778334/Alpha_a/1'>A chain</scene> is known as an N-glycosidase allowing it modify adenine in ribosomes by deleting cyanide. This causes the ribosome to be incompetent when trying to connect to an elongation factor [3]. The <scene name='77/778334/Beta_chain/1'>B chain</scene> is composed of Ile-Val-Glu-Lys-Ser-Lys-Ile-Ser-Ser-Ser-Arg-Tyr-Glu-Pro-Thr amino acids which attach to carbohydrate receptors of the cell. With these abilities, cells are very susceptible to abrin. |
== Medical Potential == | == Medical Potential == | ||
Abrin has remained a key interest in a treatment for cancer. In one study, scientists want to see if abrin would decrease the number of colon cancer cells in vitro and vivo models. One experiment showed that purified abrin can influence cell cycle arrest and apoptosis. The study states abrin “significantly increased p21 mRNA expression and decreased PCNA, cyclin B1, Ki67 mRNA expression” [6] which induces a halt in cell growth. For example, p21 can inhibit the CDK2 which regulate the checkpoints of the cell cycle; meaning, if there is an increased level of p21, more CDK2s will be affected. It also stated that abrin can enhance Bcl-2 which causes cytochrome c to be released. With this data, the study suggested that abrin could act as an anticancer treatment for colon cancer; however, a further experiment would have to test abrin’s impact on other cells such as erythrocytes, neurons, or dendritic cells. | Abrin has remained a key interest in a treatment for cancer. In one study, scientists want to see if abrin would decrease the number of colon cancer cells in vitro and vivo models. One experiment showed that purified abrin can influence cell cycle arrest and apoptosis. The study states abrin “significantly increased p21 mRNA expression and decreased PCNA, cyclin B1, Ki67 mRNA expression” [6] which induces a halt in cell growth. For example, p21 can inhibit the CDK2 which regulate the checkpoints of the cell cycle; meaning, if there is an increased level of p21, more CDK2s will be affected. It also stated that abrin can enhance Bcl-2 which causes cytochrome c to be released. With this data, the study suggested that abrin could act as an anticancer treatment for colon cancer; however, a further experiment would have to test abrin’s impact on other cells such as erythrocytes, neurons, or dendritic cells. | ||
Revision as of 19:54, 30 April 2018
| This Sandbox is Reserved from Jan 22 through May 22, 2018 for use in the course Biochemistry II taught by Jason Telford at the Maryville University, St. Louis, Missouri, USA. This reservation includes Sandbox Reserved 1446 through Sandbox Reserved 1455. |
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Abrin
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References
1. Alhamdani, Mazin, et al. “Abrin Poisoning in an 18-Month-Old Child.” The American Journal of Case Reports, International Scientific Literature, Inc., 10 Mar. 2015, www.ncbi.nlm.nih.gov/pmc/articles/PMC4356263/.
2. “Facts About Abrin.” Centers for Disease Control and Prevention, Centers for Disease Control and Prevention, 18 Nov. 2015, emergency.cdc.gov/agent/abrin/basics/facts.asp.
3. Tam, Christina, et al. “Abrin Toxicity and Bioavailability after Temperature and PH Treatment.”MDPI, Multidisciplinary Digital Publishing Institute, 13 Oct. 2017, www.mdpi.com/2072-6651/9/10/320/htm.
4. Riedel, Stefan. “Biological Warfare and Bioterrorism: a Historical Review.” Proceedings (Baylor University. Medical Center), Baylor Health Care System, 17 Oct. 2004, www.ncbi.nlm.nih.gov/pmc/articles/PMC1200679/.
5. Wang, Junhong, et al. “A Novel Recombinant Vaccine Protecting Mice against Abrin Intoxication.” Human Vaccines & Immunotherapeutics, vol. 11, no. 6, 3 June 2015, pp. 1361–1367. US National Library of Medicine, doi:10.1080/21645515.2015.1008879.
6. Yu, Ying, et al. “Abrin P2 Suppresses Proliferation and Induces Apoptosis of Colon Cancer Cells via Mitochondrial Membrane Depolarization and Caspase Activation.” Acta Biochimica Et Biophysica Sinica, vol. 48, no. 5, 2016, pp. 420–429., doi:10.1093/abbs/gmw023.
