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Full-Text Articles in Life Sciences

In Vivo Method For Labeling And Tracking Cells In The Mammalian Limb Bud, James T. Mccarthy, Andrew Schilb, Sarah Calve Oct 2013

In Vivo Method For Labeling And Tracking Cells In The Mammalian Limb Bud, James T. Mccarthy, Andrew Schilb, Sarah Calve

The Summer Undergraduate Research Fellowship (SURF) Symposium

The extracellular matrix (ECM) is composed of many different proteins excreted by cells and is believed to play a very important role in development as well as regeneration and wound healing. In this research, a method to determine the ECM’s effect on the migration of muscle progenitor cells into the mammalian limb bud was investigated. It has traditionally been difficult to obtain in vivo images of the limb bud, due to the difficulty of maintaining embryos in culture and limitations of imaging techniques. In this study, we have worked on optimizing the culture conditions to allow growth of mouse embryos …


Developmental Characterization Of Tissue Inhibitor Of Metalloproteinase Domain Functions In Xenopus Laevis, Michelle A. Nieuwesteeg Sep 2013

Developmental Characterization Of Tissue Inhibitor Of Metalloproteinase Domain Functions In Xenopus Laevis, Michelle A. Nieuwesteeg

Electronic Thesis and Dissertation Repository

During development the extracellular matrix is cleaved and remodeled to facilitate the large-scale cell rearrangements that are necessary for processes like gastrulation, neurulation, angiogenesis and organogenesis. ECM remodeling occurs primarily through secreted enzymes called matrix metalloproteinases (MMPs). Regulation of MMP activity is achieved through the tissue inhibitor of metalloproteinases (TIMPs), a small family of secreted proteins that bind MMPs in a 1:1 manner to inhibit their activity. Although TIMPs were originally characterized based on their MMP-inhibitory activities, in vitro studies have revealed that TIMPs are multifunctional proteins, with structurally and functionally distinct N- and C-terminal domains. TIMP N-terminal domains bind …