Challenges in the design of indicators for assessing the impact of the Scotland Rural Development Programme 2007–2013 on climate change mitigation

This paper addresses the use of impact indicators with respect to climate change in the 2007–2013 Rural Development Programme (RDP) of the European Union, with particular reference to the Scotland Rural Development Programme (SRDP). It concludes that the policy context has highlighted the need for the rural land use sector to respond to climate change but that the associated Common Monitoring and Evaluation Framework (CMEF) did not develop suitable indicators to assess the impact of SDRP measures on GHG emission mitigation. It suggests improved impact indicators based on the relationship between rural land use and greenhouse gas (GHG) emissions: first, an indicator based on net GHG emissions per holding; and a second based on net GHG emissions per unit volume of output. The paper points out the challenges in measuring land-based emissions accurately. It further proposes screening of RDP measures to ensure that climate change mitigation impacts are properly appraised. It is recognised that climate change policy in relation to rural land use is still at an early stage of development but greater sophistication of policy instrument design and evaluation will be required if the RDP is to contribute significantly to climate change policy objectives.     

Neurofilament Proteins Are Distributed in a Diminishing Proximodistal Gradient Along Rat Sciatic Nerve

Neurofilament (NF) proteins are distributed in a diminishing proximodistal gradient along rat sciatic nerve when compared with total noncollagen or other proteins in nerve. About a twofold decline of NF proteins can be detected by quantitating nerve proteins that have been separated by gel electrophoresis. A similar decrease of immunoreactivity to each NF subunit is seen in distal nerve segments when noncollagen nerve proteins are immunoblotted. Parallel decreases occur in all three NF proteins, thereby maintaining neurofilament subunit stoichiometry along the neuraxis. The same NF gradient can be detected when the NF contents in nerve branches to the gluteus and gastrocnemius muscles are compared with each other and with those in nerve segments taken from the same proximodistal levels of the parent sciatic nerve. The gradient of NF proteins increases during postnatal development and is readily detected by postnatal day 16. During the same period of development, the heavy NF subunit appears for the first time and is rapidly incorporated throughout the sciatic nerve. Hence, the NF gradient becomes manifest during the development and maturation of the adult form of the axonal cytoskeleton. The basis for the proximodistal gradient of NF proteins in peripheral nerve is presently unknown. The extent of the gradient cannot be accounted for on the basis of diminishing numbers of nerve fibers or increasing amounts of other nerve proteins, e.g., collagen, in distal nerve. An alternative interpretation is that the gradient reflects a low level of NF protein turnover during axonal transport.     

Timing of Expression of r and Its Encoding mRNAs in the Developing Cerebral Neocortex and Cerebellum of the Mouse

The expression of tau mRNA and of the corresponding encoded protein variants was studied during postnatal development in two brain regions differing in their timing of differentiation: the cerebral neocortex and the cerebellum. (a) The expression of tau mRNA was different in the two regions. Maximal contents were found at early stages in the cerebral neocortex, with a 10-fold decrease at later stages. In the cerebellum, two peaks of tau mRNA were observed soon after birth and in adulthood, with minimal values at postnatal day 6. (b) The expression of total tau proteins was similar to that of their encoding mRNAs in the cerebral neocortex, i.e., high concentrations after birth and low contents at later stages. In contrast, two peaks of tau proteins were observed in the cerebellum: the first perinatally and the second with a maximum at postnatal day 15. (c) Both in the cerebral neocortex and especially in the cerebellum, increasing concentrations of mature tau variants were expressed at late developmental stages, i.e., when total tau protein contents were decreased. In conclusion, the fluctuations in expression of tau and of its encoding mRNA seen in the cerebellum seem to reflect differences in the timing of differentiation of the various cell types, i.e., the macroneurons and the interneurons, present in this brain region. The adult tau variants appear in both the neocortex and the cerebellum only at late developmental stages, i.e., when most of the circuitry has been established, although these two regions markedly differ in their timing of differentiation.     

海洋可持续发展目标与海洋和滨海生态系统管理

海洋和海岸带可以为人类提供多种生态系统服务,保护与持续利用海洋资源以促进海洋和海岸带可持续发展已被正式纳入联合国可持续发展目标。实施海洋可持续发展目标面临几大挑战,包括如何减小陆基人类活动的影响、加强海岸带的综合管理、提高海洋资源效率、适应气候变化和提高沿海居民的人类福祉等。为应对这些挑战,需要将海洋和海岸带融合为一个大型生态系统,利用基于生态系统的管理方法,综合考虑各个部门和多种胁迫因素的累积影响,通过建立综合的海洋观测体系,合理划分海洋功能区,按照海洋环境承载力限制陆基人类活动,合理配置并有效利用海洋资源,提升海洋和海岸带生态系统的整体服务功能,从而进一步推进实施海洋可持续发展目标。     

Noncanonical Transforming Growth Factor β (TGFβ) Signaling in Cranial Neural Crest Cells Causes Tongue Muscle Developmental Defects

Microglossia is a congenital birth defect in humans and adversely impacts quality of life. In vertebrates, tongue muscle derives from the cranial mesoderm, whereas tendons and connective tissues in the craniofacial region originate from cranial neural crest (CNC) cells. Loss of transforming growth factor β (TGFβ) type II receptor in CNC cells in mice (Tgfbr2^fl/fl;Wnt1-Cre) causes microglossia due to a failure of cell-cell communication between cranial mesoderm and CNC cells during tongue development. However, it is still unclear how TGFβ signaling in CNC cells regulates the fate of mesoderm-derived myoblasts during tongue development. Here we show that activation of the cytoplasmic and nuclear tyrosine kinase 1 (ABL1) cascade in Tgfbr2^fl/fl;Wnt1-Cre mice results in a failure of CNC-derived cell differentiation followed by a disruption of TGFβ-mediated induction of growth factors and reduction of myogenic cell proliferation and differentiation activities. Among the affected growth factors, the addition of fibroblast growth factor 4 (FGF4) and neutralizing antibody for follistatin (FST; an antagonist of bone morphogenetic protein (BMP)) could most efficiently restore cell proliferation, differentiation, and organization of muscle cells in the tongue of Tgfbr2^fl/fl;Wnt1-Cre mice. Thus, our data indicate that CNC-derived fibroblasts regulate the fate of mesoderm-derived myoblasts through TGFβ-mediated regulation of FGF and BMP signaling during tongue development.     

Developmental patterns of galactosyltransferase activity in various regions of rat brain

Abstract: The developmental pattern of glycoprotein-galactosyltransferase activity was determined in the microsomal fractions of three regions of the embryonic rat brain and in parts of the visual system and the cerebellum postnatally. It could be shown that the enzyme activity was highest in the embryonic brain, where regional differences were apparent, and decreased progressively after birth. The enzyme profile in the cerebellum showed no marked postnatal changes.     

Developmental Changes in Polypeptide Composition of, and Precursor Incorporation into, Cellular and Subcellular Fractions of Rat Cerebral Cortex

Abstract: Neuronal-enriched and glial-enriched fractions from rat cerebral cortex at 2. 5, 9, 14 and 23 days postnatally, and subcellular fractions from 2, 14 and 46 day old rat were prepared. The polypeptide composition of all fractions was analysed by sodium dodecyl sulphate (SDS) polyacrylamide gel electro-phoresis and quantified by densitometry. Fifty-nine polypeptides (mol. wts., 13,200–251,000) were resolved in the cell fractions of which the majority remained unchanged throughout postnatal development. Three polypeptides (mol. wts., 102,000, 56,000, 53,700) were found to increase in amount devel-opmentally in both cellular fractions, the latter two showing a peak in relative amount on day 14 and a subsequent decline. Three polypeptides (mol. wts., 47,000, 28,200, 17,400) were found to be common to the glial-enriched fraction as well as the myelin fraction, and all showed a developmental increase. The neuronal-enriched fraction was found to be enriched in five polypeptides of which one (mol. wt., 51,900) showed a developmental increase after ten days postnatally, the others (mol. wts., 178,700, 142,000, 109,000, 24,000) showing a decrease. In vitro incorporation of [³⁵S]-methionine into the glial-enriched fraction was carried out, and a developmental decline was observed in the labelling of a polypeptide of 42,000 mol. wt.     

Nicotinamide methylation tissue distribution,developmental and neoplastic changes

The distribution of cytosolic activity of nicotinamide:S-adenosylmethionine methyltransferase (nicotinamide methylase, EC 2.1.1.1) in normal tissues from adult rat and mouse and in tumors and the change in the enzyme activity during the the development of rat tissues were studied. (1) Rat liver exhibited the highest nicotinamide methylase activity among all adult tissues tested; other rat tissues, like adrenal, pancreas, kidney, brain and mouse tissues, had only less than 15% of the adult rat liver activity. (2) 3 days before birth, fetal liver showed a very low nicotinamide methylase activity (2% of adult rat liver), which, however, increased already 1 day before birth and reached the adult level on the day 28 after birth. (3) In a variety of hepatomas and ascites tumors, an inverse correlation, with some exceptions, between tumor growth rate and nicotinamide methylase activity could be seen. In all hepatomas, with the exception of Morris hepatoma 5123tc, nicotinamide methylase activity was significantly decreased in comparison to normal adult rat liver. The highly malignant Zajdela hepatoma, Yoshida sarcoma, sarcoma 180 and Ehrlich ascites tumor methylated nicotinamide only at a negligibly low rate. (4) Cultured RLC cells (an established rat liver cell line) from the stationary growth phase or G₁-arrested RLC cells had about half of the adult rat liver activity, yet the activity was 70% higher than that of the logarithmically growing RLC cells.     

The ADP-ribosylation factor-like small GTPase FgArl1 participates in growth,pathogenicity and DON production in Fusarium graminearum

Fusarium graminearum is the main pathogen of Fusarium head blight (FHB) in wheat and related species, which causes serious production decreases and economic losses and produces toxins such as deoxynivalenol (DON), which endangers the health of humans and livestock. Vesicle transport is a basic physiological process required for cell survival in eukaryotes. Many regulators of vesicle transport are reported to be involved in the pathogenicity of fungi. In yeast and mammalian cells, the ADP-ribosylation factor-like small GTPase Arl1 and its orthologs are involved in regulating vesicular trafficking, cytoskeletal reorganization and other significant biological processes. However, the role of Arl1 in F. graminearum is not well understood. In this study, we characterized the Arl1-homologous protein FgArl1 in F. graminearum and showed that FgArl1 is located in the trans-Golgi apparatus. The deletion of FgARL1 resulted in a significant decrease in vegetative growth and pathogenicity. Further analyses of the ΔFgarl1 mutant revealed defects in the production of DON. Taken together, these results indicate that FgArl1 is important in the development and pathogenicity of F. graminearum.     

Ontogeny of ppp(A2′p)nA-binding protein in mouse brain

Mouse brain tissue extracts at various stages of development show a drastic change in the specific activity of pp(A2′p)₂A-[³²P]pCp binding protein. Identification of the ppp(A2′p)₃A-[³²P]pCp binding protein was established by (i) binding to the specific ligand ppp(A2′p)₃A-[³²P]pCp, (ii) displacement of binding by nanomolar concentration of pppA(pA)₃, and (iii) affinity labeling techniques in which periodate oxidized ppp(A2′p)₃A-[³²P]pC was specifically cross-linked to a protein with a molecular weight of 86 000. These data suggest that the ppp(A2′p)₃A-[³²P]pCp protein is closely associated with the process of cellular proliferation and differentiation.