Enhancement of S-Nitrosylation in Glycosylated Hemoglobin

• Published in: Biochemical and biophysical research communications Vol. 271; no. 1; pp. 217 - 221
• Main Authors: Padrón, Julio, Peiró, Concepción, Cercas, Elena, Llergo, José L., Sánchez-Ferrer, Carlos F.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 29.04.2000
• Subjects: Analysis of Variance; Animals; Cysteine - analogs & derivatives; Cysteine - metabolism; diabetes mellitus; Diabetes Mellitus, Experimental - blood; Erythrocytes - metabolism; Glycated Hemoglobin A - chemistry; Glycated Hemoglobin A - metabolism; glycosylated hemoglobin; Hemoglobins - metabolism; Humans; In Vitro Techniques; Isoelectric Focusing; Male; nitric oxide; Nitric Oxide - metabolism; Nitroso Compounds - metabolism; Rats; Rats, Sprague-Dawley; S-nitrosohemoglobin; S-Nitrosothiols; Time Factors; S-nitrosohemoglobin; nitric oxide; diabetes mellitus; glycosylated hemoglobin
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.2000.2617

In this study, we report a novel differential nitric oxide interaction with nonglycosylated and glycosylated hemoglobin. After in vitro incubation of hemoglobin with S-nitroso N-acetyl penicillamine (SNAP), S-nitrosoglutathione, or S-nitrosocysteine, S-nitrosylation was significantly higher in human glycosylated hemoglobin purified from diabetic subjects compared to nondiabetic controls. Inversely, spontaneous decomposition was significantly lower for S-nitrosohemoglobin obtained from glycosylated hemoglobin. Bidimensional isoelectric focusing of hemoglobins incubated in vitro with SNAP also revealed a greater interaction of nitric oxide with glycosylated hemoglobin. In addition, a significantly higher level of S-nitrosohemoglobin was found in erythrocyte lysates from streptozotocin-induced diabetic rats compared to control rats. We suggest that highly glycosylated hemoglobin in diabetic subjects may favor S-nitrosylation, which may in turn impair vascular function, and participate in diabetic microangiopathy.