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��ࡱ�>��	�����������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������������y����bjbj��	7��{�{�Y�������vv������������8|�<��=0�����=======$?��Af(=��(=����4�=N7N7N7�����=N7=N7N7N7�����q�9w�������2*N7�<�=0�=N77B�6|7BN77B�N7�N7(=(=N7�=��������������������������������������������������������������������7Bv �:INCREASED COMPLEMENT C3 AND ADIPSIN PROTEIN EXPRESSION IN HUMAN CORONARY ATHEROSCLEROTIC PLAQUES IN SMOKERS

Subheading: Increased C3 and adipsin expression in plaques
Fatih Tangi1, Mehmet Karaduman2, Ugur Musabak3, Rahsan I. Sagkan3, Oben Baysan4, Faruk Cingoz5, and Cagatay Oktenli6*.

Division of Internal Medicine1, G�lhane Military Medical Academy, Haydarpasa Training Hospital, Istanbul, TURKEY. Departments of Internal Medicine2, Immunology and Allergic Diseases3, Cardiology4, Cardiovascular Surgery5 G�lhane Military Medical Academy, Ankara, TURKEY. Department of Internal Medicine6, Anadolu Medical Center, Kocaeli, TURKEY

*Corresponding author:
Prof. Cagatay Oktenli
Department of Internal Medicine, Anadolu Medical Center, TR-41400 Gebze/Kocaeli, Turkey. E-mail: cagatay.oktenli@anadolusaglik.org or coktenli@yahoo.com
Tel: +90 216 547 1122; Fax: +90 216 317 9503


Abstract
Objective: Little information available about any link between smoking status and protein expression levels of acylation stimulating protein, complement 3 and adipsin in coronary atherosclerotic plaques. We aimed to determine protein expression levels of acylation stimulating protein, complement 3 and adipsin by Western blot analysis in the plaques obtained from coronary artery bypass grafting and to evaluate whether there is any relationship with smoking status. 
Methods: Coronary artery specimens were obtained from 32 consecutive patients who underwent coronary artery bypass grafting procedure. Smoking was classified as current [smoking more than 5 cigarettes within the past 3 months (n=7)], past [< 3 months and < 40 years (n=15)], or never smoking (n=10) ). Group A consisted of current or former smoker patients (n=22), while group B consisted of nonsmoker patients (n=10). 
Results: Increased complement 3 and adipsin protein expression was observed in group A patients than those of group B. We showed that no signal of protein expression of acylation stimulating protein in the plaques in both groups. 
Conclusions: This is the first report regarding the association of complement 3 and adipsin, but not acylation stimulating protein, with smoking status in coronary atherosclerotic plaques. Our results provide confirmatory data to prior publications dealing with structural changes in complement 3 induced by smoking, in addition to other physiopathological mechanisms, might accelerate the coronary atherosclerotic process. 
Keywords: coronary atherosclerotic plaque, complement 3, adipsin, smoking
Introduction

	Acute coronary syndromes show the presence of multiple complex coronary stenoses and fissures, and rupture of atherosclerotic lesion is the most common cause of the syndrome [1,2]. Recent research has shown that immune and inflammatory processes plays a crucial role in these coronary events [3,4]. Complement 3 (C3), central player in the immune system, secreted by activated macrophages at inflammation sites and by adipocytes [5-7]. Interestingly, it has been reported that hyperlipidemia or coronary artery disease is rare in C3-deficient subjects [8]. In prospective studies on the relations of C3 with coronary artery disease (CAD), C3 was shown to be a powerful predictor of coronary events but not independently of the established risk factors [9,10]. Acylation stimulating protein (ASP) is produced through the interaction of three essential components of the alternative complement pathway, factor B, adipsin (identical to complement factor D) and C3 [11-13]. ASP stimulates free fatty acid esterification to form triglycerides by activating diacylglycerol acyltransferase [14-16]. ASP also supresses lipolysis via inhibition of hormone sensitive lipase [12,17]. Previous studies have demonstrated elevaled fasting plasma ASP concentrations in obese subjects [11,12]. Moreover, potential factors for generation of ASP like C3, factor B and adipsin were shown to be increased in type 2 diabetic men, which probably contributes to increased ASP levels [12]. On the other hand, even in the absence of obesity, not only ASP but also its precursor C3 have been reported to be increased in diabetes [18], cardiovascular disease [19-24], nephrotic syndrome [25], thyroidal dysfunction [26], polycystic ovary syndrome [27], and nonalcoholic fatty liver disease [28]. 
	In CAD, although the inflammatory and immune activation has been assessed extensively by measuring circulating levels, limited data is available for the local status of ASP and its precursors at the site of the atherosclerotic plaques. Atherectomy specimens obtained from coronary artery bypass grafting (CABG) provide a unique source of plaque tissues [3,4]. Therefore, we aimed to determine protein expression levels of ASP, C3 and adipsin by Western blot analysis in the coronary atherosclerotic plaques and to evaluate whether there is any relationship with smoking status.













Material and Methods

	Coronary artery specimens were obtained from 32 consecutive patients (24 men and 8 women) who underwent CABG procedure. Exclusion criteria were patients with any systemic disease besides atherosclerosis, prior myocardial infarction within 30 days before surgery, coexisting malignancy, metabolic, neurological or immunologic disease, acute or chronic infectious diseases, secondary or familial hypercholesterolemia, renal or hepatic failure, any medication other than a beta-blocker, calcium antagonists, nitrates, acetylsalicylic acid d" 250 mg/day, angiotensin-converting enzyme inhibitors, angiotensin-II receptor blockers, oral antidiabetics or statins. Each subjects gave his informed consent to the study, which was previously approved by our local ethics committee and institutional review board.
	Clinical history was assessed for smoking, diabetes mellitus, hypertension, and hyperlipidemia. Smoking was classified as current smoking [smoking more than 5 cigarettes within the past 3 months (n=7)], smoked in the past [< 3 months and < 40 years (n=15)], or never smoking (n=10). Group A consisted of current or former smoker patients (n=22), while group B consisted of nonsmoker patients (n=10). BMI was calculated as weight (kilograms) divided by height (meters) squared. Blood pressure was calculated as the avarage of three measurements taken under standardized conditions in a supine position with a sphygmomanometer. 
	Blood samples for laboratory assays were obtained before the procedure following overnight fasting. Serum was separated and frozen at -80�C until the time of the assay. Fasting blood glucose, triglyceride and high-density lipoprotein levels were measured by enzymatic colorimetric method with Olympus AU 600 autoanlyzer using reagents from Olympus Corp. (Hamburg, Germany). Low-density lipoprotein was calculated by Friedewald�s formula. 
	Thirty-two coronary atherosclerotic plaque specimens were derived from proximal lesions in the left anterior descending coronary artery (n=29), right coronary artery (n=1), left circumflex artery (n=2) during the elective CABG surgery. Immediately after the procedure, all specimens were washed in cold phosphate buffer saline (PBS) and they were quickly frozen and stored at -80�C until use for Western blot analysis.

Western blot analysis

	Coronary atherosclerotic plaque specimens from patients corresponding to the two different patient groups (group A and B) were pooled for Western blot analysis. The samples were washed with PBS and then lysed in homogenization buffer [50 mM Tris-HCL, pH 8.0; 0.25% (w/v) SDS; 1% (w/v) Nonidet P40 [NP40]; 1 mM (w/v) paramethylsulfonide [PMSF]; 150 mM (w/v) NaCl; 1X protease inhibitor cocktail]. Collected proteins measured using Qubit Fluorometer (Invitrogen, Carlsbad, CA, USA). Approximately, 65 �g/ml of protein samples loaded to gel. Proteins were separated on NuPAGE 4-12% Bis-Tris Gel (Invitrogen, Carlsbad, CA, USA). Proteins were transferred by dry-blotting via Cu ions (iBlot Gel Transfer Stacks to a PVDF membrane) (Invitrogen, Carlsbad, CA, USA). Adipsin (1/200), C3 (1/200) and �-actin (1/200) were detected using the mouse monoclonal antibodies (Santa Cruz Biotechnology, Santa Cruz, CA, USA) and we also used ASP (1/5000) which is a mouse monoclonal antibody against human peptide with aminoacid sequence RASHLGLA which is located in C-terminal part of the human ASP (BioVendor, Candler, NC, USA) as primary antibodies. Detected with an alkaline phosphatase-conjugated mouse anti-mouse IgG secondary antibody using a Western Breeze Immunodetection System (Invitrogen, Carlsbad, CA, USA). The signals from the Western blots were normalized to the constitutive �-actin control. We showed that adipsin:b-actin, ASP:b-actin and C3:b-actin ratios, as determined by densitometric scanning of signals from two groups. Quantum-Capture Software was used for the densitometric analyses.










Results

	In Table 1, clinical and laboratory characteristics of patients were shown. Hyperlipidemia were present in 14 patients (44%), hypertension in 17 (53%), diabetes mellitus in 11 (34%), family history of CAD in 13 (40%), prior MI in 11 (34%). Drug use as follows: aspirin (n=30), beta-blockers (n=18), calcium antagonists (n=16), angiotensin-converting enzyme inhibitors/angiotensin-II receptor blockers (n=20), oral antidiabetics (n=11), nitrates (n=10), and statins (n=27).
	As mention above, coronary atherosclerotic plaque specimens from patients corresponding to the two different patient groups (group A and B) were pooled for Western blot analysis. Increased C3 (Figure 1) and adipsin (Figure 2) protein expression was observed in group A. However, we were unable to display any signal for ASP in the plaques (Figure 3).







Discussion 
	
In the current study, we investigated protein expression of ASP and, its precursors,  C3 and adipsin by Western blot analysis in the coronary atherosclerotic plaques obtained from CABG procedure. Interestingly, both C3 and adipsin, but not ASP, protein expression in the plaques were found to be higher in group A patients (former and currently smoker patients) than group B patients (nonsmokers). On the one hand, our finding that increased expression of adipsin in coronary atherosclerotic plaques of smoker patients is novel finding. Adipsin is a unique member of the alternative complement pathway and adipose tissue is the major source of plasma adipsin [17]. Peripheral monocytes/macrophages, brain, lung, synovial tissue, and muscle are nonadipose sources of plasma adipsin [29] Napolitano et al. [30] suggested that adipsin levels were slightly higher in the obese subjects than control subjects. However, in the current study, pathophysiological and clinical relevance of increased adipsin expression in the plaques in smokers patients with CAD remain to be answered. On the other hand, Cianflone et al. reported significantly higher plasma ASP levels in patients with CAD than in age-matched healthy controls [19]. Unexpectedly, in spite of the increased expression of C3 and adipsin, potential factors for generation of ASP, we were unable to display any signal for ASP in atherosclerotic plaque. This leads us to believe that the both C3 and adipsin may contribute independently through direct effects in atherosclerotic plaque development or progression in smoker patients.
	The present study expands our knowledge of the role of C3 in the pathogenesis of smoking-associated coronary atherosclerosis. Although little is known about relation between smoking and complement, smoking was previously suggested in vitro to activate the alternative complement pathway by modifying C3 [5,31]. Our findings are in line the previous data that detection of C3 in extracts from atherosclerotic plaques [32-35]. Normally, C3 is an acute phase reactant produced by not only liver, but also in extra-hepatic tissues including adipocytes, endothelium, mononuclear cells, and myoblasts [36]. In this context, it has been demonstrated that complement deposition in the intima precedes the infiltration of inflammatory cells in experimental atherosclerosis model [37]. Moreover, complement components have been suggested to be deposited and activated in the vessel wall in patients with CAD [38], and lipid components of plaques may actually activate complements [39,40]. Previous data mentioned above, along with the present findings, lead us to think that C3 is not only an independent risk factor but also an immune mediator in the development or progression of atherosclerosis in smokers. Furthermore, we have previously suggested that inflammation plays an intrinsic role in atherosclerotic plaque development and progression [3,4]. This concept was largely developed from the observations that tissue levels of inflammatory cytokines like interleukin-6 (IL-6) and C-reactive protein (CRP) are found to be increased in coronary atherosclerotic plaques of smoker patients [3,4]. As cytokines, particularly IL-6 and CRP [7] have been suggested to increase C3 production, they may contribute increased C3 expression in the plaques of smoker patients with CAD.  
	The present study had a number of limitations need to be mentioned. First, the sample size of this study was small. Second, localization or origin of C3 and adipsin in atherosclerotic plaques are unknown. In immunohistochemical studies, the detection of the localization of these proteins would be much more convincing. Third, as our subjects were on drugs until CABG procedure, these drugs may cause a confounding effect on our findings. In this study, coronary atherosclerotic plaque samples were pooled. Therefore, we were unable to perform statistical analysis. Since the current study was perfomed in patients with CAD without a reference population, it cannot be readily generalized to individuals without atherosclerosis. Finally, small representation of females is another limitation of the study. However, it is possible that this reflects the relatively smaller representation of females in overall population of patients with CAD.
This is the first study regarding the association of C3 and adipsin, but not ASP, with smoking status in coronary atherosclerotic plaques. Our results provide confirmatory data to prior publications dealing with structural changes in C3 induced by smoking, in addition to other physiopathological mechanisms, might accelerate the coronary atherosclerotic process. As the present data provide evidence of association rather than of causation, the biological significance of relations must be interpreted with great caution. 

Acknowledgements
	This study was supported by grant from Research Center of G�lhane Military Medical Academy.
Disclosure statement: Authors of this study have no interest which might be perceived as posing a conflict or bias.


References

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CJOJQJaJhbh�CJOJQJaJh�_�h�=hCJOJQJaJh})Oh�=hCJOJQJaJh�_�CJOJQJaJh})Oh�_�CJOJQJaJ�`�`�`�`aaaaa
a�a�a�a�a�a�a�a�a�a�a�a�a�a�a�a�a�a�a�ab�������Ǹ����ǎ�����sd�d�d���dbS�hEL�hw+CJOJQJaJUh})Ohw+CJOJQJaJh})Oh�3.CJOJQJaJh�.CJOJQJaJhEL�h_R�CJOJQJaJh})OhEL�CJOJQJaJhEL�CJOJQJaJh})OhL8�CJOJQJaJhbh�CJOJQJaJh})OhuQCJOJQJaJh})Oh_R�CJOJQJaJh})Oh�=hCJOJQJaJ Dev Comp Immunol 25: 745-762.
37- Seifert PS, Hugo F, Hansson GK, Bhakdi S. (1989) Prelesional complement activation in experimental atherosclerosis. Terminal C5b-9 complement deposition coincides with cholesterol accumulation in the aortic intima of hypercholesterolemic rabbits. Lab Invest 60: 747-754.
38- Oksjoki R, Kovanen PT, Pentikainen MO. (2003) Role of complement activation in atherosclerosis. Curr Opin Lipidol 14: 477-482.
39- Niculescu F, Rus H. (1999) Complement activation and atherosclerosis. Mol Immunol 36: 949-955.
40- Seifert PS, Hugo F, Tranum-Jensen J, Zahringer U, Muhly M, et al. (1990) Isolation and characterization of a complement-activating lipid extracted from human atherosclerotic lesions. J Exp Med 172: 547-557.












Figure Legends

Figure 1. Western blot analysis of protein level for C3 (M, Marker). For quantification of C3 protein content, the ratio of C3 and �-actin band densities of group A and group B samples of atherosclerotic plaques.
Figure 2. Western blot analysis of protein level for Adipsin (M, marker). For quantification of adipsin protein content, the ra��������� �!�+�J�L�M�Q�S��#�$�&�'�(�,�-�/�0�1�3�4�Z�[�\�������ֻ����ւs��d�d�֬ʬ��U�U�Uh})Oh�G�CJOJQJaJhEL�hQ~<CJOJQJaJh})OhEL�CJOJQJaJhEL�CJOJQJaJh})Oh~�CJOJQJaJh})OhuQCJOJQJaJh})OhQ~<CJOJQJaJh})Oh_R�CJOJQJaJh�.CJOJQJaJhbh�CJOJQJaJh})Ohw+CJOJQJaJhEL�hw+CJOJQJaJ \�]�a�c�����������������������������������	�
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�CJOJQJaJh})Oh�9WCJOJQJaJh�.CJOJQJaJhTMCJOJQJaJh})Oh~�CJOJQJaJh�}�hPQ�CJOJQJaJh�}�CJOJQJaJh})Oh�}�CJOJQJaJh})OhPQ�CJOJQJaJ�������������J�L�N�h����������������
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Figure 3. Western blot analysis of protein level for ASP (M, marker)


Table legend
Table 1. Clinical and Laboratory Characteristics of Patients (n=32)



















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