Part:BBa_K4869004
Mus mucus (mouse) Afamin gene
General Information & Literature Review:
Mus mucus (mouse) Afamin gene was used in this study (1824 bp). Afamin, otherwise named alpha-albumin, alpha-1D-glycoprotein, vitamin E-binding protein, is a glycoprotein that is first synthesized in the liver of an organism and then secreted into the bloodstream. This gene is a member of the albumin gene family, comprising four localized genes to chromosome 4 in tandem arrangement. It also belongs to the albumin protein family while structurally similar to serum albumin.
Application in Our Project:
">Figure 1: Afamin-Wnt3a CM enhances cell proliferation and differentiation. The cell image was taken after 96 hours of incubation of four types of culture media (CM) conditions: without FBS, with 10% FBS, with 10% Afamin-Wnt3a CM, and with 20% Afamin-Wnt3a CM.
">Figure 2: Predicted Afamin-Wnt3a complex structure. Afamin in gray and Wnt3a in green.
">Figure 3: Afamin-Wnt3a CM enhances cell proliferation of the bovine muscle cells (MyoB) cell line. Prestoblue assay was used to quantify cell proliferation incubation at five incubation times: 0 hr, 24 hr, 48 hr, 72 hr, and 96 hr. The mean and standard deviation (SD) were plotted in the graph (N = 2). Mann-Whitney test was used to calculate the p-value.
Afamin proteins serve various, integral roles in human physiology. The first major function of afamin is being capable of combining and transporting vitamin E in the blood across the blood-brain barrier. Vitamin E, in this scenario, is a crucial antioxidant that acts as a protection layer from possible oxidative damage caused by free radicals; this also facilitates the immune system. Maintaining vitamin E levels ensures tissue delivery to multiple places in the body. By this function, the combination of Afamin and Wnt3a can proliferate bovine cells that contribute to the development of lab-cultured meat, as shown from the visual of cell proliferation and the subsequent graph of this data.
The previous research showed that Afamin forms a complex with Wnt3a protein. This complex helps to stabilize the Wnt3a protein and prevents its self-aggregation in the conditioned media. Therefore, as a result, the coexpression of Afamin and Wnt3a would enable the production of stable Wnt3a proteins, which enhances the Wnt3a-dependent cell proliferation signaling in bovine muscle cells.
Further, Afamin serves other physiological processes, such as regulating inflammation, modulating the immune response, and affecting insulin sensitivity. Additionally, recent studies have discovered that afamin can be used as a biomarker for ovarian and other types of cancer. The clinical-grade analysis and study of Afamin proteins lead to the conclusion that Afamin assays meet the laboratory medicine thus, comparative proteomics has identified it as a potential biomarker in the human body.
Moreover, Afamin is also related to the prevalence and development of metabolic syndrome. This was discovered through the basic knowledge that transgenic mouse data had a strong association with the aforementioned function. In our project, Afamin is integral in proliferating bovine cells when functioning with Wnt3a. As the combination of these two proteins induces signaling of various cellular systems, including intestinal stem cell growth, these two proteins create an ideal environment for bovine muscle growth and allow for bovine cell proliferation.
References:
Dieplinger, H., & Dieplinger, B. (2015). Afamin--A pleiotropic glycoprotein involved in various disease states. Clinica chimica acta; international journal of clinical chemistry, 446, 105–110. doi.org/10.1016/j.cca.2015.04.010.
Naschberger, A., Orry, A., Lechner, S., Bowler, M. W., Nurizzo, D., Novokmet, M., Keller, M. A., Oemer, G., Seppi, D., Haslbeck, M., Pansi, K., Dieplinger, H., & Rupp, B. (2017). Structural Evidence for a Role of the Multi-functional Human Glycoprotein Afamin in Wnt Transport. Structure (London, England : 1993), 25(12), 1907–1915.e5.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 1152
Illegal PstI site found at 1279 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 1152
Illegal PstI site found at 1279 - 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 426
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 1152
Illegal PstI site found at 1279 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 1152
Illegal PstI site found at 1279
Illegal NgoMIV site found at 349 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 1341
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