Abstract |
Even though one of the characteristic features of myotonic dystrophy (MyD) is the high level of circulating insulin, 125I-insulin-binding data in MyD have been controversial. In the present study we utilized cultured monocytes to avoid problems of reproducibility and variability in age, and examined the affinity and binding characteristics of 125I-insulin binding in MyD patients and controls. The Bmax and mean affinity constant, Ka, were significantly lower, while the number of receptors per cell had increased in the patient group as compared to the controls. The data confirm our earlier findings that there is no primary defect in insulin receptors in MyD, and the disturbed insulin response may be due to an abnormality in the membrane environment. Since the insulin receptor is an integral membrane protein, abnormal plasma membrane lipid composition may lead to impaired lipid- protein interactions, and hence affect the binding characteristics in MyD.
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Authors | S K Mishra, S Chetty, M Kataoka |
Journal | Biochemical medicine and metabolic biology
(Biochem Med Metab Biol)
Vol. 47
Issue 2
Pg. 161-7
(Apr 1992)
ISSN: 0885-4505 [Print] United States |
PMID | 1515174
(Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, Non-P.H.S.)
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Chemical References |
- Insulin
- Receptor, Insulin
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Topics |
- Humans
- Insulin
(metabolism)
- Kinetics
- Monocytes
(metabolism)
- Muscular Dystrophies
(blood)
- Receptor, Insulin
(metabolism)
- Reference Values
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