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Similarities and differences between the two cohorts

Create a list of five people that you know that use social media at least 2 or more hours per day. This group of people will make up your first cohort. Then create a list of five people that you know that either do not use social media or use it very rarely. Take into account age when creating the cohorts, and try to keep the ages as similar as possible between the cohorts. Keeping a certain level of consistency in the two cohorts will help to negate the potential effects of generational differences. Provide a brief description of each of the ten people you are going to interview divided into their respective cohorts.

In other words, list the five people in the social media at least 2 or more hours a day, and provide a brief description of each along with why you chose them. Then provide a list of the five people that rarely or never use social media, and provide a brief description of each along with why you chose them.

Interview the participants to learn the similarities and differences between the two cohorts as it relates to attitudes, lifestyles, and relationships. Write a two-page paper comparing and contrasting what you learned about the two cohorts.

Sample Solution

eurofilament mRNAs are selectively reduced in diabetic rats and alterations on post-translational modification of NF proteins have been detected. A reduction of myelinated fiber size is correlated with axonal NFs loss in peripheral nerves of STZ-induced diabetic rats (25, 26), and mRNAs levels encoding for NF-L and NF-H are reduced in the same animal model of diabetes (7). Moreover, changes on the expression of several NF-associated protein kinases isoforms may also contribute to diabetes-induced changes (4). Several protein kinases regulate NF phosphorylation status, being NFs hyperphosphorylation a hallmark of several neurodegenerative diseases. Abnormal NF phosphorylation has been described in sensory neurons of animal models of type 1 diabetes (27). Moreover, in the spinal cord of diabetic rats there is increased phosphorylation of NF-H, (28). Additionally, changes on the activity of Cdk5 and GSK-3β kinases have been described to alter the phosphorylation status of NFs in an animal model of type 1 diabetes. Specifically, in dorsal root ganglion neuronsincreased phosphorylation of GSK-3β correlated linearly with increased phosphorylation of NF-H, while decreasing activity of Cdk5 is associated with reduced phosphorylation of NF-M, which may result in progressive deficits of axonal function (29). Microfilaments Microfilaments (or actin filaments) are the thinnest filaments of the cytoskeleton, having 6 nm in diameter, providing both stability and dynamics to neurons. In neurons, actin filaments are packed into networks and stabilized by interacting proteins (22). Microfilaments play a role in spine formation and spine volume stabilization (30), with the dynamics of actin leading to the formation of new synapses as well as increased cell communication. The actin cytoskeleton controls several cellular processes. In animal models of diabetes there is an impairment of slow axonal transport of cytoskeletal elements like tubulin and NF proteins (slow component a), and polypeptides such as actin (slow component b) (31-33). Actin undergoes glycation in the brain of STZ-induced diabetic rats and the appearance of glycated actin is prevented by administration of insulin (9, 34). More recently, it was investigated if the receptor for advanced glycation end-product (RAGE) is involved in axonal transport impairment via interaction with its cytoplasmic domain binding partner mDia1, which is involved in actin structure modifications. Slow axonal transport in the peripheral nerves is indeed affected by diabetes, but in a RAGE-independent manner (35). Moreover, mDia1 axonal transport is impaired, suggesting that diabetes-induced changes affecting actin binding proteins are early events in the course of the pathology (35), and forward the hypothesis that mDia1 axonal transport impairment might be correlated with the extent of actin glycation (34).

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