Christine Bobin-Dubigeon1, Armelle Lefrançois2, Jean-Marc Classe3, Marie-Pierre Joalland2, Jean-Marie Bard4. 1. Institut de Cancérologie de l'Ouest-Biopathologie, Boulevard Jacques Monod 44805 Saint-Herblain, France; Université de Nantes, MMS - EA 2160 - Mer Molécules Santé, IUML - Institut Universitaire Mer et Littoral - FR3473 CNRS, France. 2. Institut de Cancérologie de l'Ouest-Biopathologie, Boulevard Jacques Monod 44805 Saint-Herblain, France. 3. Institut de Cancérologie de l'Ouest-Oncologie Chirurgicale, Boulevard Jacques Monod 44805 Saint-Herblain, France. 4. Institut de Cancérologie de l'Ouest-Biopathologie, Boulevard Jacques Monod 44805 Saint-Herblain, France; Université de Nantes, MMS - EA 2160 - Mer Molécules Santé, IUML - Institut Universitaire Mer et Littoral - FR3473 CNRS, France. Electronic address: jean-marie.bard@univ-nantes.fr.
Abstract
OBJECTIVES: Paraoxonase 1 (PON1) and serum amyloid A (SAA) are carried by HDL. In case of inflammation, SAA and PON1 tend to change in opposite direction. In this study we determined if inflammation leads to altered PON1 activity using three different substrate hydrolysis rates, paraoxonase (PON), arylesterase (ARE) and lactonase (LAC) in breast cancer recurrence. DESIGN AND METHODS: 49 patients with a recurrence of breast cancer were analyzed for SAA, CRP, lipids, oxidized LDL, PON, ARE and LAC. Distribution of PON1 activities across the quartiles of CRP and SAA were compared by the Kruskal Wallis test. Non-parametric estimates of the survivor function were computed with Kaplan-Meier method. The association of SAA and ARE with short term death was assessed by logistic regression models. RESULTS: HDL and ARE decrease significantly across the quartiles of CRP. No significant differences were observed across SAA quartiles. The survival time was significantly related to the level of SAA (log rank: p<0.001) as well as the level of ARE (log rank: p=0.039). SAA and ARE were independently related to survival time below one year. CONCLUSIONS: PON1 does not seem to be directly affected by SAA, for any of the tested substrates, PON, ARE and LAC. The combined measurement of SAA and ARE could be a useful tool in this clinical situation, since they are independently related to short term death.
OBJECTIVES:Paraoxonase 1 (PON1) and serum amyloid A (SAA) are carried by HDL. In case of inflammation, SAA and PON1 tend to change in opposite direction. In this study we determined if inflammation leads to altered PON1 activity using three different substrate hydrolysis rates, paraoxonase (PON), arylesterase (ARE) and lactonase (LAC) in breast cancer recurrence. DESIGN AND METHODS: 49 patients with a recurrence of breast cancer were analyzed for SAA, CRP, lipids, oxidized LDL, PON, ARE and LAC. Distribution of PON1 activities across the quartiles of CRP and SAA were compared by the Kruskal Wallis test. Non-parametric estimates of the survivor function were computed with Kaplan-Meier method. The association of SAA and ARE with short term death was assessed by logistic regression models. RESULTS: HDL and ARE decrease significantly across the quartiles of CRP. No significant differences were observed across SAA quartiles. The survival time was significantly related to the level of SAA (log rank: p<0.001) as well as the level of ARE (log rank: p=0.039). SAA and ARE were independently related to survival time below one year. CONCLUSIONS:PON1 does not seem to be directly affected by SAA, for any of the tested substrates, PON, ARE and LAC. The combined measurement of SAA and ARE could be a useful tool in this clinical situation, since they are independently related to short term death.