Modulation of 125I-insulin degradation by receptors in liver plasma membranes

Lanyard K. Dial, Suzanne Miyamoto, Edward R. Arquilla

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

This study investigated the interactions of insulin with receptors in a purified mouse liver plasma membrane. Two processes were found when insulin was incubated with the liver plasma membranes at 30°C; 1) the binding of insulin to these membranes and 2) the degradation of insulin by one or more associated insulinases or proteases. These two activities were physically separated, analyzed, and it was found that bound insulin is a substrate for insulin degradation. In addition, the rate of degradation of free insulin in solution was found to be 1.1% degraded insulin/available insulin/min in a 30 minute period. This rate is compared to 25.3% degraded insulin/available insulin/min under similar conditions when insulin is bound to the plasma membranes. Thus, insulin binding was shown to aid in its degradation. These results suggest that a specific binding by at least one of the receptors for insulin orients the molecule such that its degradation is facilitated.

Original languageEnglish (US)
Pages (from-to)545-552
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume74
Issue number2
DOIs
StatePublished - Jan 24 1977
Externally publishedYes

Fingerprint

Insulin Receptor
Cell membranes
Liver
Cell Membrane
Modulation
Insulin
Degradation
Insulysin
Peptide Hydrolases

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Modulation of 125I-insulin degradation by receptors in liver plasma membranes. / Dial, Lanyard K.; Miyamoto, Suzanne; Arquilla, Edward R.

In: Biochemical and Biophysical Research Communications, Vol. 74, No. 2, 24.01.1977, p. 545-552.

Research output: Contribution to journalArticle

Dial, Lanyard K. ; Miyamoto, Suzanne ; Arquilla, Edward R. / Modulation of 125I-insulin degradation by receptors in liver plasma membranes. In: Biochemical and Biophysical Research Communications. 1977 ; Vol. 74, No. 2. pp. 545-552.
@article{0111fa83d3ea4db3a3bd0ab5e3b622de,
title = "Modulation of 125I-insulin degradation by receptors in liver plasma membranes",
abstract = "This study investigated the interactions of insulin with receptors in a purified mouse liver plasma membrane. Two processes were found when insulin was incubated with the liver plasma membranes at 30°C; 1) the binding of insulin to these membranes and 2) the degradation of insulin by one or more associated insulinases or proteases. These two activities were physically separated, analyzed, and it was found that bound insulin is a substrate for insulin degradation. In addition, the rate of degradation of free insulin in solution was found to be 1.1{\%} degraded insulin/available insulin/min in a 30 minute period. This rate is compared to 25.3{\%} degraded insulin/available insulin/min under similar conditions when insulin is bound to the plasma membranes. Thus, insulin binding was shown to aid in its degradation. These results suggest that a specific binding by at least one of the receptors for insulin orients the molecule such that its degradation is facilitated.",
author = "Dial, {Lanyard K.} and Suzanne Miyamoto and Arquilla, {Edward R.}",
year = "1977",
month = "1",
day = "24",
doi = "10.1016/0006-291X(77)90338-2",
language = "English (US)",
volume = "74",
pages = "545--552",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Modulation of 125I-insulin degradation by receptors in liver plasma membranes

AU - Dial, Lanyard K.

AU - Miyamoto, Suzanne

AU - Arquilla, Edward R.

PY - 1977/1/24

Y1 - 1977/1/24

N2 - This study investigated the interactions of insulin with receptors in a purified mouse liver plasma membrane. Two processes were found when insulin was incubated with the liver plasma membranes at 30°C; 1) the binding of insulin to these membranes and 2) the degradation of insulin by one or more associated insulinases or proteases. These two activities were physically separated, analyzed, and it was found that bound insulin is a substrate for insulin degradation. In addition, the rate of degradation of free insulin in solution was found to be 1.1% degraded insulin/available insulin/min in a 30 minute period. This rate is compared to 25.3% degraded insulin/available insulin/min under similar conditions when insulin is bound to the plasma membranes. Thus, insulin binding was shown to aid in its degradation. These results suggest that a specific binding by at least one of the receptors for insulin orients the molecule such that its degradation is facilitated.

AB - This study investigated the interactions of insulin with receptors in a purified mouse liver plasma membrane. Two processes were found when insulin was incubated with the liver plasma membranes at 30°C; 1) the binding of insulin to these membranes and 2) the degradation of insulin by one or more associated insulinases or proteases. These two activities were physically separated, analyzed, and it was found that bound insulin is a substrate for insulin degradation. In addition, the rate of degradation of free insulin in solution was found to be 1.1% degraded insulin/available insulin/min in a 30 minute period. This rate is compared to 25.3% degraded insulin/available insulin/min under similar conditions when insulin is bound to the plasma membranes. Thus, insulin binding was shown to aid in its degradation. These results suggest that a specific binding by at least one of the receptors for insulin orients the molecule such that its degradation is facilitated.

UR - http://www.scopus.com/inward/record.url?scp=0017367139&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017367139&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(77)90338-2

DO - 10.1016/0006-291X(77)90338-2

M3 - Article

VL - 74

SP - 545

EP - 552

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -