Abstract. Two mAbs that are specific for heparan sulfate-related epitopes have been raised and used to analyze the cellular and tissular distribution of this glycosaminoglycan during development, mAb 10E4 reacts with an epitope that occurs in native heparan sulfate chains and that is destroyed by N-desulfation of the glycosaminoglycan. The antibody does not react with hyaluronate, chondroitin sulfate, or DNA, and reacts only poorly with heparin. The reactivity of proteoglycan extracts or tissue sections with the 10E4 antibody is completely abolished by heparitinase, but is only partially affected by heparinase, mAb 3G10, in contrast, reacts only with heparitinase-treated heparan sulfate chains, proteoglycans, or tissue sections. The 3G10 epitope is destroyed by treatment with mercuric acetate, which indicates that the desaturated uronate generated by the lyase is essential for the reactivity of the antibody. The 3G10 epitope is not generated by treating heparan sulfate proteoglycans with heparinase or chondroitin sulfate proteoglycans with chondroitin sulfate lyases, which indicates that the 3G10 antibody recognizes desaturated uronates that occur in specific structural contexts. The antibody 10E4 and, after heparitinase treatment, the antibody 3G10 decorate the surfaces of many cell types and the extracellular matrix in proximity of the cells, in particular, the basement membranes. The analysis of embryonic and adult tissues reveals important temporal and regional differences in the abundance of the 10E4 and 3G10 epitopes at these sites. Moreover, the staining pattern of the two antibodies is not always superimposable, which is indicative of regional differences in the exposure or structure of the tissular heparan sulfates. As a whole the results suggest that heparan sulfate abounds at sites of active morphogenesis and that the expression of this glycosaminoglycan is developmentally regulated.

Heparan sulfate accumulates on cell surfaces and at cell-matriK interfaces, and functionally modulates several of the effector molecules that support the interactions, growth, and differentiation of developing tissues. Using heparan sulfatespecific monoclonal antibodies MAb, we obtained evidence that extracts from rodent embryos contain multiple forms of cell surface-associated heparan sulfate proteoglycan (PG).Taking tooth development in the mouse embryo as a model to further investigate the relevance of this PG redundancy and using MAb against heparan sulfate, antibodies specific for syndecan (syndecan-1) andfibroglycan (syndecan-2) (two distinct members of a larger family of cell-surface heparan

The embryonic and postembryonic developmental toxicity of imidazolium-based ionic liquids (ILs) to the snail Physa acuta was evaluated in this study. The results of embryonic toxicity tests showed that lower concentrations of 1-octyl-3-methylimidazolium bromide ([C8 mim]Br) (1.5 and 2.1 mg/L) inhibited the hatching rate of snail embryos, and partial snails hatched normally and died, while all of the treated embryos died when the exposure concentration was higher than 4.16 mg/L, at which IL caused the deformation, death, and decay of snail embryos. Statistical analyses revealed obvious differences in the hatching rates between three developmental stages in the 2.1 and 2.94 mg/L groups, indicating that the veliger stage is more sensitive to [C8 mim]Br exposure than the blastula and gastrula stages. Furthermore, the 96 h LC50 values of [C8 mim]Br on the tested snails at three developmental stages (juvenile, subadult, and adult) were 70.83 ± 2.99, 97.59 ± 4.05, and 109.3 ± 2.22 mg/L, respectively, indicating that young snails were more sensitive to [C8 mim]Br toxicity than adults. In addition, the 96 h LC50 values of ILs with different alkyl chain lengths, that is, [C12 mim], [C10 mim], [C8 mim], and [C6 mim], in adult snails were 1.35 ± 0.24, 8.96 ± 5.66, 109.3 ± 4, and 359.6 ± 11.6 mg/L, respectively, suggesting that longer alkyl chains can increase the toxicity of imidazolium ILs on snails.

Fibroglycan (syndecan-2) is a member of a family of cell surface heparan sulfate proteoglycans that interact with adhesion molecules, growth factors and a variety of other effector systems that support the shaping, maintenance and repair of an organism. To investigate this apparent redundancy of proteoglycans at the cell surface, we have studied the expression of fibroglycan in the mouse embryo and compared this expression with that of syndecan-1. The characterisation of mouse embryo cDNA clones that crosshybridized to human fibroglycan-cDNA predicted that murine and human fibroglycan were highly similar in structure. Consistently, the analysis of transfectant cells, murine cell lines and embryo extracts indicated that the murine proteoglycan reacted specifically with monoclonal antibody 10H4 developed against the human protein. Fibroglycan, as detected by monoclonal antibody 10H4 in sections of embryonic tissues, occurred exclusively on mesenchymal cells that represented the putative precursors of the hard and connective tissue cells. No fibroglycan was detected in epithelia or in muscle cells. Areas where fibroglycan was particularly abundant were sites of high morphogenetic activity where intense cell-cell and cell-matrix interactions are known to occur (e.g. the epithelial-mesenchymal interfaces, the prechondrogenic and preosteogenic mesenchymal condensations). The expression of fibroglycan was weak in the early embryo, culminated during the morphogenetic phase and at the moment of cell lineage differentiation, and persisted in the perichondrium, periosteum and connective tissue cells. Syndecan-1, in contrast, was primarily detected in epithelia, and transiently in some mesenchymal cells, with mesenchymal localisations that did not or only partially overlap with those of fibroglycan. In situ hybridization analyses confirmed these expression patterns at the transcriptional level, identifying mesenchymal cells as the major source of fibroglycan production. These data indicate that the expression of fibroglycan occurs along unique and developmentally regulated patterns, and suggest that fibroglycan and syndecan-1 may have distinctive functions during tissue morphogenesis and differentiation.

This article uses WebGIS technology to achieve the design and implementation of sports fitness service platform. This article includes five parts which are overview, the design goal of WebGIS sports fitness service platform, the data preparation, system implementation, and conclusion. This article emphasizes data preparation and system implementation. The construction of sports fitness service platform based on WebGIS, can fully integrate sports venues resources, promote scientific exercise methods, strengthen the consciousness of citizen scientific exercise and improve the level of public health.