1. Mary noticed a large, brown spot on her skin. She has been playing tennis in the sun for several years without sun protection. She reported the discovery to a friend, who told her to apply the ABCD rule to determine whether or not she had malignant melanoma. Her friend told her that if her answer was "no" to the questions that were asked by the ABCD rule, she had nothing to worry about. What is the ABCD rule and should she ignore the spot if her answers are negative? Please explain with as much detail as possible so that I have a complete understanding.
2. What is the importance of membranes in the body? What are the three types of membranes? Compare and contrast each type. What homeostatic imbalances may occur relating to membranes, and what are their implications? Please provide as much detail as possible I will have to write an essay on this questions and just want as much information as possible.
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See attached document.
ABCD is a set of initial guidelines to ...
The ABCD rules of assessing moles, as well as the importance of our bodies' membranes, is explained.
Literature Review: Cadherin-Mediated Cell-Cell Adhesion
See the attached file.
Review of the article titled "Transmembrane control of cadherin-mediated cell adhesion: a 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin." The review includes a short description of what cadherins are, what they do, and how they function with the actin-cytoskeleton, including information about the C-terminal domains. Information is provided specifically on the properties of E-cadherin. This remaining information includes a summary of experimental methods used by the authors of this study. Mutant E-cadherin ELβ20, dissociation/aggregation assay in the presence of Ca2+, immunoprecipitation of E-cadherin, and electrophoretic analysis are methods used by the authors to identify the active domain of E-cadherin.
Abstract for article:
"Cadherins are a family of transmembrane glycoproteins which play a key role in Ca(2+)-dependent cell-cell adhesion. Cytoplasmic domains of these molecules are anchored to the cell cytoskeleton and are required for cadherin function. To elucidate how the function of cadherins is controlled through their cytoplasmic domains, we deleted five different regions in the cytoplasmic domain of E-cadherin. After transfecting L cells with cDNA encoding the mutant polypeptides, we assayed aggregating activity of these transfectants; all these mutant proteins were shown to have an extracellular domain with normal Ca(2+)-sensitivity and molecular weight. Two mutant polypeptides with deletions in the carboxy half of the cytoplasmic domain, however, did not promote cell-cell adhesion and had also lost the ability to bind to the cytoskeleton, whereas the mutant molecules with deletions of other regions retained the ability to promote cell adhesion and to anchor to the cytoskeleton. Thus, the cytoplasmic domain contains a subdomain which was involved in the cell adhesion and cytoskeleton-binding functions. When E-cadherin in F9 cells or in L cells transfected with wild-type or functional mutant cadherin polypeptides was solubilized with nonionic detergents and immunoprecipitated, two additional 94 and 102 kDa components were coprecipitated. The 94 kDa component, however, was not detected in the immunoprecipitates from cells expressing the mutant cadherins which had lost the adhesive function. These results suggest that the interaction of the carboxy half of the cytoplasmic domain with the 94 kDa component regulates the cell binding function of the extracellular domain of E-cadherin."
Full text can be located at: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=361423.View Full Posting Details