Collagen content, but not the ratios of collagen type III/I mRNAs, differs among hypertensive, alcoholic, and idiopathic dilated cardiomyopathy

Soufen, Helena Nogueira; Salemi, Vera Maria Cury; Aneas, Ivy; Ramires, Felix José Alvarez; Benício, Anderson; Benvenuti, Luiz Alberto; Mady, Carlos Eduardo Keutenedjian

doi:10.1590/s0100-879x2008001200009

Cited by 30 publications

(29 citation statements)

References 37 publications

(40 reference statements)

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“…Our collagen expression results are in agreement with reports that clinical alcoholic cardiomyopathy is associated with increased collagen expression and total collagen content (Soufen et al, 2008). This change in collagen can directly affect cardiac structure and function, and may play a role in the progression of alcoholic cardiomyopathy (Brown et al, 1999; Brower et al, 2006; Collins et al, 2009; Graham et al, 2008; Mukamal et al, 2005; Piano, 2002; Walsh et al, 2002).…”

Section: Discussionsupporting

confidence: 93%

“…Similar increases in collagen expression have been reported in human alcoholic cardiomyopathy (Soufen et al, 2008). However, whether alcohol produces these alterations in collagen expression by altering cardiac fibroblast production of collagen, MMPs or TIMPs has not been previously investigated.…”

Section: Introductionsupporting

confidence: 85%

“…Although an increase of cardiac interstitial fibrosis has been reported in patients with alcoholic cardiomyopathy (Soufen et al, 2008), the role of altered MMP and TIMP expression in cardiac fibroblasts of chronic alcoholics has not been investigated. However, many reports suggest that alcohol-mediated dysregulation of MMP/TIMP balance may be an underlying mechanism in several pathological conditions.…”

Section: Introductionmentioning

confidence: 99%

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Alcohol Modulation of Cardiac Matrix Metalloproteinases (MMPs) and Tissue Inhibitors of MMPs Favors Collagen Accumulation

Hajj

Voloshenyuk

et al. 2013

Alcohol Clin Exp Res

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Background Chronic alcohol consumption has been shown in human and animal studies to result in collagen accumulation, myocardial fibrosis, and heart failure. Cardiac fibroblasts produce collagen and regulate extracellular matrix (ECM) homeostasis through the synthesis and activity of matrix metalloproteinases (MMP) and tissue inhibitors of MMPs (TIMP), with the balance of MMPs/TIMPs determining the rate of collagen turnover. Dynamic changes of MMP and TIMP expression were reported in alcohol induced hepatic fibrosis; however, the effect of alcohol on MMP/TIMP balance in the heart and cardiac fibroblasts is unknown. We hypothesized that alcohol exposure alters cardiac fibroblast MMP and TIMP expression to promote collagen accumulation in the heart. Methods Cardiac fibroblasts isolated from adult rats were cultured in the presence of alcohol (12.5–200 mM) for 48 hrs. MMP, TIMP, and collagen type I and III expression were assayed by Western blot analysis. Hydroxyproline (HPro) was used as a marker of collagen production. The in vivo cardiac effects of ethanol were determined using rats exposed to ethanol vapor for two weeks, resulting in blood alcohol levels of 150–200 mg/dl. Cardiac collagen volume fraction (CVF), as well as MMP, TIMP and collagen expression, was assessed. Results Ethanol exposed rats exhibited upregulation of TIMP-1, -3 and -4 in the heart, with no significant increases in MMPs. Cardiac fibroblasts exhibited transformation to a profibrotic phenotype following exposure to alcohol. These changes were reflected by increased α-smooth muscle actin and collagen I and III expression, as well as increased collagen secretion. In vivo ethanol exposure also produced fibrosis, indicated by increased CVF and expression of collagens. Conclusion Alcohol exposure modulates cardiac fibroblast MMP/TIMP expression favoring a profile associated with collagen accumulation. Our data suggest that this disrupted MMP/TIMP profile may contribute to the development of myocardial fibrosis and cardiac dysfunction resulting from chronic alcohol abuse.

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Section: Discussionsupporting

confidence: 93%

Section: Introductionsupporting

confidence: 85%

Section: Introductionmentioning

confidence: 99%

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Alcohol Modulation of Cardiac Matrix Metalloproteinases (MMPs) and Tissue Inhibitors of MMPs Favors Collagen Accumulation

Hajj

Voloshenyuk

et al. 2013

Alcohol Clin Exp Res

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“…We believe that vimentin specifically marked the fibroblast-type connective cells, responsible for collagen fibrillogenesis. In other words, the reaction to vimentin can be used for early diagnosis of myocardosclerosis [9].…”

Section: Resultsmentioning

confidence: 99%

Experimental ‏review ‏of ‏cobalt ‏induced cardiomyopathy

Zadnipryany¹,

Третьякова²,

Sataieva³

et al. 2017

Russ. Open Med. J.

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Abstract:The heart is a target of injury for many chemical compounds, both medically prescribed and not. Pathophysiological mechanisms underlying development of chemical-induced cardiomyopathies vary depending on the inciting agent, and can include: direct toxic effects, neurohormonal activation, altered calcium homeostasis, and oxidative stress. The fact that drug-induced heart disease, and in particular cobalt-induced cardiomyopathy, does not occur more often, as would be expected from the diversity of various mechanisms, is perhaps surprising. In spite of this, cardiotoxicity remains a major problem of hundreds of pharmaceutical agents, industrial chemicals and naturally occurring products and is often a limiting factor in treatment of certain diseases. Hence, it must be taken in account in the process of clinical decision making and treatment as well as in the process of drug research and development. The primary morphological alteration is mitochondrial damage that possibly reflects an enzymatic block of oxidative decarboxylation at pyruvate and ketogluterate levels. Due to that myofibrils of the myocardial cells were affected highlighting that the main cause of myofibril reduction could be a lower oxygen intake in the perinuclear area. The reduction of the contractile support of myocardial cells can explain the possible myocardial dysfunction. Nuclear changes were consistent with sarcoplasmic alterations, our study showing deformed, twisted, hyperchromatic nuclei with heterogeneous chromatin and even disintegrating nuclei. Changes of the interstitial connective tissue were sometimes extensive and sometimes barely noticeable. The most common alteration of this structure was the onset and development of a mainly perivascular collagen fibrillogenetic process.

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“…The higher III/I ratio may contribute to progressive ventricular dilation and dysfunction in dilated cardiomyopathy patients (30). Collagen type I coexists with collagen type III in fibrils of both collagenous and reticular fibers (31).…”

Section: Discussionmentioning

confidence: 99%

Endothelin-1 and type III collagen alterations in the heart of rats following cisplatin-induced toxicity

Huang

Liu

2011

Mol Med Report

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Abstract. Cisplatin-induced heart damage is associated with enzymes and protein alterations. The purpose of this study was to investigate cisplatin-induced alterations in cardiac endothelin (ET)-1 and type III collagen following administration of cisplatin. Male Wistar rats were randomly divided into two groups: a control and a cisplatin group. The cisplatin group received cisplatin intraperitoneally (i.p.) at a single dose of 7 mg/kg on day 6, while the controls were given the same amount of saline via the same route. On day 11, the rats were anesthetized and a thoracotomy was performed on all animals. Immunohistochemical analysis was performed to evaluate the protein expression of ET-1 and type III collagen. Sections were analyzed by digital image analysis. Results showed that the cardiac protein expression of ET-1 and type III collagen was altered following cisplatin-induced toxicity in rats. The expression of ET-1 and type III collagen was significantly increased after cisplatin treatment, supported by integrated optical density, when compared to the control group (P<0.05). The present findings indicate that such alterations may be reflected in abnormal cardiac function. Additionally, the proteins identified in this study may benefit investigations into the mechanisms underlying cisplatin-induced toxicity, thereby providing the necessary evidence for further research. IntroductionCisplatin is a chemotherapeutic agent widely used to treat a variety of solid tumors (1,2). It is also an antineoplastic drug that causes an array of adverse effects on various organs and tissues (3). Nephrotoxicity is one of the major side-effects of cisplatin chemotherapy (4) limiting the promising efficacy of cisplatin (5). Cisplatin-based chemotherapy also has a variety of vascular side-effects (6). Acute administration of cisplatin induces nausea/emesis and diarrhea (7). Chronic cisplatin may induce an enteric neuropathy characterized by changes in myenteric neurons associated with marked gastrointestinal motor dysfunction (7). Dysfunction in immune surveillance during anticancer chemotherapy of patients often causes weakness of the host defense system and a subsequent increase in microbial infections (8).Cisplatin-induced toxicity is known to be involved in the changes of antioxidant enzymes (GST, SOD, CAT, GSH-Px and GSH), serum superoxide dismutase (SOD), glutathione (GSH), malondiethylaldehyde (MDA), nitric oxide (NO) (9) and DNA (2,10). However, little is known about the changes in endothelin (ET)-1 and type III collagen expression in the heart following cisplatin-induced toxicity.The present study used immunohistochemical analysis to evaluate the expression of ET-1 and type III collagen in the heart, and to determine whether or not the protein expression is altered with cisplatin-induced toxicity. Materials and methodsAnimals and study design. Sixteen healthy adult male Wistar rats, weighing 210-250 g, were used in this study. The animals were housed individually in stainless-steel wire-bottomed cages in an air-conditione...

show abstract

Collagen content, but not the ratios of collagen type III/I mRNAs, differs among hypertensive, alcoholic, and idiopathic dilated cardiomyopathy

Cited by 30 publications

References 37 publications

Alcohol Modulation of Cardiac Matrix Metalloproteinases (MMPs) and Tissue Inhibitors of MMPs Favors Collagen Accumulation

Alcohol Modulation of Cardiac Matrix Metalloproteinases (MMPs) and Tissue Inhibitors of MMPs Favors Collagen Accumulation

Experimental ‏review ‏of ‏cobalt ‏induced cardiomyopathy

Endothelin-1 and type III collagen alterations in the heart of rats following cisplatin-induced toxicity

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