scholarly journals Evaluation of lipoprotein‐associated phospholipase A2, serum amyloid A, and fibrinogen as diagnostic biomarkers for patients with acute cerebral infarction

2020 ◽  
Vol 34 (3) ◽  
Author(s):  
Liang Tao ◽  
Wang ShiChuan ◽  
Zhang DeTai ◽  
Hu Lihua
Keyword(s):  
Cerebral Infarction ◽  
Phospholipase A2 ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Acute Cerebral Infarction ◽  
Diagnostic Biomarkers ◽  
Amyloid A

Serum amyloid A, phospholipase A2-IIA and C-reactive protein as inflammatory biomarkers for prostate diseases

2013 ◽  
Vol 62 (12) ◽  
pp. 1063-1072 ◽  
Author(s):  
Mario Menschikowski ◽  
Albert Hagelgans ◽  
Susanne Fuessel ◽  
Olga A. Mareninova ◽  
Liana Asatryan ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Inflammatory Biomarkers ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Amyloid A ◽  
Prostate Diseases

Serum amyloid A stimulates lipoprotein-associated phospholipase A2 expression in vitro and in vivo

2013 ◽  
Vol 228 (2) ◽  
pp. 370-379 ◽  
Author(s):  
Bo Li ◽  
Zhe Dong ◽  
Hui Liu ◽  
Yan-fei Xia ◽  
Xiao-man Liu ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

scholarly journals Serum amyloid A protein enhances the activity of secretory non-pancreatic phospholipase A2

1995 ◽  
Vol 309 (2) ◽  
pp. 461-464 ◽  
Author(s):  
W Pruzanski ◽  
F C de Beer ◽  
M C de Beer ◽  
E Stefanski ◽  
P Vadas
Keyword(s):  
Phospholipase A2 ◽  
Acute Phase ◽  
Serum Amyloid A ◽  
Acute Phase Proteins ◽  
Lipolytic Activity ◽  
Lipoprotein Metabolism ◽  
Serum Amyloid ◽  
Dependent Manner ◽  
Amyloid A ◽  
Serum Amyloid A Protein

The acute-phase proteins serum amyloid A protein (SAA) and secretory phospholipase A2 (sPLA2) are simultaneously expressed during inflammatory conditions. SAA associates with high-density lipoprotein (HDL) altering its physicochemical composition. We found that purified acute-phase SAA, but not the constitutive form, markedly enhances the lipolytic activity of sPLA2 in a dose-related manner with phosphatidylcholine/lysophosphatidylcholine or phosphatidylethanolamine/lysophosphatidylethanolamine liposomal substrates. Normal HDL was found to reduce activity of sPLA2 in a dose-dependent manner, but when acute-phase HDL containing 27% SAA was tested, it enhanced sPLA2 activity. Immunopurified monospecific antibodies against SAA completely abolished the enhancing activity of SAA and acute-phase HDL. Given the central role of HDL in lipoprotein metabolism, the interaction between HDL, SAA and sPLA2 may account for changes detected in lipoprotein metabolism during the acute phase.

scholarly journals Serum Amyloid A and Lipoprotein Associated Phospholipase A2 Levels in Patients with Malign Melanoma: Correlations with Clinical Assessment and Stage

2018 ◽  
Vol 12 (3) ◽  
pp. 135-142
Author(s):  
Yavuz Kayaş ◽  
Ferhan Sağın ◽  
Yasemin Akçay ◽  
Gizem Kocabaş Yenipazar ◽  
Elif Azarsız ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Clinical Assessment ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

scholarly journals Synergy between serum amyloid A and secretory phospholipase A2

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Shobini Jayaraman ◽  
Marcus Fändrich ◽  
Olga Gursky
Keyword(s):  
Fatty Acids ◽  
Phospholipase A2 ◽  
Free Fatty Acids ◽  
Lipid Bilayers ◽  
Serum Amyloid A ◽  
Degradation Products ◽  
Serum Amyloid ◽  
Secretory Phospholipase A2 ◽  
Secretory Phospholipase ◽  
Amyloid A

Serum amyloid A (SAA) is an evolutionally conserved enigmatic biomarker of inflammation. In acute inflammation, SAA plasma levels increase ~1,000 fold, suggesting that this protein family has a vital beneficial role. SAA increases simultaneously with secretory phospholipase A2 (sPLA2), compelling us to determine how SAA influences sPLA2 hydrolysis of lipoproteins. SAA solubilized phospholipid bilayers to form lipoproteins that provided substrates for sPLA2. Moreover, SAA sequestered free fatty acids and lysophospholipids to form stable proteolysis-resistant complexes. Unlike albumin, SAA effectively removed free fatty acids under acidic conditions, which characterize inflammation sites. Therefore, SAA solubilized lipid bilayers to generate substrates for sPLA2 and removed its bioactive products. Consequently, SAA and sPLA2 can act synergistically to remove cellular membrane debris from injured sites, which is a prerequisite for tissue healing. We postulate that the removal of lipids and their degradation products constitutes a vital primordial role of SAA in innate immunity; this role remains to be tested in vivo.

scholarly journals Secretory Phospholipase A2, Group IIA Is a Novel Serum Amyloid A Target Gene

2009 ◽  
Vol 285 (1) ◽  
pp. 565-575 ◽  
Author(s):  
Christopher P. Sullivan ◽  
Stephanie E. Seidl ◽  
Celeste B. Rich ◽  
Michel Raymondjean ◽  
Barbara M. Schreiber
Keyword(s):  
Phospholipase A2 ◽  
Target Gene ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Secretory Phospholipase A2 ◽  
Secretory Phospholipase ◽  
Amyloid A ◽  
Phospholipase A2 Group Iia
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