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Amino acids differentially regulate insulin receptor tyrosine kinase and phosphatidyl inositol-3-OH-kinase activities in human monocytes exposed to high glucose concentration

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Title Amino acids differentially regulate insulin receptor tyrosine kinase and phosphatidyl inositol-3-OH-kinase activities in human monocytes exposed to high glucose concentration
 
Creator Srinivasan, V
Rajesh, M
Sulochana, K N
Indra, C
Ramakrishnan, S
 
Subject Diabetes mellitus
Insulin receptor tyrosine kinase
Phosphatidyl inositol-3-OH-kinase
Lysine and other amino acids
Monocytes
Glucose
Insulin signaling pathway
Actin dynamics
F-actin organization
 
Description 13-18
Chronic hyperglycemia and insulin resistance are
the common factors involved in the development of vascular complications in diabetes
mellitus (DM) patients. Since insulin signaling pathway has been shown to be regulated
by nutritional supplements, in the present study, we investigated the possible
effects of free amino acids, such as lysine, arginine and alanine and their mixture
in modulating the insulin receptor tyrosine kinase (IRTK) and phosphatidyl inositol-3-OH-kinase
(PI3K) activities and on the changes in actin dynamics in monocytes (MC), exposed
to high glucose

concentration (25 mM). IRTK and PI3K activities were markedly decreased in MC, incubated with 25 mM glucose. However, on treatment with amino acids, only
lysine was effective in augmenting IRTK and PI3K activities in a dose-dependent

manner. Arginine had marginal effect in promoting these
activities. Equimolar mixture of amino acids showed marginal effect of augmenting
only IRTK activity. Alanine had no effect. The F-actin filaments showed grossly
diminished

organization in the cells treated with 25 mM glucose alone, as assessed by specific binding to phalloidin-FITC,
when compared with cells treated with 5 mM glucose. On the other hand, a significant improvement in the F-actin organization
was observed in the cells co-incubated with 25 mM glucose and lysine. A possible molecular mechanism is the antiglycating effect
of amino acids. The signal transduction starts with binding of ATP to lysine at
position 1030 in the β sub unit of the receptor. This
lysine (1030) may be protected by the added lysine or to some extent arginine
from glycation and loss of function. In summary, our findings suggest that the
amino acids apart from their antiglycating property can also modulate/influence
the activities of pivotal enzymes that are upstream in the insulin-mediated signal
transduction pathway

and bring down glucose.
 
Date 2015-01-16T11:29:29Z
2015-01-16T11:29:29Z
2005-02
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/30376
 
Language en_US
 
Relation C 12 Q 1/54
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.42(1) [February 2005]