What are the policy priorities for sustaining ecological processes? A case study from Victoria,Australia

Summary Developments in ecological theory indicate that ecological processes have major implications for sustaining biodiversity and the provision of ecosystem services. Consequently, conservation actions that focus solely on particular species, vegetation communities, habitats or sites (‘assets’) are unlikely to be effective over the long term unless the ecological processes that support them continue to function. Efforts to sustain biodiversity must embrace both ‘assets’ and ‘process‐oriented’ approaches. Existing knowledge about ecological processes, incomplete though it is, has not been adequately considered in government decision making. It is, therefore, necessary to consider how to build consideration of ecological processes into legislative and institutional frameworks, policy and planning processes, and on‐ground environmental management. Drawing on insights from interviews, a facilitated workshop, and a literature review, this paper identifies a suite of policy priorities and associated reforms which should assist in ensuring that ecological processes are given more attention in policy‐making processes. It is concluded that a multi‐pronged approach is required, because there are no ‘silver bullets’ for sustaining ecological processes.     

Comparison of circulating and peritoneal leukocyte cationic proteins in release of histamine from rat mast cells

Lysosomal cationic proteins which release histamine from rat peritoneal mast cells were prepared from circulating as well as peritoneal leukocytes of rabbits. The release of histamine by cationic proteins and by compound $\text{48}\text{80}$ was compared as a function of temperature, pH and concentration. Cationic protein-mediated histamine release appears to be a non-cytotoxic energy requiring process similar to compound $\text{48}\text{80}\text{-}\text{mediated release}$. It was inhibited by iodoacetate, n-ethylmaleimide, 2,4-dinitrophenol, malonate, oxamate, glutamate and slightly inhibited by 2-deoxyglucose. Pharmacologic inhibition of release by isoproterenol, aminophylline, dibutyryl cyclic AMP and prednisone was also demonstrated.     

DIPA-family coiled-coils bind conserved isoform-specific head domain of p120-catenin family: potential roles in hydrocephalus and heterotopia

p120-catenin (p120) modulates adherens junction (AJ) dynamics by controlling the stability of classical cadherins. Among all p120 isoforms, p120-3A and p120-1A are the most prevalent. Both stabilize cadherins, but p120-3A is preferred in epithelia, whereas p120-1A takes precedence in neurons, fibroblasts, and macrophages. During epithelial-to-mesenchymal transition, E- to N-cadherin switching coincides with p120-3A to -1A alternative splicing. These isoforms differ by a 101–amino acid “head domain” comprising the p120-1A N-terminus. Although its exact role is unknown, the head domain likely mediates developmental and cancer-associated events linked to p120-1A expression (e.g., motility, invasion, metastasis). Here we identified delta-interacting protein A (DIPA) as the first head domain–specific binding partner and candidate mediator of isoform 1A activity. DIPA colocalizes with AJs in a p120-1A- but not 3A-dependent manner. Moreover, all DIPA family members (Ccdc85a, Ccdc85b/DIPA, and Ccdc85c) interact reciprocally with p120 family members (p120, δ-catenin, p0071, and ARVCF), suggesting significant functional overlap. During zebrafish neural tube development, both knockdown and overexpression of DIPA phenocopy N-cadherin mutations, an effect bearing functional ties to a reported mouse hydrocephalus phenotype associated with Ccdc85c. These studies identify a novel, highly conserved interaction between two protein families that may participate either individually or collectively in N-cadherin–mediated development.     

Identification of Early Intestinal Neoplasia Protein Biomarkers Using Laser Capture Microdissection and MALDI MS

Obtaining protein profiles from a homogeneous cell population in tissues can significantly improve our capability in protein biomarker discovery. In this study, unique protein profiles from the top and bottom sections of mouse crypts and Apc^Min+/− adenomas were obtained using laser capture microdissection (LCM) combined with MALDI MS. Statistically significant protein peaks with differential expression were selected, and a set of novel protein biomarkers were identified. Immunohistochemistry was performed to confirm the differentially expressed protein biomarkers found by LCM combined with MALDI MS. To validate the relevance of the findings in human colorectal cancer (CRC), S100A8 was further confirmed in human CRC using immunohistochemistry. In addition, S100A8 was found to have an increased expression at different human CRC stages (Duke''s A–D) compared with controls at both protein (n = 168 cases) and RNA (n = 215 cases) levels. Overall LCM combined with MALDI MS is a promising method to identify intestinal protein biomarkers from minute amounts of tissue. The novel protein biomarkers identified from the top and bottom crypts will increase our knowledge of the specific protein changes taking place during cell migration from the crypt bottom to top. In addition, the identified cancer protein biomarkers will aid in the exploration of colorectal tumorigenesis mechanisms as well as in the advancement of molecularly based diagnosis of colorectal cancer.Obtaining protein profiles from a pure cell population can significantly improve our capability in protein biomarker discovery. Laser capture microdissection (LCM)¹ is an important tool for acquisition of specific cells of interest from heterogeneous tissue sections (1,2). Obtaining protein profiles from laser-microdissected cells has been explored using multidimensional liquid chromatography-mass spectrometry or gel electrophoresis (3–5). However, usually ∼30,000 cells are required for these approaches (6–8). Direct analysis of laser-microdissected cells using MALDI MS is a sensitive, accurate, and high throughput technique to obtain protein profiles from limited numbers of cells (∼100 cells) (9–11). Combining LCM and MALDI MS is a promising tool for discovery of protein biomarkers from minute tissue structures.Individuals with advanced colorectal cancer (CRC) continue to have a poor prognosis despite recent improvements in treatment. As a result, early diagnosis and improved understanding of the pathogenesis of CRC are vital for improved clinical outcomes. Identification of early CRC protein markers has the potential to result in earlier diagnosis, more accurate prognosis, and improved treatment for individuals with CRC. Colorectal neoplasia is believed to arise from the colonic crypt (12,13). The colon is a self-renewing epithelium that consists of an actively dividing, relatively undifferentiated crypt base and a non-dividing, differentiated surface compartment (14–16). Small numbers of stem cells reside in the base of the crypt where daughter cells differentiate into absorptive cells, goblet cells, tuft cells, and endocrine cells. Absorptive cells and goblet cells, in particular, migrate to the luminal surface where they are eventually shed into the colonic lumen. Because the top and bottom crypts contain cells at different stages of differentiation, the protein profiles of these cells are likely to be different.Adenomatous polyps originate from crypts and represent important precursor lesions in the adenoma-carcinoma sequence (12). The Apc^Min+/− mouse model, and other similar models based on truncating mutations in Apc, have been widely used to study intestinal neoplasia. This model contains a germ line mutation in the adenomatous polyposis coli (Apc) gene (17), leading to numerous adenomas in the intestine (18). In humans, loss of APC is often an early event in the cascade of genetic mutations that lead to colorectal neoplasia (19). Approximately 80% of all sporadic human CRC have inactivating mutations in the APC gene (20). Similarly human familial adenomatous polyposis patients have germ line mutations in the APC gene, and loss of heterozygosity leads to the development of hundreds of adenomatous polyps in the colon and rectum. Thus, the Apc^Min+/− mouse is a promising mouse model for the discovery of potential early CRC markers using a proteomics approach.As a discovery study, we aimed to identify a set of proteomic profiles that can differentiate murine top and bottom crypts and Apc^Min+/− adenomas using LCM combined with MALDI MS. Specific protein biomarkers were identified using tandem mass spectrometry. Finally the relevance of the identified protein biomarkers was examined in human CRC at both protein and mRNA levels.     

Real-time PCR detection of Fe-type nitrile hydratase genes from environmental isolates suggests horizontal gene transfer between multiple genera

Nitriles are widespread in the environment as a result of biological and industrial activity. Nitrile hydratases catalyse the hydration of nitriles to the corresponding amide and are often associated with amidases, which catalyze the conversion of amides to the corresponding acids. Nitrile hydratases have potential as biocatalysts in bioremediation and biotransformation applications, and several successful examples demonstrate the advantages. In this work a real-time PCR assay was designed for the detection of Fe-type nitrile hydratase genes from environmental isolates purified from nitrile-enriched soils and seaweeds. Specific PCR primers were also designed for amplification and sequencing of the genes. Identical or highly homologous nitrile hydratase genes were detected from isolates of numerous genera from geographically diverse sites, as were numerous novel genes. The genes were also detected from isolates of genera not previously reported to harbour nitrile hydratases. The results provide further evidence that many bacteria have acquired the genes via horizontal gene transfer. The real-time PCR assay should prove useful in searching for nitrile hydratases that could have novel substrate specificities and therefore potential in industrial applications.