An analytical approach to evaluate point cloud registration error utilizing targets

Point cloud registration is essential for processing terrestrial laser scanning (TLS) point cloud datasets. The registration precision directly influences and determines the practical usefulness of TLS surveys. However, in terms of target based registration, analytical point cloud registration error models employed by scanner manufactures are only suitable to evaluate target registration error, rather than point cloud registration error. This paper proposes an new analytical approach called the registration error (RE) model to directly evaluate point cloud registration error. We verify the proposed model by comparing RE and root mean square error (RMSE) for all points in three point clouds that are approximately equivalent

Tumor Suppressor Spred2 Interaction with LC3 Promotes Autophagosome Maturation and Induces Autophagy-Dependent Cell Death

The tumor suppressor Spred2 (Sprouty-related EVH1 domain-2) induces cell death in a variety of cancers. However, the underlying mechanism remains to be elucidated. Here we show that Spred2 induces caspase-independent but autophagy-dependent cell death in human cervical carcinoma HeLa and lung cancer A549 cells. We demonstrate that ectopic Spred2 increased both the conversion of microtubule-associated protein 1 light chain 3 (LC3), GFP-LC3 puncta formation and p62/SQSTM1 degradation in A549 and HeLa cells. Conversely, knockdown of Spred2 in tumor cells inhibited upregulation of autophagosome maturation induced by the autophagy inducer Rapamycin, which could be reversed by the rescue Spred2. These data suggest that Spred2 promotes autophagy in tumor cells. Mechanistically, Spred2 co-localized and interacted with LC3 via the LC3-interacting region (LIR) motifs in its SPR domain. Mutations in the LIR motifs or deletion of the SPR domain impaired Spred2-mediated autophagosome maturation and tumor cell death, indicating that functional LIR is required for Spred2 to trigger tumor cell death. Additionally, Spred2 interacted and co-localized with p62/SQSTM1 through its SPR domain. Furthermore, the co-localization of Spred2, p62 and LAMP2 in HeLa cells indicates that p62 may be involved in Spred2-mediated autophagosome maturation. Inhibition of autophagy using the lysosomal inhibitor chloroquine, reduced Spred2-mediated HeLa cell death. Silencing the expression of autophagy-related genes ATG5, LC3 or p62 in HeLa and A549 cells gave similar results, suggesting that autophagy is required for Spred2-induced tumor cell death. Collectively, these data indicate that Spred2 induces tumor cell death in an autophagy-dependent manner

Low Serum Magnesium Level Is Associated with Microalbuminuria in Chinese Diabetic Patients

Whether serum magnesium deficiency is independently associated with the prevalence of microalbuminuria is still unclear. The objective of the present study was to elucidate the association between serum magnesium and microalbuminuria in diabetic patients. A cross-sectional study was conducted in 1829 diabetic subjects (aged ≥ 40 years) from Shanghai, China. Subjects were divided into three groups according to serum magnesium tertiles. A first-voided early-morning spot urine sample was obtained for urinary albumin-creatinine ratio (UACR) measurement. Microalbuminuria was defined as 30 mg/g ≤ UACR < 300 mg/g. Overall, 208 (11.37%) of the study population had microalbuminuria, with similar proportions in both genders (). The prevalence of microalbuminuria in tertile 1 of serum magnesium was higher than the prevalence in tertile 2 and tertile 3 (15.98%, 9.72%, and 8.46%, resp.; for trend <0.0001). After adjustment for age, sex, BMI, blood pressure, lipidaemic profile, HbA1c, eGFR, history of cardiovascular disease, HOMA-IR, antihypertensive and antidiabetic medication, and diabetes duration, we found that, compared with the subjects in tertile 3 of serum magnesium, those in tertile 1 had 1.85 times more likeliness to have microalbuminuria. We concluded that low serum magnesium level was significantly associated with the prevalence of microalbuminuria in middle-aged and elderly Chinese

PP1A-Mediated Dephosphorylation Positively Regulates YAP2 Activity

Background: The Hippo/MST1 signaling pathway plays an important role in the regulation of cell proliferation and apoptosis. As a major downstream target of the Hippo/MST1 pathway, YAP2 (Yes-associated protein 2) functions as a transcriptional cofactor that has been implicated in many biological processes, including organ size control and cancer development. MST1/Lats kinase inhibits YAP2’s nuclear accumulation and transcriptional activity through inducing the phosphorylation at serine 127 and the sequential association with 14-3-3 proteins. However, the dephosphorylation of YAP2 is not fully appreciated. Methodology/Principal Findings: In the present study, we demonstrate that PP1A (catalytic subunit of protein phosphatase-1) interacts with and dephosphorylates YAP2 in vitro and in vivo, and PP1A-mediated dephosphorylation induces the nuclear accumulation and transcriptional activation of YAP2. Inhibition of PP1 by okadiac acid (OA) increases the phosphorylation at serine 127 and cytoplasmic translocation of YAP2 proteins, thereby mitigating its transcription activity. PP1A expression enhances YAP2’s pro-survival capability and YAP2 knockdown sensitizes ovarian cancer cells to cisplatin treatment. Conclusions/Significance: Our findings define a novel molecular mechanism that YAP2 is positively regulated by PP1mediate