New Evidence for the Diversity of Mechanisms and Protonated Schiff Bases Formed in the Non-Enzymatic Covalent Protein Modification (NECPM) of HbA by the Hydrate and Aldehydic Forms of Acetaldehyde and Glyceraldehyde.

Acetaldehyde is a physiological species existing in blood. Glyceraldehyde is a commonly-used surrogate for glucose in studies of nonenzymatic glycation. Both species exist in dynamic equilibrium between two forms, an aldehyde and a hydrate.

Echocardiography and electrocardiography reveal differences in cardiac hemodynamics, electrical characteristics, and thermal sensitivity between northern pike, rainbow trout, and white sturgeon.

Doppler and B-mode ultrasonography and electrocardiography (ECG) were used to determine cardiac hemodynamics and electrical characteristics in 12°C-acclimated and metomidate-anesthetized northern pike, rainbow trout and white sturgeon (7-9 per species) at 12°C and 20°C, and at a comparable heart rate (f , ~60 beats/min). Despite similar relative ventricle masses and cardiac output (Q), interspecific differences were observed at 12°C in f , ventricular filling and ejection, stroke volume, the duration ECG intervals, and cardiac valve cross-sectional areas. Vis-a-fronte filling of the atrium due to ventricular contraction was observed in all species.

Insights into the Progression of Labile Hb A to Stable Hb A a Mechanistic Assessment of 2,3-Bisphosphoglycerate Facilitation of the Slow Nonenzymatic Glycation Process.

Nonenzymatic glycation (NEG) of human hemoglobin (Hb A) consists of initial non covalent, reversible steps involving glucose and amino acid residues, which may also involve effector reagent(s) in the formation of labile Hb A (the conjugate acid of the Schiff base). Labile Hb A can then undergo slow, largely irreversible, formation of stable Hb A (the Amadori product). Stable Hb A is measured to assess diabetic progression after labile Hb A removal.

Is the teleost heart oxygen limited? - Insights using "hyperoxic" incubations of contracting cardiac tissue from rainbow trout.

Considerable effort has been devoted to understanding the negative effects of reduced PO on cardiac function. Much less is known about the impacts of elevated PO (hyperoxia) on cardiac performance and energetics, especially in fishes. The fish heart is of particular interest because cardiac dependence on oxygen is extremely variable between species and the early evolution of fish occurred when atmospheric PO was higher than current conditions.

Potential roles of inorganic phosphate on the progression of initially bound glucopyranose toward the nonenzymatic glycation of human hemoglobin: mechanistic diversity and impacts on site selectivity.

Nonenzymatic glycation (NEG) begins with the non-covalent binding of a glucopyranose to a protein. The bound glucopyranose must then undergo structural modification to generate a bound electrophile that can reversibly form a Schiff base, which can then lead to Amadori intermediates, and ultimately to glycated proteins. Inorganic phosphate (Pi) is known to accelerate the glycation of human hemoglobin (HbA), although the specific mechanism(s) of Pi as an effector reagent have not been determined.