Fascins are actin-binding proteins that cross-link filamentous actin into tightly packed parallel bundles. These bundles are important for the organization and morphology of an extremely diverse set of sub-cellular structures that include dynamic and stable cell-surface protrusions, stress fibres, and the specialized actin bundles of photoreceptor and stereocilia cells. In this review, we discuss the fascin gene family and its evolution, the actin-bundling activity of fascins and the molecular pathways by which it is regulated, and the role of the diverse actin/fascin structures in normal cellular processes. We discuss the mechanisms by which fascins contribute to disease pathologies, especially cancer, where fascin-1 is emerging as a novel therapeutic target in carcinoma metastasis.

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Abstract-Serum uric acid is associated with cardiovascular disease. However, the independent role of uric acid in the development of cardiovascular disease is uncertain. This study examined the cross-sectional association of serum uric acid level with microalbuminuria among 6771 subjects without diabetes or hypertension. Blood pressure was categorized as prehypertension (systolic blood pressure, 120 to 140 mm Hg or diastolic blood pressure, 80 to 90 mm Hg) and normotension (systolic blood pressure, Ͻ120 mm Hg and diastolic blood pressure, Ͻ80 mm Hg). Microalbuminuria was found in 4.0% of normotensive subjects (nϭ4819) and in 7.9% of prehypertensive subjects (nϭ1952 006).However, the difference in serum uric acid level according to the presence or absence of microalbuminuria was not found in the normotensive group. Multiple logistic regression models showed that, in the prehypertensive group, after adjustment for other cardiovascular risk factors, the highest uric acid quartile entailed Ͼ2 times greater risk for microalbuminuria than the lowest quartile in both men (odds ratio, 2.12; 95% CI, 1.16 to 3.87) and women (odds ratio, 3.36; 95% CI, 1.17 to 9.69). In the normotensive group, serum uric acid quartile did not show the independent association with microalbuminuria. In conclusion, serum uric acid level was strongly associated with microalbuminuria in prehypertensive subjects.

AKI after radical nephrectomy in patients with RCC is a potent risk factor for new-onset CKD. Prevention of post-operative AKI is essential for reducing the incidence of CKD after nephrectomy.

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Prescription of low GDP, pH-neutral PD solutions has rapidly increased in Korea. This change has resulted in a significant improvement in patient and technique survival without any measurable change in peritonitis incidence or rate. Reasons for the improved patient survival cannot be determined from this analysis and require further study.

The appropriate regulation of the actin cytoskeleton is essential for cell movement, changes in cell shape, and formation of membrane protrusions like lamellipodia and filopodia. Moreover, several regulatory proteins affecting actin dynamics have been identified in the motile regions of cells. Here, we provide evidence for the involvement of SPIN90 in the regulation of actin cytoskeleton and actin comet tail formation. SPIN90 was distributed throughout the cytoplasm in COS-7 cells, but exposing the cells to platelet-derived growth factor (PDGF) caused a redistribution of SPIN90 to the cell cortex and the formation of lamellipodia (or membrane ruffles), both of which were dramatically inhibited in SPIN90-knockdown cells. In addition, the binding of the C terminus of SPIN90 with both the Arp2/3 complex (actin-related proteins Arp 2 and Arp 3) and G-actin activates the former, leading to actin polymerization in vitro. And when coexpressed with phosphatidylinositol 4-phosphate 5 kinase, SPIN90 was observed within actin comet tails. Taken these findings suggest that SPIN90 participates in reorganization of the actin cytoskeleton and in actin-based cell motility.The actin cytoskeleton plays key roles in cell motility and morphology, intracellular organization, membrane trafficking, and the intracellular movement of a variety of pathogens (1, 2). Many actin-based structures, especially those involved in membrane protrusion, are assembled through the coordinated polymerization and cross-linking of actin monomers into actin filaments that in turn form orthogonal or parallel filament networks (3). In that regard, the dynamics of actin stress fibers, filopodia, and lamellipodia (or membrane ruffles) are tightly regulated by various nucleation-promoting factors (WASP 4 family proteins) and actin nucleation proteins (e.g. the Arp2/3 complex) (4, 5). Among these components, the Arp2/3 complex localizes at the leading edge of cells, where the actin cytoskeleton is nucleated and reorganized (6, 7). The major activators of the complex include the WASP family proteins, which contain a conserved VCA domain composed of one or two VPH domains, which bind actin monomers, a central region, and an A domain, which binds to the Arp2/3 complex (8). In addition, cortactin, a filamentous actin-associated protein, binds to the Arp2/3 complex via an A domain at its N terminus and stimulates nucleation of actin filaments, ultimately promoting formation and stabilization of actin filament networks (9). In similar fashion, Abp1, an F-actin binding protein, also associates with the Arp2/3 complex and stimulates actin nucleation (10).The Arp2/3 complex also plays a role in the intracellular motility of pathogens and vesicles. For instance, the pathogenic bacterium Listeria monocytogenes utilizes actin polymerization mediated by the Arp2/3 complex to move within the cytoplasm of infected host cells. Likewise, movement of intracellular vesicles (i.e. endosomes) is dependent upon actin polymerization mediated by the Arp2/3 complex, which localizes al...

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