INT275758

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Context Info
Confidence 0.03
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 9
Disease Relevance 5.39
Pain Relevance 0.04

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

extracellular space (Igfbp3) extracellular region (Igfbp3) nucleus (Igfbp3)
Anatomy Link Frequency
hypothalamus 1
xn (Mus musculus)
Igfbp3 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Potency 18 87.52 High High
vagus nerve 9 25.28 Quite Low
anesthesia 9 10.64 Low Low
Somatostatin 9 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Apoptosis 135 100.00 Very High Very High Very High
Death 36 99.08 Very High Very High Very High
Disease 225 98.76 Very High Very High Very High
Insulin Resistance 45 98.48 Very High Very High Very High
Stroke 9 96.16 Very High Very High Very High
Cognitive Disorder 36 95.52 Very High Very High Very High
Pheochromocytoma 9 89.56 High High
Targeted Disruption 9 84.08 Quite High
Diabetes Mellitus 162 75.04 Quite High
Amyloid Plaque 9 72.60 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Furthermore, we show that the effects of HN on glucose metabolism are tempered by binding of HN to IGFBP-3 in the hypothalamus, as central infusion of a non-IGFBP-3 binding analog, F6AHN, resulted in a more potent effect on insulin action than HN.
HN Binding (binding) of IGFBP-3 in hypothalamus
1) Confidence 0.03 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709436 Disease Relevance 0.14 Pain Relevance 0
A substitution of phenylalanine in the 6th position with alanine (F6A, F6AHN) alters the binding of HN to IGFBP-3 and we show here that this substitution significantly enhances its central effect on glucose metabolism.
HN Binding (binding) of IGFBP-3
2) Confidence 0.03 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709436 Disease Relevance 0.78 Pain Relevance 0.04
We have separately shown that IGFBP-3 also binds HN and antagonizes its survival effects [11].
HN Binding (binds) of IGFBP-3
3) Confidence 0.03 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709436 Disease Relevance 0.14 Pain Relevance 0
In a series of experiments, we examined the role of HN in glucose metabolism and its potential mechanism of action, including its interaction with IGFBP-3, by using HN and a variety of HN analogs.
HN Binding (interaction) of IGFBP-3
4) Confidence 0.02 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709436 Disease Relevance 0.59 Pain Relevance 0
The interaction between HN and IGFBP-3 is especially interesting since IGFBP-3 and HN have opposing roles on cell survival, such that HN protects against while IGFBP-3 induces cell death [17].
HN Binding (interaction) of IGFBP-3 associated with death
5) Confidence 0.02 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709436 Disease Relevance 0.85 Pain Relevance 0
Once dimerized, HN directly interacts with a variety of pro-apoptotic proteins, including Bax-related proteins [2] and insulin-like growth factor binding protein-3 (IGFBP-3) [11].
HN Binding (interacts) of IGFBP-3 associated with apoptosis
6) Confidence 0.02 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709436 Disease Relevance 1.33 Pain Relevance 0
Based upon the molecular interaction between HN and IGFBP-3 and the emerging link between AD and insulin resistance [20], we hypothesized that HN, in addition to its neuroprotective roles, may serve as a centrally-acting regulator of glucose homeostasis.
HN Binding (interaction) of IGFBP-3 associated with insulin resistance and disease
7) Confidence 0.02 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709436 Disease Relevance 0.58 Pain Relevance 0
To assess if IGFBP-3 attenuates the effects of HN on insulin action, we utilized a series of HN analogues that do not bind to IGFBP-3 (Fig. 4A).
HN Binding (bind) of IGFBP-3
8) Confidence 0.02 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709436 Disease Relevance 0.17 Pain Relevance 0
We previously demonstrated that HN physically binds with IGFBP-3 and that this interaction prevents the activation of caspases [11].
HN Binding (binds) of IGFBP-3
9) Confidence 0.02 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709436 Disease Relevance 0.79 Pain Relevance 0

General Comments

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