Variability in individual native fibrin fiber mechanics.

Fibrin fibers are important structural elements in blood coagulation. They form a mesh network that acts as a scaffold and imparts mechanical strength to the clot. A review of published work measuring the mechanics of fibrin fibers reveals a range of values for fiber extensibility.

A Study of the Relationship between Polymer Solution Entanglement and Electrospun PCL Fiber Mechanics.

Electrospun fibers range in size from nanometers to micrometers and have a multitude of potential applications that depend upon their morphology and mechanics. In this paper, we investigate the effect of polymer solution entanglement on the mechanical properties of individual electrospun polycaprolactone (PCL) fibers. Multiple concentrations of PCL, a biocompatible polymer, were dissolved in a minimum toxicity solvent composed of acetic acid and formic acid.

Labeling fibrin fibers with beads alter single fibrin fiber lysis, external clot lysis, and produce large fibrin aggregates upon lysis.

Fluorescent beads are often used as a tool for visualizing fibrin fibers in single fiber mechanics studies and studies of single fiber lysis. Here we investigate the effect of beads on fibrin fiber lysis and extensibility to enhance understanding of this common research technique. We selected beads of the same diameter as those used in previous studies, as well as, beads of similar size to microparticles in the bloodstream.

Erythrocytes and Vascular Function: Oxygen and Nitric Oxide.

Erythrocytes regulate vascular function through the modulation of oxygen delivery and the scavenging and generation of nitric oxide (NO). First, hemoglobin inside the red blood cell binds oxygen in the lungs and delivers it to tissues throughout the body in an allosterically regulated process, modulated by oxygen, carbon dioxide and proton concentrations. The vasculature responds to low oxygen tensions through vasodilation, further recruiting blood flow and oxygen carrying erythrocytes.

Nonuniform Internal Structure of Fibrin Fibers: Protein Density and Bond Density Strongly Decrease with Increasing Diameter.

The major structural component of a blood clot is a meshwork of fibrin fibers. It has long been thought that the internal structure of fibrin fibers is homogeneous; that is, the protein density and the bond density between protofibrils are uniform and do not depend on fiber diameter. We performed experiments to investigate the internal structure of fibrin fibers.

Exposure of fibrinogen and thrombin to nitric oxide donor ProliNONOate affects fibrin clot properties.

: Fibrin fibers form the structural backbone of blood clots. The structural properties of fibrin clots are highly dependent on formation kinetics. Environmental factors such as protein concentration, pH, salt, and protein modification, to name a few, can affect fiber kinetics through altered fibrinopeptide release, monomer association, and/or lateral aggregation.

Recent insights into nitrite signaling processes in blood.

Nitrite was once thought to be inert in human physiology. However, research over the past few decades has established a link between nitrite and the production of nitric oxide (NO) that is potentiated under hypoxic and acidic conditions. Under this new role nitrite acts as a storage pool for bioavailable NO.

Fibrin Fiber Stiffness Is Strongly Affected by Fiber Diameter, but Not by Fibrinogen Glycation.

The major structural component of a blood clot is a mesh of fibrin fibers. Our goal was to determine whether fibrinogen glycation and fibrin fiber diameter have an effect on the mechanical properties of single fibrin fibers. We used a combined atomic force microscopy/fluorescence microscopy technique to determine the mechanical properties of individual fibrin fibers formed from blood plasma.

Mechanisms of human erythrocytic bioactivation of nitrite.

Nitrite signaling likely occurs through its reduction to nitric oxide (NO). Several reports support a role of erythrocytes and hemoglobin in nitrite reduction, but this remains controversial, and alternative reductive pathways have been proposed. In this work we determined whether the primary human erythrocytic nitrite reductase is hemoglobin as opposed to other erythrocytic proteins that have been suggested to be the major source of nitrite reduction.

Loving-kindness meditation's effects on nitric oxide and perceived well-being: a pilot study in experienced and inexperienced meditators.

Background: Meditation is associated with lower blood pressure, but little is known about how loving-kindness meditation affects nitric oxide (NO) metabolism, a key mediator of cardiovascular physiology associated with vasodilation.

Methods: We studied seven inexperienced and five experienced healthy meditators at one study visit, after they refrained from eating nitrate-rich foods for at least 12h. Participants completed questionnaires on demographics and meditation practices.

Dietary nitrate supplementation improves exercise performance and decreases blood pressure in COPD patients.

Dietary nitrate (NO3(-)) supplementation via beetroot juice has been shown to increase the exercise capacity of younger and older adults. The purpose of this study was to investigate the effects of acute NO3(-) ingestion on the submaximal constant work rate exercise capacity of COPD patients. Fifteen patients were assigned in a randomized, single-blind, crossover design to receive one of two treatments (beetroot juice then placebo or placebo then beetroot juice).

Mortality increases after massive exchange transfusion with older stored blood in canines with experimental pneumonia.

Two-year-old purpose-bred beagles (n = 24) infected with Staphylococcus aureus pneumonia were randomized in a blinded fashion for exchange transfusion with either 7- or 42-day-old canine universal donor blood (80 mL/kg in 4 divided doses). Older blood increased mortality (P = .0005), the arterial alveolar oxygen gradient (24-48 hours after infection; P ≤ .

Angeli's salt counteracts the vasoactive effects of elevated plasma hemoglobin.

Plasma hemoglobin (Hb) released during intravascular hemolysis has been associated with numerous deleterious effects that may stem from increased nitric oxide (NO) scavenging, but has also been associated with reactive oxygen species generation and platelet activation. Therapies that convert plasma oxyHb to metHb, or metHb to iron-nitrosyl Hb, could be beneficial because these species do not scavenge NO. In this study, we investigated the effects of Angeli's salt (AS; sodium α-oxyhyponitrite, Na2N2O3), a nitroxyl (HNO) and nitrite (NO2(-)) donor, on plasma Hb oxidation and formation of iron-nitrosyl Hb from metHb and on the vasoactivity of plasma Hb.

A modular fibrinogen model that captures the stress-strain behavior of fibrin fibers.

We tested what to our knowledge is a new computational model for fibrin fiber mechanical behavior. The model is composed of three distinct elements: the folded fibrinogen core as seen in the crystal structure, the unstructured α-C connector, and the partially folded α-C domain. Previous studies have highlighted the importance of all three regions and how they may contribute to fibrin fiber stress-strain behavior.

α-α Cross-links increase fibrin fiber elasticity and stiffness.

Fibrin fibers, which are ~100 nm in diameter, are the major structural component of a blood clot. The mechanical properties of single fibrin fibers determine the behavior of a blood clot and, thus, have a critical influence on heart attacks, strokes, and embolisms. Cross-linking is thought to fortify blood clots; though, the role of α-α cross-links in fibrin fiber assembly and their effect on the mechanical properties of single fibrin fibers are poorly understood.