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Different glycosidic probes upon binding to coronary endothelial lectins selectively modulate cardiac contractility and A‐V node conduction
Author(s) -
RamiroDiaz Juan Manuel,
BarajasEspinosa Alma Rosa,
CastilloHernandez Jesus Ramon,
Rubio Rafael
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1379-b
Subject(s) - contractility , glycosidic bond , chemistry , biophysics , covalent bond , biochemistry , medicine , biology , organic chemistry , enzyme
Coronary flow modifies cardiac functions; stress exerted by flow on the capillary wall may be junction‐transduced by glycosidic and lectinic structures in the luminal endothelial glycocalyx. To test this we synthesized monosaccharide polymers formed by Mannose (PolMan) or Galactose (PolGal) or N‐acetyl Glucosamine (PolNGlc) covalently linked to a 70 KDa dextran. These polymers were intracoronarily administered in perfused guinea pig hearts at increasing concentrations. Left intraventricular pressure, measured as cardiac contractility (CC), and the Auricular‐Ventricular delay was taken as index of conduction time in the A‐V node (A‐V D ). PolMan increases the A‐V D without affecting CC. PolNGlc increases the A‐V D and decreases the CC. PolGal produces smaller effects than the other polymers. The effects of these polymers were not easily washed. To visualize polymer binding sites, PolMan and PolNGlc covalently linked to a dextran‐FITC were synthesized. These were intracoronarily administered and subsequently washed. Venuous effluents were collected and the fluorescence was measured. Perfused polymers were retained in the vasculature and required a 20 min wash to return to basal fluorescence. These results suggest the presence of lectinic receptors with affinity to glycosidic motifs and certain selectivity in the response elicited by the probes. Funded by CONACyT SEP‐42567, CONACyT‐SALUD 2004‐C01‐156