Hoekstra, D

Klappe, K

Niketic, Vesna

Nikolic, M.

Tomasevic, N

English

Under hypoglycemic conditions, concomitant hyperinsulinism causes an apparent modification of hemoglobin (Hb) which is manifested by its a aggregation (Niketic et al.. Clin. Chim. Acia 197 (1991) 47). In the present work the causes and mechanisms underlying this Hb modification were Studied. Hemoglobin isolated from normal erythrocytes incubated with insulin was analyzed by applying P-31-spectrometry and lipid extraction and analysis. To study the dynamics of the plasma membrane during hperinsulinisra a fluorescent lipid-analog was applied. In the presence of insulin phosphatidylserine (PS). phosphatidylethanolamine (PE) and cholesterol were found to bind to Hb. Lipid binding resulted in Hb aggregation, a condition that can be reproduced when phospholipids arc incubated with Hb in vitro. Using a fluorescent lipid-analog, it was also shown that exposing crythrocytes to supraphysiological concentrations of insulin in vitro resulted in the internalization of lipids. The results presented in this work, may have relevance to cases of diabetes mellitus and hypoglycemia.</p

ARTS repository - University of Groningen

Insulin-induced lipid binding to hemoglobin

https://pure.rug.nl/ws/files/62132994/Insulin_induced_lipid_binding_to_hemoglobin.pdf

Insulin-induced lipid binding to hemoglobin

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ARTS repository - University of Groningen