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Past research has shown that ecdysone signaling cascades are required for fat body remodeling. During the second pulse of 20E, the most active form of ecdysone, both E93 and MMP2 are expressed. In my research I examine E93 loss-of-function mutants and wild type for expression of MMP2 transcripts in fat body to test the hypothesis that E93 regulates transcription levels of MMP2 during fat body remodeling in Drosophila melanogaster.
Tissue remodeling is involved in multiple functions in the animal body, as the process through which cells dissociate and detach from each other. Tissue remodeling is the driving force behind wound healing and cancer metastasis, and is carried out partially by Matrix Metalloproteinases (MMPs). MMPs are proteases that degrade the extracellular matrix (ECM) between cells, which then allows them to move freely from one another. The expression of Mmps is highly regulated. To study Mmp regulation and tissue remodeling, Drosophila melanogaster makes for a highly useful model organism due to a process called larval fat body remodeling. Larval fat body remodeling occurs when Drosophila go from larva to adult fly, a highly regulated process thought to involve Matrix Metalloproteinase 2 (MMP2). MMP2 is believed to be the mechanism of ECM fat cell cleaving, which allows for cells to detach from each other and move around freely during larval fat body remodeling. Research suggests that the expression of Mmp2 in Drosophila is 20-hydroxyecdysone (ecdysone) hormonal cascade regulated, mediated by ßFTZ-F1 (Bond et al., 2011). Bond et al. (2011) showed that both ßftz-f1 and Mmp2 are necessary and sufficient for larval fat body remodeling in Drosophila. The hypothesis of this study is that Mmp2 is a downstream target of ßFTZ-F1 in the ecdysone hormonal cascade, more specifically that Mmp2 expression is induced by ßFTZ-F1. Levels of Mmp2 expression were relatively quantified compared to a control gene, in wild type Drosophila and transgenic Drosophila in which expression of ßftz-f1 was reduced in the larval fat body. To fully sustain my hypothesis, I expect to see reduced expression of Mmp2 in ßftz-f1 reduced larval fat body compared to wild type larval fat body. This is because if expression of Mmp2 is induced by ßftz-f1 expression, by reducing ßftz-f1 it comes that there will be a reduction of Mmp2 expression as well. The findings of this study show a reduction of Mmp2 at 10 hours after puparium formation (APF) in ßftz-f1 reduced larval fat body, which is consistent with the hypothesis. At 8 and 12 hours APF, the study found increased expression of , which does not support the hypothesis, however it might be explained by individual variances in biological samples, as well as a quickly shifting level of Mmp2 expression at these time points. Future studies using the Western blot technique might serve as a tool to more precisely study expression levels at these time points.
Matrix metalloproteinases are enzymes involved in important tissue remodeling mechanisms in many animal systems, including mammalian. They are required for scar resorption during wound healing, and are believed to also influence inflammation and re-epithelialization. MMPs work by loosening ECM contacts between cells at the wound edge, allowing uninjured cells behind the edge to proliferate and cover the damaged tissue (Gill and Parks, 2008). The proteases also take part in metastatic activity of tumor cells because they degrade the ECM of tumor cells, allowing them to detach and migrate to other parts of the body (Sato et al, 2005). In Drosophila, Matrix metalloproteinase 2 (MMP2) plays a vital role in tissue remodeling and programmed cell-death during metamorphosis (Page-McCaw, 2008). The larval fat body of Drosophila develops in the larva during the beginning stages of its life. This organ stores nutrients that power the animal through the non-feeding periods of its life, including metamorphosis. Metamorphosis is triggered by a pulse of 20-hydroxyecdysone (20E), which induces pupariation. 20E controls expression of dBlimp-1, a rapidly degrading protein that transcriptionally represses ßftz-f1. As the 20E titer declines, dBlimp-1 is degraded and the ßFTZ-F1 transcription factor is expressed (Agawa et al., 2007). ßFTZ-F1 functions as a nuclear receptor and confers competence upon tissues to be able to respond to a second pulse of 20E. MMP2 is expressed during the second pulse of 20E, and cleaves proteins in the ECM, enabling fat body cells to migrate. This second pulse induces the prepupal to pupal transition (Woodard et al., 1994). It has been shown that ßftz-f1 is necessary and sufficient to induce fat body remodeling in the presence of 20E. Without MMP2, the larval fat body fails to dissociate, and the transition does not occur normally (Bond, 2011). I am examining the regulation of MMP2 expression in larval fat body remodeling in D. melanogaster. I am testing the hypothesis that ßftz-f1 is necessary for the induction of MMP2 transcription by 20E in the late prepupa. I used transgenic flies to overexpress dBlimp-1 in the larval fat body, and examined the expression of MMP2 in the transgenic fat body compared to controls.
In wild-type animals, E93 is expressed in the fat body at 12 hours after puparium formation (APF), coinciding with the last stage of fat body remodeling, detachment, during which individual fat cells are redistributed into the head capsule and body cavity. E93 is known to regulate various tissue specific developmental changes such as programmed cell death of larval salivary glands and the midgut. Given E93's role in triggering the death of larval tissue, it is interesting that it does not trigger the death of fat tissue. However, considering the numerous roles E93 takes on during development, it is possible that E93 might also be involved in influencing fat body remodeling. Microscopy work utilizing light microscopy, fluorescence microscopy, transmission electron microscopy, scanning electron microscopy, and confocal microscopy reveals phenotypic differences between the wild-type and E93 mutant fat body after 12 hours APF. While wild-type fat body dissociates into individual and spherical fat cells, E93 mutant fat body is frequently found as aggregates of undetached fat cells and some individual, dissociated fat cells. I hypothesize that E93 may play a role in facilitating the detachment phase of fat tissue remodeling and that its absence would hinder proper fat body remodeling.
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