scholarly journals Type 2 Diabetes in Young Females Results in Increased Serum Amyloid A and Changes to Features of High Density Lipoproteins in Both HDL2 and HDL3

2017 ◽  
Vol 2017 ◽  
pp. 1-9 ◽  
Author(s):  
Kayleigh Griffiths ◽  
Agnieszka Pazderska ◽  
Mohammed Ahmed ◽  
Anne McGowan ◽  
Alexander P. Maxwell ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Serum Amyloid A ◽  
High Density ◽  
Serum Amyloid ◽  
Paraoxonase 1 ◽  
High Density Lipoproteins ◽  
Cvd Risk ◽  
Young Females ◽  
Amyloid A

Persons with type 2 diabetes mellitus (T2DM) have an elevated risk of atherosclerosis. High-density lipoproteins (HDL) normally protect against cardiovascular disease (CVD), but this may be attenuated by serum amyloid A (SAA). In a case-control study of young females, blood samples were compared between subjects with T2DM (n=42) and individuals without T2DM (n=42). SAA and apolipoprotein AI (apoAI) concentrations, paraoxonase-1 (PON-1), cholesteryl ester transfer protein (CETP), and lecithin-cholesterol acyltransferase (LCAT) activities were measured in the serum and/or HDL2 and HDL3 subfractions. SAA concentrations were higher in T2DM compared to controls: serum (30 mg/L (17, 68) versus 15 mg/L (7, 36); p=0.002), HDL2 (1.0 mg/L (0.6, 2.2) versus 0.4 mg/L (0.2, 0.7); p<0.001), and HDL3 (13 mg/L (8, 29) versus 6 mg/L (3, 13); p<0.001). Serum-PON-1 activity was lower in T2DM compared to that in controls (38,245 U/L (7025) versus 41,109 U/L (5690); p=0.043). CETP activity was higher in T2DM versus controls in HDL2 (232.6 μmol/L (14.1) versus 217.1 μmol/L (25.1); p=0.001) and HDL3 (279.5 μmol/L (17.7) versus 245.2 μmol/L (41.2); p<0.001). These results suggest that individuals with T2DM have increased SAA-related inflammation and dysfunctional HDL features. SAA may prove to be a useful biomarker in T2DM given its association with elevated CVD risk.

Abstract 84: Serum Amyloid A Does Not Modulate the Inverse Association of HDL with Coronary Artery Calcification in Type 2 Diabetes

2013 ◽  
Vol 33 (suppl_1) ◽  
Author(s):  
Claire K Mulvey ◽  
Timothy W Churchill ◽  
Karen Terembula ◽  
Jane F Ferguson ◽  
Nehal N Mehta ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Metabolic Syndrome ◽  
Logistic Regression ◽  
Coronary Artery ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Inverse Association ◽  
Tobit Regression ◽  
Amyloid A

Introduction Although high-density lipoprotein (HDL) is inversely correlated with cardiovascular risk, HDL loses its protective role in pathologic inflammatory states like type 2 diabetes (T2DM). HDL dysfunction contributes to accelerated atherosclerosis in T2DM, but the mechanism is incompletely defined. The acute phase reactant serum amyloid A (SAA) displaces apolipoprotein A-I and may impair HDL-mediated reverse cholesterol efflux. We hypothesized that SAA alters the inverse association between HDL and coronary artery calcium (CAC) in the Penn Diabetes Heart Study, a cross-sectional study of T2DM patients free of overt cardiovascular or renal disease. Methods We measured SAA in serum samples by immunonephelometry (N=975; mean age 58 ± 9 years; 63% male, 57% Caucasian; mean BMI 33 ± 6 kg/m 2 ). HDL was measured enzymatically in lipoprotein fractions after ultracentrifugation. Agatston CAC scores were quantified from electron beam tomography at the same visit. Spearman correlation and logistic regression were used to test associations of SAA with clinical factors and metabolic syndrome. We used Tobit regression to analyze associations between CAC and HDL, both overall and stratified by 3 categories of SAA: undetectable, lower half detectable, and upper half detectable. Results Spearman correlations revealed moderate association of SAA with C-reactive protein (r=0.52) and weak associations of SAA with BMI (r=0.25) and HDL (r=0.17; all p<0.001). In logistic regression, the group with highest SAA levels had increased odds of metabolic syndrome compared to those with undetectable levels (OR 1.56, 95% CI 1.03 to 2.38, p=0.036). In adjusted Tobit regression, HDL was inversely associated with CAC (Tobit coefficient for 1-SD increase in HDL: -0.30; 95% CI -0.54 to -0.06; p=0.013). Across the categories of SAA, however, there was no difference in the association of HDL with CAC (Tobit coefficient for 1-SD increase in HDL: -0.17 [95% CI -0.49 to 0.16] for undetectable vs. -0.31 [95% CI -0.79 to 0.17] for lower half detectable vs. -0.49 [95% CI -1.01 to 0.03] for upper half detectable). Conclusions Despite the association of SAA with metabolic syndrome, these data suggest that elevated SAA may not change the inverse relationship of HDL with CAC in T2DM.

Serum amyloid A and high density lipoproteins during the acute phase response

1988 ◽  
Vol 18 (6) ◽  
pp. 619-626 ◽  
Author(s):  
LINDA L. BAUSSERMAN ◽  
D. N. BERNIER ◽  
K. P. W. J. McADAM ◽  
P. N. HERBERT
Keyword(s):  
Acute Phase ◽  
Acute Phase Response ◽  
Serum Amyloid A ◽  
High Density ◽  
Phase Response ◽  
Serum Amyloid ◽  
High Density Lipoproteins ◽  
Amyloid A

scholarly journals High-Density Lipoproteins and Serum Amyloid A (SAA)

2021 ◽  
Vol 23 (2) ◽  
Author(s):  
Nancy R. Webb
Keyword(s):  
Serum Amyloid A ◽  
Inflammatory Responses ◽  
Inflammatory Diseases ◽  
Density Lipoprotein ◽  
High Density ◽  
Serum Amyloid ◽  
High Density Lipoproteins ◽  
Amyloid A

Abstract Purpose of Review Serum amyloid A (SAA) is a highly sensitive acute phase reactant that has been linked to a number of chronic inflammatory diseases. During a systemic inflammatory response, liver-derived SAA is primarily found on high-density lipoprotein (HDL). The purpose of this review is to discuss recent literature addressing the pathophysiological functions of SAA and the significance of its association with HDL. Recent Findings Studies in gene-targeted mice establish that SAA contributes to atherosclerosis and some metastatic cancers. Accumulating evidence indicates that the lipidation state of SAA profoundly affects its bioactivities, with lipid-poor, but not HDL-associated, SAA capable of inducing inflammatory responses in vitro and in vivo. Factors that modulate the equilibrium between lipid-free and HDL-associated SAA have been identified. Summary HDL may serve to limit SAA’s bioactivities in vivo. Understanding the factors leading to the release of systemic SAA from HDL may provide insights into chronic disease mechanisms.

scholarly journals Acute-Phase Serum Amyloid A Protein and Its Implication in the Development of Type 2 Diabetes in the KORA S4/F4 Study

Diabetes Care ◽  
2012 ◽  
Vol 36 (5) ◽  
pp. 1321-1326 ◽  
Author(s):  
C. Marzi ◽  
C. Huth ◽  
C. Herder ◽  
J. Baumert ◽  
B. Thorand ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Acute Phase ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Serum Amyloid A Protein ◽  
Acute Phase Serum

scholarly journals Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes.

1994 ◽  
Vol 180 (1) ◽  
pp. 203-209 ◽  
Author(s):  
R Badolato ◽  
J M Wang ◽  
W J Murphy ◽  
A R Lloyd ◽  
D F Michiel ◽  
...  
Keyword(s):  
Acute Phase ◽  
Polymorphonuclear Leukocytes ◽  
Serum Amyloid A ◽  
High Density ◽  
Serum Amyloid ◽  
High Density Lipoproteins ◽  
Secondary Amyloidosis ◽  
Polymorphonuclear Cells ◽  
Amyloid A ◽  
Cell Adhesion Molecule 1

Serum amyloid A (SAA) is an acute phase protein that in the blood is bound to high density lipoproteins; SAA is secreted mainly by hepatocytes, and its concentration increases in the blood up to 1000 times during an inflammatory response. At present, its biological function is unclear. Since some forms of secondary amyloidosis are caused by deposition in tissues of peptides derived from the SAA and leukocytes seem to be involved in this process, we investigated the effect of human SAA on human monocytes and polymorphonuclear cells (PMN). When recombinant human SAA (rSAA) was used at concentrations corresponding to those found during the acute phase (&gt; 0.8 microM), it induced directional migration of monocytes and polymorphonuclear leukocytes. Preincubation of rSAA with high density lipoproteins blocked this chemoattractant activity for both monocytes and PMN. rSAA also regulated the expression of the adhesion proteins CD11b and leukocyte cell adhesion molecule 1 and induced the adhesion of PMN and monocytes to umbilical cord vein endothelial cell monolayers. When subcutaneously injected into mice, rSAA recruited PMN and monocytes at the injection site. On the basis of these data, we suggest that SAA may participate in enhancing the migration of monocytes and PMN to inflamed tissues during an acute phase response.

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