Aisha
Khan
Sponsor: Enkhmaa Byambaa, M.D.,Ph.D. MED: Int Med - Endocrinology Elevated levels of circulating fat protein complexes, including lipoprotein(a) [Lp(a)], are risk factors for atherosclerotic cardiovascular disease (CVD). While plasma Lp(a) levels are primarily genetically regulated by a size variation in the apolipoprotein(a) [apo(a)] gene, chronic kidney disease (CKD) has been shown to influence Lp(a) levels. In this study, we investigated the associations between CKD, Lp(a) level, and apo(a) size in 98 individuals (n=37 control; n=58 CKD) enrolled in the Study of Glucose and Insulin in Renal Disease (SUGAR). Lp(a) concentrations were elevated in CKD [as defined by estimated glomerular filtration rate (eGFR) <60 mL/min/1.73 m2] patients vs controls across both, small and large apo(a) sizes; CKD patients with the greatest degree of kidney dysfunction (eGFR <30 mL/min/1.73 m2) had 2.5 times elevated Lp(a) levels compared with controls [median (IQR): 20 mg/dL (8; 71) vs 8 mg/dL (3; 45)]. Among CKD patients, Lp(a) levels were higher in those with CVD (n=17) vs without CVD (n=37) [median (IQR): 26 (4; 73) vs 11 (4; 43) mg/dL]. In conclusion, CKD influences Lp(a) concentrations across a range of apo(a) sizes, and elevated Lp(a) are associated with CVD in CKD. Further studies are warranted to understand the underlying mechanism of CKD-induced increase in Lp(a) levels. Characterization of Actin-Microtubule Crosstalk via the Nuclear Envelope Protein Nespirin-2
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Aisha Khan
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Nesprins are linker proteins in the outer nuclear membrane connecting the nucleoskeleton and cytoskeleton. They belong to the spectrin superfamily, wherein nesprin-2-Giant (N2G) is one of the largest members at over 800 kDa. While most of the protein is comprised of spectrin repeats, N2G also contains an N-terminal actin-binding domain and C-terminal region that binds to the microtubule motor protein kinesin-1. If and how N2G may network with the two major cytoskeletal systems in cells, actin and microtubules, remains unclear. N2G is required for normal embryonic growth, differentiation, and organogenesis, and critical roles of N2G in nuclear migration and positioning within cells have been reported. However, the molecular details of N2G's connections with the actin and microtubule cytoskeletons are largely undefined because of its large size and complicated architecture. We have reconstituted a minimal version of N2G and examined its interactions with the cytoskeleton in vitro. We have found that N2G can bind to actin and acts as a cargo-adapter protein that can activate kinesin-1 motility. N2G links kinesin to actin, allowing the motor to transport actin filaments along microtubules. These results provide insight into N2G's function to act as a mechanical crosslinker between actin and microtubules. UC Davis 34 th Annual Undergraduate Research, Scholarship and Creative Activities Conference 96 The Willow Clinic Behavioral Health Team: A Model for Reducing Mental Health Care Accessibility Barriers Su Thwe Myo Khin
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UC Davis / Molecular & Cellular Bio / 2023
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Aisha Khan