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Paired measurements of paraoxonase 1 and serum amyloid A as useful disease markers.

Kotani K, Yamada T, Gugliucci A - Biomed Res Int (2013)

Bottom Line: Among the HDL-associated protein molecules, SAA, an inflammation-related marker, and PON1, an antioxidant marker, tend to change in relatively clear opposite directions in physiological situations.From the findings of experimental studies, PON1 appears to be cooperatively regulated by inflammation- and oxidative stress-related molecules linked with SAA regulation in humans.More studies remain to be performed to ascertain the value of paired measurements of both promising markers in clinical practice.

View Article: PubMed Central - PubMed

Affiliation: Department of Clinical Laboratory Medicine, Jichi Medical University, Shimotsuke-shi, Tochigi 329-0498, Japan ; Glycation, Oxidation and Disease Laboratory, Touro University-California, Vallejo, CA 94592, USA.

ABSTRACT
Paraoxonase 1 (PON1) and serum amyloid A (SAA) are proteins carried by high-density lipoprotein (HDL) particles. Among the HDL-associated protein molecules, SAA, an inflammation-related marker, and PON1, an antioxidant marker, tend to change in relatively clear opposite directions in physiological situations. In clinical chemistry, paired measurements of both markers may provide useful information to understand dysfunctional HDL in diseases with inflammation and oxidative stress conditions. Actually, limited clinical studies have suggested that the combined use of PON1 and SAA may be a tool for observing the pathophysiology of some disease entities. From the findings of experimental studies, PON1 appears to be cooperatively regulated by inflammation- and oxidative stress-related molecules linked with SAA regulation in humans. More studies remain to be performed to ascertain the value of paired measurements of both promising markers in clinical practice.

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Related in: MedlinePlus

A speculative interplay between PON1 and SAA in HDL particles. Apo-I: apolipoprotein A-I, HDL: high-density lipoprotein, PON1: paraoxonase 1, and SAA: serum amyloid A. Based on well-accepted evidence, chronic inflammation induces the secretion of SAA by the liver via cytokine signaling as depicted in (1). SAA may also stem from local extrahepatic synthesis at the site of atherosclerotic lesions (2). Under such conditions of increased SAA, a reduction of PON1 activity and apoA-I is seen in HDL particles. This renders a functionally deficient HDL particle (dysfunctional HDL) (3), for instance, which has less anti-inflammatory and antioxidant effects (4). Paired measurements of both SAA and PON1 may offer useful information on these pathways of dysfunctional HDL in several disease entities and deserve future basic and clinical studies as a potential biomarker pair (5).
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fig1: A speculative interplay between PON1 and SAA in HDL particles. Apo-I: apolipoprotein A-I, HDL: high-density lipoprotein, PON1: paraoxonase 1, and SAA: serum amyloid A. Based on well-accepted evidence, chronic inflammation induces the secretion of SAA by the liver via cytokine signaling as depicted in (1). SAA may also stem from local extrahepatic synthesis at the site of atherosclerotic lesions (2). Under such conditions of increased SAA, a reduction of PON1 activity and apoA-I is seen in HDL particles. This renders a functionally deficient HDL particle (dysfunctional HDL) (3), for instance, which has less anti-inflammatory and antioxidant effects (4). Paired measurements of both SAA and PON1 may offer useful information on these pathways of dysfunctional HDL in several disease entities and deserve future basic and clinical studies as a potential biomarker pair (5).

Mentions: Inflammation and oxidative stress are coexisting conditions underlying chronic diseases [20–22], and under such conditions, nascent native HDL particles can be converted into a more proatherogenic form of HDL particles [23, 24] with an altered complement of HDL-associated proteins, that is, an increase in SAA and a decrease in PON1. Because SAA, an inflammation-related marker, and PON1, an antioxidant marker, have relatively clear opposite characteristics among the HDL-associated proteins, the approach of assessing the two markers simultaneously may provide new insights in clinical practice (Figure 1).


Paired measurements of paraoxonase 1 and serum amyloid A as useful disease markers.

Kotani K, Yamada T, Gugliucci A - Biomed Res Int (2013)

A speculative interplay between PON1 and SAA in HDL particles. Apo-I: apolipoprotein A-I, HDL: high-density lipoprotein, PON1: paraoxonase 1, and SAA: serum amyloid A. Based on well-accepted evidence, chronic inflammation induces the secretion of SAA by the liver via cytokine signaling as depicted in (1). SAA may also stem from local extrahepatic synthesis at the site of atherosclerotic lesions (2). Under such conditions of increased SAA, a reduction of PON1 activity and apoA-I is seen in HDL particles. This renders a functionally deficient HDL particle (dysfunctional HDL) (3), for instance, which has less anti-inflammatory and antioxidant effects (4). Paired measurements of both SAA and PON1 may offer useful information on these pathways of dysfunctional HDL in several disease entities and deserve future basic and clinical studies as a potential biomarker pair (5).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3818810&req=5

fig1: A speculative interplay between PON1 and SAA in HDL particles. Apo-I: apolipoprotein A-I, HDL: high-density lipoprotein, PON1: paraoxonase 1, and SAA: serum amyloid A. Based on well-accepted evidence, chronic inflammation induces the secretion of SAA by the liver via cytokine signaling as depicted in (1). SAA may also stem from local extrahepatic synthesis at the site of atherosclerotic lesions (2). Under such conditions of increased SAA, a reduction of PON1 activity and apoA-I is seen in HDL particles. This renders a functionally deficient HDL particle (dysfunctional HDL) (3), for instance, which has less anti-inflammatory and antioxidant effects (4). Paired measurements of both SAA and PON1 may offer useful information on these pathways of dysfunctional HDL in several disease entities and deserve future basic and clinical studies as a potential biomarker pair (5).
Mentions: Inflammation and oxidative stress are coexisting conditions underlying chronic diseases [20–22], and under such conditions, nascent native HDL particles can be converted into a more proatherogenic form of HDL particles [23, 24] with an altered complement of HDL-associated proteins, that is, an increase in SAA and a decrease in PON1. Because SAA, an inflammation-related marker, and PON1, an antioxidant marker, have relatively clear opposite characteristics among the HDL-associated proteins, the approach of assessing the two markers simultaneously may provide new insights in clinical practice (Figure 1).

Bottom Line: Among the HDL-associated protein molecules, SAA, an inflammation-related marker, and PON1, an antioxidant marker, tend to change in relatively clear opposite directions in physiological situations.From the findings of experimental studies, PON1 appears to be cooperatively regulated by inflammation- and oxidative stress-related molecules linked with SAA regulation in humans.More studies remain to be performed to ascertain the value of paired measurements of both promising markers in clinical practice.

View Article: PubMed Central - PubMed

Affiliation: Department of Clinical Laboratory Medicine, Jichi Medical University, Shimotsuke-shi, Tochigi 329-0498, Japan ; Glycation, Oxidation and Disease Laboratory, Touro University-California, Vallejo, CA 94592, USA.

ABSTRACT
Paraoxonase 1 (PON1) and serum amyloid A (SAA) are proteins carried by high-density lipoprotein (HDL) particles. Among the HDL-associated protein molecules, SAA, an inflammation-related marker, and PON1, an antioxidant marker, tend to change in relatively clear opposite directions in physiological situations. In clinical chemistry, paired measurements of both markers may provide useful information to understand dysfunctional HDL in diseases with inflammation and oxidative stress conditions. Actually, limited clinical studies have suggested that the combined use of PON1 and SAA may be a tool for observing the pathophysiology of some disease entities. From the findings of experimental studies, PON1 appears to be cooperatively regulated by inflammation- and oxidative stress-related molecules linked with SAA regulation in humans. More studies remain to be performed to ascertain the value of paired measurements of both promising markers in clinical practice.

Show MeSH
Related in: MedlinePlus