Abstract
Insulin internalization has been extensively studied in target cells, this process has not been characterized in human (E). Cord blood (E) were incubated with 125I-insulin at 4°C.or at 37°C. in the presence and absence of Methylamine (M) which induces intracellular accumulation of insulin or Phenylarsine oxide (P) a well known inhibitor of endocytosis. At various time points, insulin binding (I.B.), haemolysis and degradation were determined, and insulin internalization was quantified using an acid extraction technique. Our results show that (M) and (P) failed to alter (I. B.) in (E).Insulin bound at 4°C. was 90-95% extractable and TCA precipitable while at 37°C. with increasing time of incubation the extractability of cell bound insulin and the proportion of intact, undegraded, extractable insulin decrease. In adition (I.B.) degradation and non-extractable acid insulin were increased by haemolysis even at 4°C.
In conclusion our (I.B.) values in cord blood (E) from pre-term and term were 13.2±4.7 and 7.9±2.2 % x3.3×109(E) or 370 and 257 sites/(E) respectively and the differences were accounted for by a membrane interaction with minimal internalization.
Incubation at low temperature to prevent haemolysis and degradation must be taken into consideration in (I.B.) studies in (E) for clinical application.
Log in or create a free account to read this content
Gain free access to this article, as well as selected content from this journal and more on nature.com
or
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Potau, N., Bartolomé, R., Escofet, A. et al. INSULIN INTERNALIZATION STUDY IN CORD BLOOD ERYTHROCYTES. (E). Pediatr Res 20, 1206 (1986). https://doi.org/10.1203/00006450-198611000-00198
Issue date:
DOI: https://doi.org/10.1203/00006450-198611000-00198
