Association of serum amyloid A and oxidative stress with paraoxonase 1 in sarcoidosis patients
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2016
Authors
Ivanišević, Jasmina
Kotur-Stevuljević, Jelena

Stefanović, Aleksandra

Spasić, Slavica
Vučinić-Mihailović, Violeta
Videnović-Ivanov, Jelica
Jelić-Ivanović, Zorana

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Background It has been reported that high-density lipoprotein (HDL) particles have anti-inflammatory and antioxidant roles thanks to different enzymes such as paraoxonase 1 (PON1). Under inflammatory and oxidative stress conditions, HDL particles may lose their protective properties. Sarcoidosis is an inflammatory disease characterized by excessive oxidative stress. Serum amyloid A (SAA) is produced in liver and in granulomas, and its concentration increases in inflammatory conditions contributing to increased catabolism of HDL particles. The aim of our study was to determine PON1 activity, SAA concentration and their associations in patients with sarcoidosis. Materials and methods Inflammatory [high-sensitive C-reactive protein (hsCRP), angiotensin-converting enzyme (ACE), SAA], lipid [total cholesterol (TC), HDL-cholesterol (HDL-c), low-density lipoprotein cholesterol (LDL-c), triglycerides (TG)] oxidative stress status parameters [total oxidant status (TOS), malondialdehyde (MDA), p...ro-oxidant-antioxidant balance (PAB), sulfhydryl (SH) groups] and PON1 activities were determined in serum of 72 patients with sarcoidosis and 62 healthy subjects. Results HsCRP (P lt 0.05), TC, LDL-c, TG, SAA, TOS, MDA and PAB (P lt 0.001) were significantly higher, whereas HDL-c, SH groups and PON1 activity (P lt 0.001) were significantly lower in patients with sarcoidosis when compared with controls. PON1 showed significant association with SAA, MDA and PAB. It was shown that 71% of decrease in PON1 activity may be explained by increase in TOS, PAB and SAA concentration. Conclusions We found decreased PON1 activity and increased SAA concentration in patients with sarcoidosis. Inflammatory condition presented by high SAA was implicated in impaired HDL functionality evident through dysregulated PON1 activity. Excessive oxidative stress was also involved in dysregulation of PON1 activity.
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European Journal of Clinical Investigation, 2016, 46, 5, 418-424Publisher:
- Wiley-Blackwell, Hoboken
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DOI: 10.1111/eci.12610
ISSN: 0014-2972
PubMed: 26919159
WoS: 000374651600006
Scopus: 2-s2.0-84960894929
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PharmacyTY - JOUR AU - Ivanišević, Jasmina AU - Kotur-Stevuljević, Jelena AU - Stefanović, Aleksandra AU - Spasić, Slavica AU - Vučinić-Mihailović, Violeta AU - Videnović-Ivanov, Jelica AU - Jelić-Ivanović, Zorana PY - 2016 UR - https://farfar.pharmacy.bg.ac.rs/handle/123456789/2594 AB - Background It has been reported that high-density lipoprotein (HDL) particles have anti-inflammatory and antioxidant roles thanks to different enzymes such as paraoxonase 1 (PON1). Under inflammatory and oxidative stress conditions, HDL particles may lose their protective properties. Sarcoidosis is an inflammatory disease characterized by excessive oxidative stress. Serum amyloid A (SAA) is produced in liver and in granulomas, and its concentration increases in inflammatory conditions contributing to increased catabolism of HDL particles. The aim of our study was to determine PON1 activity, SAA concentration and their associations in patients with sarcoidosis. Materials and methods Inflammatory [high-sensitive C-reactive protein (hsCRP), angiotensin-converting enzyme (ACE), SAA], lipid [total cholesterol (TC), HDL-cholesterol (HDL-c), low-density lipoprotein cholesterol (LDL-c), triglycerides (TG)] oxidative stress status parameters [total oxidant status (TOS), malondialdehyde (MDA), pro-oxidant-antioxidant balance (PAB), sulfhydryl (SH) groups] and PON1 activities were determined in serum of 72 patients with sarcoidosis and 62 healthy subjects. Results HsCRP (P lt 0.05), TC, LDL-c, TG, SAA, TOS, MDA and PAB (P lt 0.001) were significantly higher, whereas HDL-c, SH groups and PON1 activity (P lt 0.001) were significantly lower in patients with sarcoidosis when compared with controls. PON1 showed significant association with SAA, MDA and PAB. It was shown that 71% of decrease in PON1 activity may be explained by increase in TOS, PAB and SAA concentration. Conclusions We found decreased PON1 activity and increased SAA concentration in patients with sarcoidosis. Inflammatory condition presented by high SAA was implicated in impaired HDL functionality evident through dysregulated PON1 activity. Excessive oxidative stress was also involved in dysregulation of PON1 activity. PB - Wiley-Blackwell, Hoboken T2 - European Journal of Clinical Investigation T1 - Association of serum amyloid A and oxidative stress with paraoxonase 1 in sarcoidosis patients VL - 46 IS - 5 SP - 418 EP - 424 DO - 10.1111/eci.12610 ER -
@article{ author = "Ivanišević, Jasmina and Kotur-Stevuljević, Jelena and Stefanović, Aleksandra and Spasić, Slavica and Vučinić-Mihailović, Violeta and Videnović-Ivanov, Jelica and Jelić-Ivanović, Zorana", year = "2016", abstract = "Background It has been reported that high-density lipoprotein (HDL) particles have anti-inflammatory and antioxidant roles thanks to different enzymes such as paraoxonase 1 (PON1). Under inflammatory and oxidative stress conditions, HDL particles may lose their protective properties. Sarcoidosis is an inflammatory disease characterized by excessive oxidative stress. Serum amyloid A (SAA) is produced in liver and in granulomas, and its concentration increases in inflammatory conditions contributing to increased catabolism of HDL particles. The aim of our study was to determine PON1 activity, SAA concentration and their associations in patients with sarcoidosis. Materials and methods Inflammatory [high-sensitive C-reactive protein (hsCRP), angiotensin-converting enzyme (ACE), SAA], lipid [total cholesterol (TC), HDL-cholesterol (HDL-c), low-density lipoprotein cholesterol (LDL-c), triglycerides (TG)] oxidative stress status parameters [total oxidant status (TOS), malondialdehyde (MDA), pro-oxidant-antioxidant balance (PAB), sulfhydryl (SH) groups] and PON1 activities were determined in serum of 72 patients with sarcoidosis and 62 healthy subjects. Results HsCRP (P lt 0.05), TC, LDL-c, TG, SAA, TOS, MDA and PAB (P lt 0.001) were significantly higher, whereas HDL-c, SH groups and PON1 activity (P lt 0.001) were significantly lower in patients with sarcoidosis when compared with controls. PON1 showed significant association with SAA, MDA and PAB. It was shown that 71% of decrease in PON1 activity may be explained by increase in TOS, PAB and SAA concentration. Conclusions We found decreased PON1 activity and increased SAA concentration in patients with sarcoidosis. Inflammatory condition presented by high SAA was implicated in impaired HDL functionality evident through dysregulated PON1 activity. Excessive oxidative stress was also involved in dysregulation of PON1 activity.", publisher = "Wiley-Blackwell, Hoboken", journal = "European Journal of Clinical Investigation", title = "Association of serum amyloid A and oxidative stress with paraoxonase 1 in sarcoidosis patients", volume = "46", number = "5", pages = "418-424", doi = "10.1111/eci.12610" }
Ivanišević, J., Kotur-Stevuljević, J., Stefanović, A., Spasić, S., Vučinić-Mihailović, V., Videnović-Ivanov, J.,& Jelić-Ivanović, Z.. (2016). Association of serum amyloid A and oxidative stress with paraoxonase 1 in sarcoidosis patients. in European Journal of Clinical Investigation Wiley-Blackwell, Hoboken., 46(5), 418-424. https://doi.org/10.1111/eci.12610
Ivanišević J, Kotur-Stevuljević J, Stefanović A, Spasić S, Vučinić-Mihailović V, Videnović-Ivanov J, Jelić-Ivanović Z. Association of serum amyloid A and oxidative stress with paraoxonase 1 in sarcoidosis patients. in European Journal of Clinical Investigation. 2016;46(5):418-424. doi:10.1111/eci.12610 .
Ivanišević, Jasmina, Kotur-Stevuljević, Jelena, Stefanović, Aleksandra, Spasić, Slavica, Vučinić-Mihailović, Violeta, Videnović-Ivanov, Jelica, Jelić-Ivanović, Zorana, "Association of serum amyloid A and oxidative stress with paraoxonase 1 in sarcoidosis patients" in European Journal of Clinical Investigation, 46, no. 5 (2016):418-424, https://doi.org/10.1111/eci.12610 . .