ABSTRACT
Marine protected areas (MPAs) are a primary policy instrument for managing and protecting coral reefs. Successful MPAs ultimately depend on knowledge-based decision making, where scientific research is integrated into management actions. Fourteen coral reef MPA managers and sixteen academics from eleven research, state and federal government institutions each outlined at least five pertinent research needs for improving the management of MPAs situated in Australian coral reefs. From this list of 173 key questions, we asked members of each group to rank questions in order of urgency, redundancy and importance, which allowed us to explore the extent of perceptional mismatch and overlap among the two groups. Our results suggest the mismatch among MPA managers and academics is small, with no significant difference among the groups in terms of their respective research interests, or the type of questions they pose. However, managers prioritised spatial management and monitoring as research themes, whilst academics identified climate change, resilience, spatial management, fishing and connectivity as the most important topics. Ranking of the posed questions by the two groups was also similar, although managers were less confident about the achievability of the posed research questions and whether questions represented a knowledge gap. We conclude that improved collaboration and knowledge transfer among management and academic groups can be used to achieve similar objectives and enhance the knowledge-based management of MPAs.
Subject(s)
Conservation of Natural Resources , Coral Reefs , Academies and Institutes , Australia , Government , ResearchABSTRACT
The AP-2 family of transcription factors consists of three known members, namely AP-2alpha, AP-2beta, and AP-2gamma. In experimental systems AP-2 factors possess tumor suppressor-like activities, and alterations in the AP-2 expression pattern have been described for some tumor entities. In addition, AP-2 has been implicated in the transcriptional control of human papillomaviruses (HPVs). We investigated here the expression pattern of AP-2alpha, AP-2beta, and AP-2gamma, as well as that of the cellular AP-2 target gene c-erbB-2, in a series of cervical cancer cell lines. In addition, we analyzed the influence of AP-2 factors on the activity of the HPV16 and HPV18 E6/E7 oncogene promoter. We found that, with the exception of HPV-negative C33A cells, all investigated cervical cancer cell lines expressed all three AP-2 family members, although at varying levels. No linear correlation between AP-2 and c-erbB-2 levels was observed. Although AP-2alpha, AP-2beta, and AP-2gamma can activate the c-erbB-2 promoter in reporter gene assays, they do not stimulate the HPV16 or HPV18 E6/E7 promoter. These results indicate that, although a rare event, loss of AP-2 expression occurs in cervical cancer cells. Moreover, AP-2alpha, AP-2beta, and AP-2gamma are neither sufficient nor required to activate the viral E6/E7 promoter.
Subject(s)
DNA-Binding Proteins/metabolism , Gene Expression Regulation, Neoplastic/genetics , Gene Expression Regulation, Viral/genetics , Oncogenes/genetics , Papillomaviridae/genetics , Transcription Factors/metabolism , Uterine Cervical Neoplasms/genetics , Uterine Cervical Neoplasms/virology , Antibody Specificity , Blotting, Western , Cell Line , DNA-Binding Proteins/genetics , DNA-Binding Proteins/immunology , Female , Genes, Viral/genetics , Genes, erbB-2/genetics , Genetic Vectors , HeLa Cells , Humans , Mutation/genetics , Promoter Regions, Genetic/genetics , Transcription Factor AP-2 , Transcription Factors/genetics , Transcription Factors/immunology , Transcription, Genetic/genetics , Transfection , Tumor Cells, CulturedABSTRACT
CAM 17.1-Ab is a recently described monoclonal antibody that detects a mucus glycoprotein with high specificity for intestinal mucus, particularly in the colon, small intestine, biliary tract and pancreas. We investigated the expression and release of CAM 17.1 in pancreatic carcinoma cell lines and tissue specimens of normal pancreas, chronic pancreatitis and pancreatic cancer. CAM 17.1 was weakly expressed on normal ductal cells and chronic pancreatitis, whereas it was overexpressed in pancreatic cancer. Serum analysis using a new enzyme-linked antibody sandwich assay (CAM 17.1/WGA) of patients with chronic pancreatitis, pancreatic cancer or other gastrointestinal cancer and of healthy blood donors revealed a high sensitivity (67%) and excellent specificity (90%) of CAM 17.1/WGA assay in pancreatic cancer. In comparison with the tumour marker CA19-9, the sensitivity of the CAM 17.1/WGA assay was similar to the sensitivity of CA 19-9 (67% and 76%, P = 0.22), whereas the specificity of CAM 17.1/WGA assay was higher than in CA 19-9 (90% compared with 78% in chronic pancreatitis, P > 0.05).
Subject(s)
Biomarkers, Tumor/analysis , Carcinoma/diagnosis , Pancreatic Neoplasms/diagnosis , Adult , Aged , Antibodies, Monoclonal/analysis , Antibodies, Monoclonal/blood , Biomarkers, Tumor/blood , Carcinoma/chemistry , Carcinoma/metabolism , Female , Flow Cytometry/methods , Humans , Immunohistochemistry/methods , Male , Middle Aged , Neoplasm Staging , Pancreas/chemistry , Pancreas/metabolism , Pancreas/pathology , Pancreatic Diseases/metabolism , Pancreatic Diseases/pathology , Pancreatic Neoplasms/chemistry , Pancreatic Neoplasms/metabolism , Pancreatitis/metabolism , Pancreatitis/pathology , Sensitivity and Specificity , Survival Analysis , Tumor Cells, CulturedABSTRACT
The distribution of [3H]taurocholate between albumin and the lipoproteins of serum of patients with various diseases in which lipoprotein metabolism and/or bile salt concentrations were altered and of healthy control subjects was investigated by means of the density gradient centrifugation method. 1. In control sera, bile salts distribute mainly between albumin and high-density lipoprotein. An amount of 19.7 +/- 3.6% (mean +/- S.D., n = 6) of the total serum bile salts was found in the high-density lipoprotein fraction of the density gradient. 2. In sera of nonicteric patients, the distribution pattern of [3H]taurocholate in the fractions of the density gradient showed no essential differences to normal serum. The relative amounts of taurocholate in the albumin-containing fractions and the high-density lipoprotein fractions were dependent on the concentrations of albumin and high-density lipoprotein. 3. In sera of deeply jaundiced patients, the distribution pattern of [3H]taurocholate showed two distinct peaks in the high-density lipoprotein density range, one of which codistributed with high-density lipoprotein2 and the other with a high-density fraction of high-density lipoprotein3 in the density range of 1.19 to 1.23 gm per ml. The distribution of [3H]taurocholate between albumin and high-density lipoprotein was markedly shifted toward high-density lipoprotein. No [3H]taurocholate association with lipoprotein X was observed. 4. Bilirubin was found to cause a shift of taurocholate from albumin to high-density lipoprotein in vitro. It is proposed that bilirubin is responsible, at least in part, for the observed shift in icteric sera.