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Calcium Ion Concentration (calcium + ion_concentration)
Selected AbstractsFactors affecting proliferation and differentiation of lepidopteran midgut stem cells,ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY (ELECTRONIC), Issue 1 2010Marcia J. Loeb Midgut stem cells of last instar larvae and pupae of Heliothis virescens, Lymantria dispar and several other Lepidopteran species have been cultured in vitro and have been induced to proliferate using low titers of ecdysteroids and the 77-Kda peptide fragment, ,-arylphorin, isolated and identified from pupal fat body tissue. The insulin-related hormone, Bombyxin, also induced mitosis in cultured midgut stem cells; it appeared to be fast-acting and quickly inactivated, while ,-arylphorin was slower to act and had a longer lasting effect in vitro, indicating different functions for these proliferation agents. Changes in Calcium ion concentration within or outside the cells discretely affected stem cell differentiation, indicating a role for second messenger participation in peptide regulation of this process. Four different peptides (MDFs 1,4) that induced midgut stem cells to differentiate to mature midgut cell types in vitro were isolated and characterized from conditioned media and hemolymph of H. virescens and L. dispar. However, platelet-derived growth factor (PDGF), epidermal growth factor (EGF), and all-trans retinoic acid (RA) from vertebrate sources induced differentiation to non-midgut cell types as well. MDF1 was located in basal areas of columnar cells of midgut epithelium, although MDF2 was observed in all of the cytoplasm of columnar cells and in droplets of antibody positive material in the midgut lumen, suggesting a digestive function as well for this peptide. Anti-MDF-3 stained the central areas of cultured midgut columnar cells and the bases of columnar cells of midgut epithelium in vivo. Midgut secretory cells stained with anti-MDF-4; streams of MFD-4-positive material were observed extending from secretory cells facing the epithelial lumen, and as a layer on the hemolymph-facing side, suggesting an endocrine or paracrine function for this or an immunologically similar peptide. Published 2010 Wiley Periodicals, Inc. [source] Stimulation of epidermal calcium gradient loss and increase in TNF-, and IL-1, expressions by glycolic acid in murine epidermisEXPERIMENTAL DERMATOLOGY, Issue 8 2005Se Kyoo Jeong Abstract:, In a previous study, we reported that ,-hydroxy acids (AHA), such as glycolic acid and lactic acid, did not induce any significant changes in transepidermal water loss for normal murine skin. The ultrastructural observations, however, showed that the extent of lamellar body exocytosis significantly increased. Because AHA can theoretically decrease the calcium ion concentration by chelation, topical AHA may induce the loss of epidermal calcium gradient by lowering the calcium ion concentration in the granulocytes and, subsequently, induce lamellar body secretion. The aim of this study is to verify that glycolic acid could modulate the epidermal calcium gradient and increase lamellar body exocytosis. Seventy per cent of glycolic acid aqueous solution was applied to the normal skin of hairless mice and biochemical and morphological studies were performed. The loss of epidermal calcium gradient was observed in glycolic-acid-applied skin of hairless mice and subsequent barrier function recovery processes, such as an increase in lamellar body secretion, were observed. The extracellular glycolic acid was found to inhibit the change in intracellular calcium ion concentration in response to extracellular calcium ion concentration changes in the cultured mouse keratinocyte in vitro. The protein and mRNA expressions of tumour necrosis factor-, and interleukin-1, in the murine epidermis were significantly increased after glycolic acid application. An in vitro study using cultured keratinocytes suggested that glycolic acid could lower the calcium ion concentration, at least in part, through the chelating effects of the glycolic acid on the cationic ions. [source] Insights into the structure of plant ,-type phospholipase DFEBS JOURNAL, Issue 10 2007Susanne Stumpe Phospholipases D play an important role in the regulation of cellular processes in plants and mammals. Moreover, they are an essential tool in the synthesis of phospholipids and phospholipid analogs. Knowledge of phospholipase D structures, however, is widely restricted to sequence data. The only known tertiary structure of a microbial phospholipase D cannot be generalized to eukaryotic phospholipases D. In this study, the isoenzyme form of phospholipase D from white cabbage (PLD,2), which is the most widely used plant phospholipase D in biocatalytic applications, has been characterized by small-angle X-ray scattering, UV-absorption, CD and fluorescence spectroscopy to yield the first insights into its secondary and tertiary structure. The structural model derived from small-angle X-ray scattering measurements reveals a barrel-shaped monomer with loosely structured tops. The far-UV CD-spectroscopic data indicate the presence of ,-helical as well as ,-structural elements, with the latter being dominant. The fluorescence and near-UV CD spectra point to tight packing of the aromatic residues in the core of the protein. From the near-UV CD signals and activity data as a function of the calcium ion concentration, two binding events characterized by dissociation constants in the ranges of 0.1 mm and 10,20 mm can be confirmed. The stability of PLD,2 proved to be substantially reduced in the presence of calcium ions, with salt-induced aggregation being the main reason for irreversible inactivation. [source] Effect of Soluble Soybean Protein Hydrolysate-Calcium Complexes on Calcium Uptake by Caco-2 CellsJOURNAL OF FOOD SCIENCE, Issue 7 2008Y. Lv ABSTRACT:, Soybean protein hydrolysates (SPHs) bind with calcium, forming soluble SPH-calcium complexes via the carboxyl groups of glutamic and aspartic acid residues. However, their effect on calcium uptake is still unclear. In this study, Caco-2 cells were used to estimate the effect of SPH-calcium complexes with different molecular weights on calcium uptake in vitro. The changes in intracellular calcium ion concentration were measured by Fura-2 loading and expressed in fluorescence intensity. SPH-calcium complexes could promote calcium uptake. Improved fluorescence intensity was significantly different in SPH-calcium complexes (10 to 30 kDa), SPH-calcium complexes (3 to 10 kDa), and SPH-calcium complexes (1 to 3 kDa). The maximum levels of relative fluorescence intensity (18.3) occurred with SPH-calcium complexes (10 to 30 kDa). The effect of SPH-calcium complexes (10 to 30 kDa) on Ca2+ increase was determined to be concentration dependent in the range of 0.5 to 4 mg/mL. Our results indicate that soybean protein itself might be responsible for promoting calcium absorption. [source] The intensity of the 1602 cm,1 band in human cells is related to mitochondrial activityJOURNAL OF RAMAN SPECTROSCOPY, Issue 5 2009Vishnu Vardhan Pully Abstract We report a Raman band at 1602 cm,1 in the spectra of human cells, which previously had only been observed in mitochondria of yeast cells. This band, which has not yet been assigned to a particular molecular species, was found to occur in HeLa cells, peripheral blood lymphocytes, human mesenchymal stem cells and bovine chondrocytes. The band is proposed as an indicator of the activity of mitochondria in cells. Cells were cultured with and without serum or temporarily deprived of serum. The band can be observed for all these variations in cell culture methodology. The band intensity decreases under the influence of an increase of the calcium ion concentration in the surrounding medium. Copyright © 2009 John Wiley & Sons, Ltd. [source] A two-step coagulation test to identify anti,2 -glycoprotein I lupus anticoagulantsJOURNAL OF THROMBOSIS AND HAEMOSTASIS, Issue 5 2004V. Pengo Summary., Lupus anticoagulants (LA) are immunoglobulins which inhibit phospholipid (PL)-dependent coagulation tests. LA are not specific, as they may reflect the presence of antibodies to human prothrombin, human ,2 -Glycoprotein I (,2GPI), an association of previous antibodies or other antibodies. Antibodies to human ,2GPI act as in vitro anticoagulants by enhancing the binding of ,2GPI to PL, and this binding may be influenced by calcium ion concentration. A reduction in final calcium concentration, from 10 mm to 5 mm, increased coagulation times in both dilute Russell Viper Venom Time (dRVVT) and dilute Prothrombin Time (dPT) when plasmas of patients with anti,2GPI antibodies were used. Ten LA patients showed increased dRVVT and dPT ratios from means of 1.5 to 1.7 (P < 0.001) and 2.4 to 4.3 (P = 0.002), respectively. Instead, all LA-positive anti,2GPI antibody-negative patients showed decreased coagulation times from mean ratios of 1.5 to 1.3 (P = 0.004) in dRVVT and from 2.0 to 1.5 (P = 0.01) in dPT. These results are confirmed by running dRVVT of normal plasma spiked with affinity purified IgG anti,2GPI antibodies. Therefore, when a PL,dependent coagulation test is run twice, at different final calcium concentrations, anti,2GPI LA can be identified. [source] The effect of short-term low-temperature treatments on gene expression in Arabidopsis correlates with changes in intracellular Ca2+ levelsPLANT CELL & ENVIRONMENT, Issue 4 2003K. NORDIN HENRIKSSON ABSTRACT The role of changes in intracellular calcium ion concentration ([Ca2+]i) in low-temperature signal transduction in plants has lately been supported by several studies. An analysis to determine whether the low-temperature-induced increase in cytosolic Ca2+ concentration ([Ca2+]cyt) could be correlated with a downstream response such as gene expression was carried out. The induction of the low-temperature-regulated gene LTI78 was used as an end point marker of the signal transduction pathway. It was found that this gene is induced by very brief low-temperature exposures and that the induction does not depend on a continuous exposure to low temperature. By altering the cooling rate, different patterns of the Ca2+ response were obtained which could be correlated with different patterns of LTI78 induction. Furthermore, reducing the Ca2+ transients by pre-treatment with the Ca2+ channel blocker La3+ also led to a reduced level of gene induction. The results show that brief exposures to low temperature results in the onset of a signalling pathway that leads to the induction of gene expression. This indicates the involvement of changes in [Ca2+]cyt in low-temperature signalling leading to LTI78 expression but the presence of multiple signalling pathways is suggested. [source] Evaluation of glucose sensitive affinity binding assay entrapped in fluorescent dissolved-core alginate microspheresBIOTECHNOLOGY & BIOENGINEERING, Issue 6 2009Ayesha Chaudhary Abstract The feasibility of dissolved-core alginate-templated fluorescent microspheres as "smart tattoo" glucose biosensors was investigated in simulated interstitial fluid (SIF). The sensor works on the principle of competitive binding and fluorescence resonance energy transfer. The sensor consists of multilayer thin film coated alginate microspheres incorporating dye-labeled glucose receptor and competing ligand within the partially dissolved alginate core. In this study, different approaches for the sensing and detection chemistry were studied, and the response of encapsulated reagents was compared with the solution-phase counterparts. The glucose sensitivity of the encapsulated TRITC-Con A/FITC-dextran (500,kDa) assay in DI water was estimated to be 0.26%/mM glucose while that in SIF was observed to be 0.3%/mM glucose. The glucose sensitivity of TRITC-apo-GOx/FITC-dextran (500,kDa) assay was estimated to be 0.33%/mM glucose in DI water and 0.5%/mM glucose in SIF and both demonstrated a response in the range of 0,50,mM glucose. Therefore, it is hypothesized that the calcium ion concentration outside the microsphere (in the SIF) does not interfere with the response sensitivity. The sensor response was observed to exhibit a maximum response time of 120,s. The system further exhibited a sensitivity of 0.94%/mM glucose with a response in range of 0,50,mM glucose, using near-infrared dyes (Alexa Fluor-647-labeled dextran as donor and QSY-21-conjugated apo-GOx as acceptor), thereby making the sensor more amenable to in vivo use, when implanted in scattering tissue. Biotechnol. Bioeng. 2009; 104: 1075,1085. © 2009 Wiley Periodicals, Inc. [source] Effect of antisense oligonucleotide against mouse dentine matrix protein 1 on mineralization ability and calcium ions metabolism in odontoblast-like cell line MDPC-23INTERNATIONAL ENDODONTIC JOURNAL, Issue 7 2006J. L. Pang Abstract Aim, To study the mineralization ability and the dynamic changes of intracellular and extracellular concentrations of calcium ions in the odontoblast-like cell line MDPC-23 affected by antisense oligonucleotide (AS-ODN) against mouse dentine matrix protein 1 (DMP1). Methodology, The expression of DMP1 in MDPC-23 cells was detected by an immunohistochemical method and its blocking outcome by the Western blot method. The alkaline phosphatase (ALP) activity, size and number of mineralized nodules, and the intracellular free ([Ca2+]if), total ([Ca2+]it) and the extracellular ([Ca2+]e) calcium ion concentrations in MDPC-23 cells in the experimental group affected with AS-ODN were compared with those in the control group (paired-samples t -test). Results, Dentine matrix protein 1 was stably expressed in a stable way in MDPC-23 cells; the expression was only just detectable at 12 h and became negative after 24 h affected by AS-ODN. Compared with the control groups, ALP activity of MDPC-23 cells in the AS-ODN group was decreased (P < 0.05), and both the number and size of mineralized nodules were smaller than those in the control group. [Ca2+]if in the AS-ODN group increased and then decreased after 24 h. [Ca2+]it dropped substantially to the lowest point at 24 h (P < 0.01). [Ca2+]e increased before treatment for 24 h and then dropped, however, it was still higher than that of the control group. Conclusions, Antisense oligonucleotide against DMP1 could decrease mineralization ability and affect the intracellular and extracellular concentrations of calcium ions in MDPC-23 cells. This would indicate that DMP1 regulates the metabolism and transportation of calcium ions in odontoblasts, and thus boosts dentine mineralization. [source] | ||||||||||||||||