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Connect Tissue Res. 1998;38(1-4):189-99; discussion 201-5.
Two new in vitro calcification systems showing the higher calcifiability of enamel proteins than dentin and bone matrices.
Kuboki Y, Liu A, Ren LD, Ono M, Taira T, Takita H, Moriwaki Y, Iijima M, Takagi T.
Department of Biochemistry, School of Dentistry, Hokkaido University, Japan.
One of the difficulties in simulating in vivo calcification by in vitro experiments is how to prepare and apply a suitable calcifying solution. We have previously developed an entirely new model system consisting of 40% acrylamide gel blocks that contains matrix proteins and is immersed in fetal calf serum at 37 degrees C. (40% gel system) for 18 hr (Connect. Tissue Res., 33, 185, 1995). The gels were analyzed for immobilized calcium. In this system bovine enamel proteins (0.1% in the gel) showed the highest calcifiability among the tested matrices, followed by insoluble bovine dentin, bone and skin collagens. The 40% gel system provides a barrier for high molecular weight inhibitor molecules in the body fluid. The new calcifying system developed in this study consists of the matrix protein sealed in dialysis tubing within a glass chromatography column that was eluted with a calcifying solution. In this system (dialysis tubing system), again the enamel protein showed higher calcifiability than dentin, bone and skin collagens. It was also shown that enamel proteins became not only a reversible opaque gel, but also a relatively-irreversible coagulant, if the solution contained calcium and phosphate ions at concentration below saturation (1 mM calcium and 1 mM phosphate). With both systems combined, deposition and crystal growth of minerals in enamel proteins will be better understood than with previous methods.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11063027&dopt=Abstract
Life Sci. 2000 Oct 6;67(20):2493-512.
Early effects of exogenous arginine after the implantation of prosthetic material into the rat abdominal wall.
Arbss MA, Ferrando JM, Vidal J, Quiles MT, Huguet P, Castells J, Segarra A, Armengol M, Schwartz S.
Unitat de Matriu Extracel.lular, Centre d'Investigacions en Bioquimica i Biologia Molecular, Hospitals Universitaris Vail d'Hebron, Barcelona, Spain. a_arbog.vhebron.es
We have investigated the effects of high arginine (Arg) levels (7.5 mg/100 g body weight per hour) on the early integration of biocompatible mesh grafts into the rat abdominal wall. Studies were performed over implantation intervals of 6, 12, 24 or 48 hours (n=12, each). Arginine and related compounds were quantified in plasma, wound fluids and multiple tissues. Plasma nitric oxide (NO) production was studied. Strips were taken from the polypropylene fiber-host tissue interfaces (PTIs) for optical microscopic analysis and for immunohistochemical analysis using rat-specific antibodies against type I and type III collagens. Exogenous Arg was metabolized at the peripheral tissues but reliably reached the wound space. High amounts of Arg and ornithine (Orn) were detected in the specimens considered. No changes on citrulline (Ctr) or NO concentrations were observed, overall suggesting that, during the period studied, the arginase pathway predominated. The acute scarring response differed significantly in the two placements considered. The P-SS interface evidenced more extensive new tissue growth than the P-DS interface. Forty-eight hours after mesh implantation cellular infiltration, fibroblast proliferation, and mesh-surrounding angiogenesis were higher in the arginine-treated rats. Type III collagen staining was related to arginine treatment, being higher (++) in the study group. In conclusion, and independently of the site of mesh placement, supplemental Arg seemed to favorably affect early local collagen deposition. This could be potentially helpful to ameliorate the integration of biomaterials into the tissues and, consequently, to allow for the design of more selective therapeutic strategies to prevent hernia recurrence rates.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11065172&dopt=Abstract
UTHSCSA.edu
The two major dentin matrix proteins, dentin sialoprotein and dentin phosphoprotein have been shown to be expressed as a single large transcript termed dentin sialophosphoprotein (DSPP). These non-collagenous matrix proteins, identified biochemically by their unique physical-chemical properties, are specific cleavage products of a large parent acidic phosphorylated protein (pI 4.0). Previous studies have shown expression of dentin sialoprotein at the protein level by ameloblasts. The purpose of this study was to determine the temporal-spatial pattern of DSPP expression during amelogenesis. In situ hybridization and immunohistochemistry were performed on sections of developing mouse molars. These data were correlated with RT-PCR analysis of in vitro enamel organ epithelium monolayer cell cultures enriched for ameloblasts. Our data indicates initial expression of the DSPP transcripts and protein during early ameloblast differentiation prior to the secretory phase when the majority of the enamel matrix is formed. Ameloblasts appear to tightly down-regulate DSPP transcription as enamel matrix formation is up-regulated. These data demonstrate DSPP expression during amelogenesis is under highly controlled developmental regulation. Therefore, DSPP may have a primary role in the initial mineralization events of both enamel and dentin, acting as a potential nucleator of hydroxyapatite crystal formation.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11062986&dopt=Abstract
Am J Clin Nutr. 2000 Nov;72(5):1150-5.
The flavonoids quercetin and catechin synergistically inhibit platelet function by antagonizing the intracellular production of hydrogen peroxide.
Pignatelli P, Pulcinelli FM, Celestini A, Lenti L, Ghiselli A, Gazzaniga PP, Violi F.
Department of Experimental Medicine and Pathology, Institute of 1st Clinical Medicine, University La Sapienza, National Institute for Nutrition, Rome, Italy. gazzanigniroma1.it
BACKGROUND: Epidemiologic studies have shown an inverse relation between moderate consumption of red wine and cardiovascular disease. Studies have shown that red wine and its component flavonoids inhibit in vivo platelet activation, but the underlying mechanism has not yet been identified. OBJECTIVE: Because we showed previously that collagen-induced platelet aggregation is associated with a burst of hydrogen peroxide, which in turn contributes to stimulating the phospholipase C pathway, the aim of this study was to investigate whether flavonoids synergize in inhibiting platelet function and interfere with platelet function by virtue of their antioxidant effect. DESIGN: We tested the effect of 2 flavonoids, quercetin and catechin, on collagen-induced platelet aggregation and hydrogen peroxide and on platelet adhesion to collagen. RESULTS: Catechin (50-100 micromol/L) and quercetin (10-20 micromol/L) inhibited collagen-induced platelet aggregation and platelet adhesion to collagen. The combination of 25 micromol catechin/L and 5 micromol quercetin/L, neither of which had any effect on platelet function when used alone, significantly inhibited collagen-induced platelet aggregation and platelet adhesion to collagen. Such a combination strongly inhibited collagen-induced hydrogen peroxide production, calcium mobilization, and 1,3,4-inositol triphosphate formation. CONCLUSIONS: These data indicate that flavonoids inhibit platelet function by blunting hydrogen peroxide production and, in turn, phospholipase C activation and suggest that the synergism among flavonoids could contribute to an understanding of the relation between the moderate consumption of red wine and the decreased risk of cardiovascular disease.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11063442&dopt=Abstract
Methods Cell Biol. 2001;63:583-97.
Three-dimensional imaging of extracellular matrix and extracellular matrix-cell interactions.
Voytik-Harbin SL, Rajwa B, Robinson JP.
Department of Basic Medical Sciences, School of Veterinary Medicine, Purdue University, West Lafayette, Indiana 47907, USA.
In summary, noninvasive and nondestructive imaging modalities such as reflection and autofluorescence can readily be used in conjunction with the 3-D optical sectioning capabilities of confocal and multiphoton microscopy to investigate biological processes within living systems. The elimination of specimen fixation and extensive processing reduces the possibility of structural artifacts and facilitates repeat observations within a single sample. Therefore, information representing up to four dimensions (x, y, z, and time) can be readily collected and reconstructed for purposes of visualization and/or quantitative analysis. An advantage of using the techniques described in this chapter is the possibility of performing quantitative measurement of cell size, surface area, volume, depth (in matrix), orientation, receptor density, as well as fluorescence-based indicators of phenotype and function. At present, we are effectively utilizing these techniques to study collagen fibrillogenesis and ECM assembly, structural aspects of ECM-based biomaterials, as well as cell interactions within 3-D matrices (e.g., migration). New insights provided by these techniques regarding ECM and ECM-cell signaling will further the understanding of tissue structure and function and contribute to the development of new and improved strategies for tissue repair, replacement, and maintenance.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11060860&dopt=Abstract
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