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Collagen fibrils in extracellular matrices of connective tissues (tendon, cornea, etc.) are bridged and linked by the anionic glycosaminoglycans (AGAGs) of the small proteoglycans (decoron, etc.). It was proposed that these bridges and ties maintain the collagen fibril dispositions in relation to each other, helping to define tissue shape, and hence called shape modules. This investigation describes chemical and physicochemical conditions in which these structures are stable and what treatments cause their disruption. The effects on fixed and unfixed sections of tendon, cornea, lung and ear from rat, mouse and rabbit of pH, electrolyte concentration, EDTA, mercaptoethanol, hydrogen peroxide, free radicals, periodate, acetylation, urea, nonionic detergent and organic solvents were assessed by staining with Cupromeronic blue or Alcec blue in CEC techniques to localise AGAG bridges or their disintegration products. Ca2+ was not involved in the structures, oxidation/reduction had no effect and Triton X100, a nonionic detergent did not damage them. They were stable between pH 4.5 and 9.5. Periodate as a glycol-cleaving reagent did not affect them. High concentrations of urea (> 2.0 M) and MgCl2 (0.5 M) disrupted the tissues. The combination of Triton and urea at concentrations too low to cause damage separately was disruptive. Free radicals in periodate solutions were damaging. Organic solvents caused collapse and rearrangements of the AGAG filaments. Acetylation caused considerable disruption of shape modules. Dermochondan but not keratan sulphate AGAGs were removed by treatment with NaOH. After fixing with glutaraldehyde only free radical and NaOH treatments were severely disruptive of shape modules. The results are compatible with a previously proposed structure for the shape modules, stabilised by hydrophobic and hydrogen bonding.
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PMID:The structure of interfibrillar proteoglycan bridges (shape modules') in extracellular matrix of fibrous connective tissues and their stability in various chemical environments. 968 5

Wyoming montmorillonite (Volclay) with different charges were produced by Li-incorporation and the interlayer cations were replaced by tetramethyl ammonium. Their XRD pattern showed a regular sequence of expanded and collapsed interlayers. The regularly interstratified structure corresponds to a regularity of Reichweite R = 1. The expanded part of the interlayers was calculated by comparing XRD pattern with simulations using NEWMOD software. The calculations of the cation exchange capacity CEC for the expanded interlayer part gives a constant value of 65 +/- 2 mmol/100 g fully swellable montmorillonite. This value is denoted as the lower CEC limit of montmorillonite. We propose a model which considers montmorillonite to be a stacked two-dimensional polyelectrolyte. The model propose that interlayers of the stack collapse spontaneously by cation shifting into the neighboring interlayers, if the charge density of a montmorillonite has a value below the lower CEC value. The shifted cations of the collapsed interlayer increase the charge density in the neighboring interlayers and prevent their collapse. A regularly interstratified structure arises with the sequence expanded/collapsed/expanded interlayer, which can be observed by XRD. The behavior of low charged montmorillonite is explained with the properties of a two-dimensional polyelectrolyte. Below the critical layer charge, the Van der Waals forces dominate over electrostatic repulsive forces and the interlayers collapse. Copyright 1999 Academic Press.
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PMID:The Lower Cation Exchange Capacity Limit of Montmorillonite. 1044 13

We tested the effect of ACE inhibition on the survival of bovine retinal (REC) and choroidal (CEC) endothelial cells (EC) in culture. The ACE inhibitor captopril delayed the apoptotic tube collapse of REC on Matrigel for >15 days. Captopril treatment of confluent monolayers (2-8 weeks) followed by slow starvation (2-4 weeks) increased EC viability by approximately 200%. Two-week captopril exposures were sufficient to confer maximal protection. Only vehicle-treated EC demonstrated apoptotic features such as membrane blebbing and DNA laddering. By RT-PCR, the starvation marker p202 was upregulated only in starved cells. In REC, captopril upregulated the pro-survival proteins mortalin-2, uPA, and uPAR while downregulating the anti-growth sprouty-4 and tPA. In CEC, captopril also upregulated tPA and its inhibitor PAI-1. Amiloride (uPA inhibitor) blocked the captopril-induced increase in EC survival, secondary sprouting, and invasion in Matrigel. The pro-survival effects of captopril involve the reprogramming of genes involved in cell survival and immortalization.
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PMID:ACE inhibition actively promotes cell survival by altering gene expression. 1455 46