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Regulation of insulin receptor functions by a peptide derived from a major histocompatibility complex class I antigen.
- Source :
-
Cell [Cell] 1990 Jul 27; Vol. 62 (2), pp. 297-307. - Publication Year :
- 1990
-
Abstract
- A 25 residue peptide, Dk-(61-85), derived from the alpha 1 domain of a murine MHC class I molecule (H-2Dk), enhances cellular glucose uptake, prolongs the effect of insulin, and inhibits insulin receptor internalization without affecting insulin binding or dissociation. Full effect of the peptide is obtained at 10-100 microM. The magnitude of the peptide-mediated enhancement of glucose uptake is insulin dependent and is at maximum approximately 50% above that of full insulin stimulation, excluding a merely insulinomimetic action of the peptide. Dk-(61-85) does not interact directly with the glucose transporter molecule. Furthermore, the peptide-mediated inhibition of insulin receptor internalization results in 2-3 times more receptors in the plasma membrane. The peptide also causes hypoglycemia in rats. The biological activity of Dk-(61-85) suggests that an important nonimmunological role of MHC class I molecules is to affect some of the key functions of ligand-activated receptors.
- Subjects :
- Amino Acid Sequence
Animals
Blood Glucose metabolism
Endocytosis
Glucose metabolism
Insulin physiology
Molecular Sequence Data
Monosaccharide Transport Proteins metabolism
Peptide Fragments chemical synthesis
Rats
Rats, Inbred Strains
Structure-Activity Relationship
H-2 Antigens physiology
Receptor, Insulin physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0092-8674
- Volume :
- 62
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Cell
- Publication Type :
- Academic Journal
- Accession number :
- 2196997
- Full Text :
- https://doi.org/10.1016/0092-8674(90)90367-n