Subjective cognitive decline (SCD) is prevalent in the general population, particularly among Hispanic adults. SCD increases the risk of mild cognitive impairment (MCI) and dementia. While ...non-pharmacologic interventions are recommended to mitigate cognitive decline and preserve daily function in SCD and MCI, such interventions are not readily available for Spanish-speaking Hispanic adults with SCD. This pilot study, preregistered at clinicialtrials.gov, aimed to develop a linguistically and culturally appropriate adaptation of an existing memory compensation intervention, the Memory Support System (MSS), from English to Spanish, and to gather data to assess its impact in this population. Twenty Spanish-speaking Hispanic adults with SCD and 16 support partners were recruited. Measures of treatment adherence, daily function, self-efficacy for memory, quality of life, mood, anxiety, and caregiver burden were assessed at baseline, treatment end, and 8-week follow-up. By treatment end, participants with SCD improved their general functional status, daily activities requiring organizational skills, and depression and anxiety symptoms. Partners reported improvement in anxiety by treatment end and in caregiver burden at follow-up. The MSS was successfully translated into Spanish and readily learned by participants with SCD and their partners. The MSS in Spanish may help with daily functioning and aspects of patient and family well-being.
An essential aspect of undergraduate biology includes visualization of the relationship between protein structure and function. Glucokinase (GCK) is significant to glucose homeostasis. When mutated, ...GCK has been demonstrated to play a role in Type II Diabetes, leading to diminished sensitivity to insulin detection. The focus of this project was to create a molecular dynamic simulation that could be used to visualize mutations at residues L25Q, L25R, R36P, V33E, E40K, G44D, M41T, and T49N on GCK and, in turn, illustrate how amino acid substitutions alter the structure and function of GCK. Glucokinase was selected because it is a common protein demonstrated to have mutations suspected of the Type II Diabetes phenotype when screened through Clinvar, Polyphen, Provean, and SIFT. Specific residues were determined as most prevalent and classifiable as “damageable” or “pathogenic” in the impact of affected cellular function upon comparing information from the aforementioned databases. Yet Another Scientific Alternate Reality Application (YASARA) and cloud computing were used to model selected mutations to asses structural changes compared to wild type. Such research and specific use of bioinformatics is important because it has the capacity to consolidate large masses of information from multiple sources and specify the focus for groups working on treatments of particular diseases. Modelling is further useful in communication of disease and amino acid level mutations to patients as it provides visuals to compare wild type and mutated phenotypes of affected proteins. Further research could be conducted on specific perturbations caused by selected GCK variants.
This is from the Experimental Biology 2019 Meeting. There is no full text article associated with this published in The FASEB Journal.
O‐GlcNAcylase (OGA): A Sugar Cleaver Gallen, Corey; Rios‐Rosales, Anapaula; Jacus, Isabella G. ...
The FASEB journal,
April 2018, 2018-04-00, Volume:
32, Issue:
S1
Journal Article
Peer reviewed
A basic component of learning undergraduate biology concepts is grasping the interplay between carbohydrates and proteins. O‐GlcNAcylation is a post‐translational modification that covalently ...attaches O‐linked N‐acetylglocosamine (O‐GlcNAc) moieties to target proteins. Two enzymes regulate O‐GlcNAcylation; O‐GlcNAc transferase catalyzes the addition of O‐GlcNAc to specific serine and threonine residues, and O‐GlcNAcylase (OGA) hydrolyses the monosaccharide from the substrate. The focus of this project was to design and build a physical model that illustrates the key functional features of human OGA. Two isoforms of the enzyme exist in humans; 1 and 3 which are expressed in the cytoplasm and nucleus, respectively. The cytoplasmic isoform includes a full length protein, while the nuclear isoform is shorter that lacks a C‐terminal acetyltransferase‐like domain and demonstrates reduced enzymatic activity in vitro. Human OGAs possess a fugitive substrate binding groove that is highly conserved through metazoans. Two aspartic acid residues 174 and 175 comprise the catalytic activity of the enzyme and are conserved across all domains. Residues significant to binding O‐GlcNAc are close to the sugar/catalytic machinery or occupy positions shown to undergo a conformational change upon inhibitor binding. Mutations targeting the substrate binding groove identified residues that are not required for hydrolysis, but serve roles in recognition and binding of substrate. The differences between the residues required for the turnover of these substrates may reflect a change in molecular movement in OGA sites. Further elucidation of this mechanism could help advance our treatment and/or prevention of diseases like neurological disorders and diabetes.
Support or Funding Information
Funded in part by NSF‐DUE 1725940 for the CREST Project.
This is from the Experimental Biology 2018 Meeting. There is no full text article associated with this published in The FASEB Journal.
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