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	<id>https://transhumanist.ru/index.php?action=history&amp;feed=atom&amp;title=PON3</id>
	<title>PON3 - История изменений</title>
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	<updated>2026-05-02T15:00:53Z</updated>
	<subtitle>История изменений этой страницы в вики</subtitle>
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		<id>https://transhumanist.ru/index.php?title=PON3&amp;diff=5055&amp;oldid=prev</id>
		<title>OdysseusBot: Новая страница: «Serum paraoxonase/lactonase 3 (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1)  ==Publications==  {{medline-entry |title=Expression and activity of paraoxonase 1 in human...»</title>
		<link rel="alternate" type="text/html" href="https://transhumanist.ru/index.php?title=PON3&amp;diff=5055&amp;oldid=prev"/>
		<updated>2021-05-12T13:27:16Z</updated>

		<summary type="html">&lt;p&gt;Новая страница: «Serum paraoxonase/lactonase 3 (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1)  ==Publications==  {{medline-entry |title=Expression and activity of paraoxonase 1 in human...»&lt;/p&gt;
&lt;p&gt;&lt;b&gt;Новая страница&lt;/b&gt;&lt;/p&gt;&lt;div&gt;Serum paraoxonase/lactonase 3 (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1)&lt;br /&gt;
&lt;br /&gt;
==Publications==&lt;br /&gt;
&lt;br /&gt;
{{medline-entry&lt;br /&gt;
|title=Expression and activity of paraoxonase 1 in human cataractous lens tissue.&lt;br /&gt;
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/19439227&lt;br /&gt;
|abstract=Paraoxonase 1 ([[PON1]]) is a high-density lipoprotein-associated enzyme that is believed to be involved in the protection against oxidative stress. There is evidence that paraoxonase activity is reduced in patients with diabetes and cataract. In the current study, we analyzed mRNA expression of [[PON1]] as well as other members of the paraoxonase family, [[PON2]] and [[PON3]], in human cataractous lens samples. Our results indicate that only [[PON1]] is expressed at the gene and protein levels in human lens tissues. We quantified MDA levels and measured [[PON1]] (paraoxonase/arylesterase) enzymatic activities in subjects suffering from cataract due to aging and diabetes. Decreased [[PON1]] activity was more pronounced in diabetic patients (p&amp;lt; 0.001) compared to senile subjects, which may be due to glycation and increased oxidative insult. To examine the structural alterations that occur in response to glycation, we constructed a three-dimensional model of [[PON1]] and its glycated variant. Glycation at Lys70 and Lys75 is predicted to cause hindrance in binding of substrate to the active site of the enzyme.&lt;br /&gt;
|mesh-terms=* Aged&lt;br /&gt;
* Aging&lt;br /&gt;
* Aryldialkylphosphatase&lt;br /&gt;
* Cataract&lt;br /&gt;
* Diabetes Mellitus, Type 2&lt;br /&gt;
* Esterases&lt;br /&gt;
* Female&lt;br /&gt;
* Gene Expression Regulation&lt;br /&gt;
* Glycation End Products, Advanced&lt;br /&gt;
* Humans&lt;br /&gt;
* Immunohistochemistry&lt;br /&gt;
* Lens, Crystalline&lt;br /&gt;
* Lipid Peroxidation&lt;br /&gt;
* Male&lt;br /&gt;
* Malondialdehyde&lt;br /&gt;
* Middle Aged&lt;br /&gt;
* Models, Chemical&lt;br /&gt;
* Oxidative Stress&lt;br /&gt;
* Substrate Specificity&lt;br /&gt;
&lt;br /&gt;
|full-text-url=https://sci-hub.do/10.1016/j.freeradbiomed.2009.01.012&lt;br /&gt;
}}&lt;/div&gt;</summary>
		<author><name>OdysseusBot</name></author>
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