INT238854

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Context Info
Confidence 0.73
First Reported 2008
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 39
Total Number 40
Disease Relevance 21.89
Pain Relevance 1.13

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

cytosol (LIPE) extracellular space (LIPE) small molecule metabolic process (LIPE)
lipid particle (LIPE) plasma membrane (LIPE) lipid metabolic process (LIPE)
Anatomy Link Frequency
skeletal muscle 8
muscle 6
adipocyte 2
LIPE (Homo sapiens)
Pain Link Frequency Relevance Heat
Catecholamine 161 98.32 Very High Very High Very High
agonist 191 84.12 Quite High
noradrenaline 28 37.84 Quite Low
anesthesia 43 5.00 Very Low Very Low Very Low
alcohol 38 5.00 Very Low Very Low Very Low
lidocaine 1 5.00 Very Low Very Low Very Low
withdrawal 1 5.00 Very Low Very Low Very Low
local anesthetic 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Obesity 3993 99.84 Very High Very High Very High
Hyperinsulinism 38 87.48 High High
Diabetes Mellitus 76 64.76 Quite High
Weight Loss 37 64.08 Quite High
Insulin Resistance 113 53.64 Quite High
Natriuresis 7 50.00 Quite Low
Sprains And Strains 37 40.76 Quite Low
Hyperglycemia 1 36.80 Quite Low
Rheumatoid Arthritis 185 5.00 Very Low Very Low Very Low
Heart Rate Under Development 44 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The absence of correlation between protein expression and mRNA level suggests that HSL may be regulated at some post-transcriptional levels (such as phosphorylation which activates HSL activity and induces HSL translocation from the cytosol to the lipid droplet upon adipocyte stimulation [3]).
Phosphorylation (phosphorylation) of HSL in adipocyte
1) Confidence 0.73 Published 2009 Journal Lipids Health Dis Section Body Doc Link PMC2804660 Disease Relevance 0.68 Pain Relevance 0.04
-adrenergic agents, perilipins phosphorylation in response to PKA activation induces an important physical alteration of the droplet surface that facilitates the action of phosphorylated lipases such as HSL and initiates lipolysis [6-8].
Phosphorylation (phosphorylated) of HSL
2) Confidence 0.64 Published 2009 Journal Lipids Health Dis Section Body Doc Link PMC2804660 Disease Relevance 0.88 Pain Relevance 0.06
It should be recognized, however, that when corrected for total HSL protein, HSL Ser563, Ser565, and Ser659 phosphorylation was comparable between lean and obese subjects, suggesting that a similar percentage of HSL molecules was phosphorylated on these three serine sites in lean and obese subjects.
Phosphorylation (phosphorylation) of HSL Ser563 associated with obesity
3) Confidence 0.53 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.92 Pain Relevance 0
In vitro studies on purified bovine adipocyte HSL have shown that AMP-activated protein kinase (AMPK) phosphorylates HSL on Ser565, thereby abolishing PKA-induced HSL activation (15).
Phosphorylation (phosphorylates) of HSL in adipocyte
4) Confidence 0.53 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.06 Pain Relevance 0.08
On the other hand, HSL Ser563 and Ser565 phosphorylation have been suggested not to be major regulators of HSL activity in human skeletal muscle (11,13).
Phosphorylation (phosphorylation) of HSL Ser563 in skeletal muscle
5) Confidence 0.53 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.71 Pain Relevance 0
Ser659 appears to be a likely candidate because HSL Ser659 phosphorylation and HSL activity show a similar response to exercise with concomitant increase in circulating epinephrine (13).
Phosphorylation (phosphorylation) of HSL
6) Confidence 0.53 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.11 Pain Relevance 0.12
Furthermore, our data suggest that phosphorylation of HSL on the PKA target sites Ser563 and Ser659, and on the AMPK target site Ser565, was lower in obese than in lean subjects.
Phosphorylation (phosphorylation) of HSL associated with obesity
7) Confidence 0.53 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.98 Pain Relevance 0
Ser659 appears to be a likely candidate because HSL Ser659 phosphorylation and HSL activity show a similar response to exercise with concomitant increase in circulating epinephrine (13).
Phosphorylation (phosphorylation) of HSL Ser659
8) Confidence 0.53 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.11 Pain Relevance 0.12
Expression of HSL protein and phosphorylation of HSL Ser563, Ser565, and Ser659 was detected by Western blotting on the muscle lysates.
Phosphorylation (phosphorylation) of HSL Ser563 in muscle
9) Confidence 0.53 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.07 Pain Relevance 0
Thus, the reduced phosphorylation of HSL on these two sites may not have been important in determining the blunted baseline lipolysis in obese subjects.
Phosphorylation (phosphorylation) of HSL associated with obesity
10) Confidence 0.53 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.58 Pain Relevance 0
This was accompanied by lower HSL protein expression (P = 0.004), HSL phosphorylation on PKA sites Ser563 (P = 0.041) and Ser659 (P = 0.09), and HSL phosphorylation on the AMPK site Ser565 (P = 0.007), suggesting a blunted skeletal muscle lipolysis in obesity.
Phosphorylation (phosphorylation) of HSL in skeletal muscle associated with obesity
11) Confidence 0.53 Published 2008 Journal Diabetes Section Abstract Doc Link PMC2453623 Disease Relevance 0.67 Pain Relevance 0.04
It can be speculated that obese subjects increase HSL Ser659 phosphorylation during ?
Phosphorylation (phosphorylation) of HSL Ser659 associated with obesity
12) Confidence 0.53 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.34 Pain Relevance 0
This was accompanied by lower HSL protein expression (P = 0.004), HSL phosphorylation on PKA sites Ser563 (P = 0.041) and Ser659 (P = 0.09), and HSL phosphorylation on the AMPK site Ser565 (P = 0.007), suggesting a blunted skeletal muscle lipolysis in obesity.
Phosphorylation (phosphorylation) of HSL in skeletal muscle associated with obesity
13) Confidence 0.53 Published 2008 Journal Diabetes Section Abstract Doc Link PMC2453623 Disease Relevance 0.61 Pain Relevance 0.04
It has been demonstrated that skeletal muscle HSL can be phosphorylated on at least five serine residues (Ser563, Ser565, Ser600, Ser659, and Ser660) (11–13).
Phosphorylation (phosphorylated) of HSL in skeletal muscle
14) Confidence 0.46 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.34 Pain Relevance 0.12
In the present study, HSL Ser659 phosphorylation significantly increased during ?
Phosphorylation (phosphorylation) of HSL Ser659
15) Confidence 0.46 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.30 Pain Relevance 0
In contrast to lean subjects, an increased HSL Ser659 phosphorylation was observed in skeletal muscle of obese subjects during ?
Phosphorylation (phosphorylation) of HSL Ser659 in skeletal muscle associated with obesity
16) Confidence 0.46 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.83 Pain Relevance 0
This is in accordance with previous studies, in which HSL Ser563 phosphorylation was not increased during exercise despite an increase in circulating epinephrine (11,13).
Phosphorylation (phosphorylation) of HSL Ser563
17) Confidence 0.46 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.33 Pain Relevance 0
Interestingly, this was accompanied by an increase in HSL Ser659 phosphorylation in obese subjects during ISO compared with baseline (P = 0.008).
Phosphorylation (phosphorylation) of HSL Ser659 associated with obesity
18) Confidence 0.46 Published 2008 Journal Diabetes Section Abstract Doc Link PMC2453623 Disease Relevance 0.63 Pain Relevance 0.03
Maybe HSL Ser563 is already maximally phosphorylated in the basal, resting state.
Phosphorylation (phosphorylated) of HSL Ser563
19) Confidence 0.46 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.44 Pain Relevance 0
In human skeletal muscle, changes in AMPK activity during exercise were also associated with an increased HSL Ser565 phosphorylation, but this was not accompanied by an increased HSL activity, suggesting that AMPK can phosphorylate HSL on Ser565 but that AMPK is of minor importance as a regulator of HSL activity in human skeletal muscle during exercise (11).
Phosphorylation (phosphorylation) of HSL Ser565 in skeletal muscle
20) Confidence 0.46 Published 2008 Journal Diabetes Section Body Doc Link PMC2453623 Disease Relevance 0.13 Pain Relevance 0.10

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