Tingkat Kepuasan Konsumen Terhadap Pelayanan Bongkar-muat Barang Pada Terminal Peti Kemas Semarang

This study aimed to analyze the level of consumer expectations and the performance of the service and the satisfaction level of stevedoring service users at the Container Terminal of Semarang. It also analyzes the factors that have to be maintained, the main priority, and low priority of customer satisfaction. The samples are 73 respondents (companies) with the data analysis performed using the Important Performance Analysis. Based on the Cartesian diagram analysis, it is known that factors considered essential are in accordance with the reality perceived by the customer so that the satisfaction level is relatively high for the clarity of service personnel, service personnel discipline, fairness of service, and comfort environment. While the factors that are considered less important by customers and in fact not very special are service procedures, service attendant responsibilities, service speed and courtesy and hospitality workers

Comparative analysis of four medicinal floras: phylogenetic methods to identify cross-cultural patterns

Summary Four medicinal floras were compared using phylogenetic methods, to test whether there are shared patterns in medical plant use at the level of the whole medicinal floras, or for specific therapeutic applications. Checklists of the native plants and medicinal plants of Oman were compiled, and analyzed alongside existing checklists for Nepal, the Cape of South Africa and New Zealand. We reconstructed a plant phylogeny at generic level for Oman, and a new, more inclusive phylogeny to represent the genera found in all four local floras. Methods from community phylogenetics were used to identify clustering and overdispersion of the plants used. The impacts of using local or more inclusive phylogenies and different null model selections were explored. We found that Omani medicinal plant use emphasizes the same deep lineages of flowering plants as the other three medicinal floras, most strongly when comparing Omani and Nepalese medicinal plants. Drivers of this similarity might be floristic composition, opportunity for exchange of knowledge and shared beliefs in the causation of illness. Phylogenetic patterns among therapeutic applications are cross‐predictive within and between cultures, and must be interpreted with care since inappropriate use of null models can result in spurious similarity. High levels of cross‐predictivity suggest that targeting plants used for specific therapeutic applications to identify specific bioactives may have limited value. We outline the questions that might be addressed using a global phylogeny and medicinal plant checklists, suggest the best methods for future studies and propose how findings might be interpreted

Expression, Localization, and Phosphorylation of Akt1 in Benign and Malignant Thyroid Lesions

The serine/threonine protein kinase Akt is a key molecule in the phosphatidyl inositol 3-kinase pathway that is often overactivated in human cancers. Three Akt isoforms (Akt1, Akt2, Akt3) have been identified in human cells and they show different distribution and have non-redundant functions. The aim of this study was to determine whether the expression, phosphorylation, and localization of Akt1 isoform in human thyroid malignant lesions are different from those in benign lesions. Nuclear and cytoplasmic fractions were isolated from tissue samples and Western blot method was used to detect Akt1 presence in both cellular fractions. Akt1 expression was also assessed by ELISA method. To estimate Akt1 phosphorylation, kinase was immunoprecipitated from cell lysates and tested with anti-phospho-Akt antibodies. The Akt1 expression in majority of thyroid cancer samples was significantly higher than in benign lesions (p < 0.05). Akt1 both in differentiated cancers (follicular and papillary) and benign lesions was localized mainly in cytoplasmic fraction. In two of three anaplastic cancer samples Akt1 was predominantly localized in nucleus. The ratio of phosphorylated Akt1 to total Akt1 was lower in cancers than in non-neoplastic lesions and adenomas. Thus, although Akt1 seems to be overexpressed in thyroid neoplasms, its high phosphorylation is not characteristic for thyroid cancers

Characterization of a novel PTEN mutation in MDA-MB-453 breast carcinoma cell line

<p>Abstract</p> <p>Background</p> <p>Cowden Syndrome (CS) patients with germ line point mutations in the <it>PTEN </it>gene are at high risk for developing breast cancer. It is believed that cells harboring these mutant <it>PTEN </it>alleles are predisposed to malignant conversion. This article will characterize the biochemical and biological properties of a mutant PTEN protein found in a commonly used metastatic breast cancer cell line.</p> <p>Methods</p> <p>The expression of PTEN in human breast carcinoma cell lines was evaluated by Western blotting analysis. Cell line MDA-MB-453 was selected for further analysis. Mutation analysis of the <it>PTEN </it>gene was carried out using DNA isolated from MDA-MB-453. Site-directed mutagenesis was used to generate a PTEN E307K mutant cDNA and ectopic expressed in PC3, U87MG, MCF7 and <it>Pten</it>^-/-mouse embryo fibroblasts (MEFS). Histidine (His)-tagged PTEN fusion protein was generated in <it>Sf9 </it>baculovirus expression system. Lipid phosphatase and ubiquitination assays were carried out to characterize the biochemical properties of PTEN E307K mutant. The intracellular localization of PTEN E307K was determined by subcellular fractionation experiments. The ability of PTEN E307K to alter cell growth, migration and apoptosis was analyzed in multiple PTEN-null cell lines.</p> <p>Results</p> <p>We found a mutation in the <it>PTEN </it>gene at codon 307 in MDA-MB-453 cell line. The glutamate (E) to lysine (K) substitution rendered the mutant protein to migrate with a faster mobility on SDS-PAGE gels. Biochemically, the PTEN E307K mutant displayed similar lipid phosphatase and growth suppressing activities when compared to wild-type (WT) protein. However, the PTEN E307K mutant was present at higher levels in the membrane fraction and suppressed Akt activation to a greater extent than the WT protein. Additionally, the PTEN E307K mutant was polyubiquitinated to a greater extent by NEDD4-1 and displayed reduced nuclear localization. Finally, the PTEN E307K mutant failed to confer chemosensitivity to cisplatinum when re-expressed in <it>Pten</it>^-/-MEFS.</p> <p>Conclusions</p> <p>Mutation at codon 307 in PTEN C2 loop alters its subcellular distribution with greater membrane localization while being excluded from the cell nucleus. This mutation may predispose breast epithelial cells to malignant transformation. Also, tumor cells harboring this mutation may be less susceptible to the cytotoxic effects of chemotherapeutics.</p