Aging in humans and animals is associated with gradual and variable changes in some cognitive functions, but what causes them and explains individual variations remains unclear. Hydration decreases with aging but whether dehydration contributes to cognitive dysfunction is not known. The brain hydration of aging mice was determined by colloidosmotic-pressure titration.
View Article and Find Full Text PDFThe interstitial myocardial matrix is a complex and dynamic structure that adapts to local fluctuations in pressure and actively contributes to the heart's fluid exchange and hydration. However, classical physiologic models tend to treat it as a passive conduit for water and solute, perhaps because local interstitial regulatory mechanisms are not easily accessible to experiment in vivo. Here, we examined the interstitial contribution to the fluid-driving pressure ex vivo.
View Article and Find Full Text PDFThermal injury disrupts fluid homeostasis and hydration, affecting hemodynamics and local interstitial fluid-driving forces, leading rapidly to edema. This study explores local mechanisms in vivo, after deep partial-thickness burns in the dermal matrix. Heat-damaged skin was obtained from pig corpses, byproducts of unrelated burn treatment protocols approved by the Institutional Animal-Care-and-Use Committee.
View Article and Find Full Text PDFIn the interstitial matrix, collagen unfolding at physiologic temperatures is thought to facilitate interactions with enzymes and scaffold molecules during inflammation, tissue remodeling, and wound healing. We tested the hypothesis that it also plays a role in modulating flows and matrix hydration potential. After progressively unfolding dermal collagen in situ, we measured the hydration parameters by osmotic stress techniques and modeled them as linear functions of unfolded collagen, quantified by differential scanning calorimetry after timed heat treatment.
View Article and Find Full Text PDFThe local pathogenesis of interstitial edema in burns is incompletely understood. This ex vivo study investigates the forces mediating water-transfer in and out of heat-denatured interstitial matrix. Experimentally, full-thickness dermal samples are heated progressively to disrupt glycosaminoglycans, kill cells, and denature collagen under conditions that prevent water loss/gain; subsequently, a battery of complementary techniques including among others, high-resolution magnetic resonance imaging, equilibrium vapor pressure and osmotic stress are used to compare water-potential parameters of nonheated and heated dermis.
View Article and Find Full Text PDFAm J Physiol Regul Integr Comp Physiol
June 2009
Water transfer across the extracellular matrix (ECM) involves interstitial osmotic forces in as yet unclear ways. In particular, the traditional values of Starling forces cannot adequately explain fluid transfer rates. Here, we reassess these forces by analyzing fluid transfer in live pig and human dermal explants.
View Article and Find Full Text PDFMany biologically important macromolecular reactions are assembled and catalyzed at the cell lipid-surface and thus, the extracellular matrix and the glycocalyx layer mediate transfer and exchange of reactants and products between the flowing blood and the catalytic lipid-surface. This paper presents a mathematical model of reaction-diffusion equations that simply describes the transfer process and explores its influence on surface reactivity for a prototypical pathway, the tissue factor (Tf) pathway of blood coagulation. The progressively increasing friction offered by the matrix and glycocalyx to reactants and to the product (coagulation factors X, VIIa and Xa) approaching the reactive surface is simulated and tested by solving the equations numerically with both, monotonically decreasing and constant diffusion profiles.
View Article and Find Full Text PDFGlycosaminoglycans (GAGs) in pericellular and interstitial spaces help to maintain local water homeostasis and blood coagulation balance. This study explored whether dehydrating microenvironment conditions influence dermatan sulfate's (DS) anticoagulant activity. Water transfer during antithrombin activation by dermatan sulfate was measured using osmotic stress techniques.
View Article and Find Full Text PDFAntithrombin is a key inhibitor of blood coagulation proteases and a prototype metastable protein. Heparin binding to antithrombin induces conformational transitions distal to the binding site. We applied osmotic stress techniques and rate measurements in the stopped flow fluorometer to investigate the possibility that hydration changes are associated with these transitions.
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