Serum prolidase activity in idiopathic and ischemic cardiomyopathy patients

Sezen, Yusuf; Baş, Memduh; Altiparmak, Halil; Yıldız, Ali; Büyükhatipoğlu, Hakan; Dağ, Ömer; Kaya, Zekeriya; Aksoy, Nurten

doi:10.1002/jcla.20388

Cited by 25 publications

(15 citation statements)

References 23 publications

(18 reference statements)

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“…2011). A similar situation occurs in dilated cardiomyopathy where the vasculature surrounding the heart becomes fibrotic and prolidase activity is decreased (Sezen et al. 2010).…”

Section: Prolidase As a Marker For Diseasementioning

confidence: 85%

Prolidase function in proline metabolism and its medical and biotechnological applications

Kitchener

Grunden

2012

J Appl Microbiol

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Summary Prolidase is a multifunctional enzyme that possesses the unique ability to degrade imidodipeptides in which a proline or hydroxyproline residue is located at the C‐terminal end. Prolidases have been isolated from archaea and bacteria, where they are thought to participate in proline recycling. In mammalian species, prolidases are found in the cytoplasm and function primarily to liberate proline in the final stage of protein catabolism, particularly during the biosynthesis and degradation of collagen. Collagen comprises nearly one‐third of the total protein in the body, and it is essential in maintaining tissue structure and integrity. Prolidase deficiency (PD), a rare autosomal recessive disorder in which mutations in the PEPD gene affect prolidase functionality, tends to have serious and sometimes life‐threatening clinical symptoms. Recombinant prolidases have many applications and have been investigated not only as a possible treatment for PD, but also as a part of anti‐cancer strategies, a component of biodecontamination cocktails and in the dairy industry. This review will serve to discuss the many in vivo functions of procaryotic and eucaryotic prolidases, as well as the most recent advances in therapeutic and biotechnological application of prolidases.

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“…2011). A similar situation occurs in dilated cardiomyopathy where the vasculature surrounding the heart becomes fibrotic and prolidase activity is decreased (Sezen et al. 2010).…”

Section: Prolidase As a Marker For Diseasementioning

confidence: 85%

Prolidase function in proline metabolism and its medical and biotechnological applications

Kitchener

Grunden

2012

J Appl Microbiol

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“…Prolidase activity is related to the pathogenesis of various diseases Savas et al 2010;Sezen et al 2010;Toy et al 2009aToy et al , 2010Vural et al 2010b;Yildiz et al 2008a). Since its property of representation of collagen turnover, prolidase is an important marker for tumour size and aggression of the fi broid growth (Wolanska et al 2001).…”

Section: Introductionmentioning

confidence: 99%

Oxidative stress and prolidase activity in women with uterine fibroids

Vural

Camuzcuoğlu

Toy

et al. 2011

Journal of Obstetrics and Gynaecology

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The aim of this study was to investigate oxidative stress markers and prolidase activity in serum and tissue samples of women with uterine fibroids, with further analysis on position and size. Lipid hydroperoxide, ceruloplasmin, catalase, arylesterase, free sulfhydryl group activity and prolidase activity levels were measured in fibroid tissue, myometrial tissue and serum of the same patients (n = 51), at the same time. Results show that ceruloplasmin, catalase, arylesterase, free sulfhydryl group and prolidase activities were higher in fibroid tissue than those in myometrial tissue (p = 0.003, 0.009, 0.004, 0.02, 0.008, respectively). Serum levels of catalase and prolidase were lower, and arylesterase and free sulfhydryl groups were higher in the fibroid group than those in the control group (p < 0.001 for all). Fibroid volume in submucosal subgroup of the fibroid group yield significant correlation with ceruloplasmin, catalase, arylesterase and prolidase activities (r = 0.84, p = 0.02; r = 0.93, p < 0.001; r = 0.63, p = 0.049 and r = 0.87, p = 0.01, respectively). Despite the lack of statistical significance, the highest levels of prolidase activity were found in fibroid samples, especially in submucosal ones. It is concluded that this study demonstrated increased antioxidative repair system in the fibroid tissue compared to the myometrium and serum of the same patients. Additionally, higher pathophysiological potential of the submucosal fibroids over intramural and subserosal fibroids were shown with the levels of oxidative stress markers and prolidase activity levels.

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“…Sezen et al has detected lower prolidase activity than in control group in idiopathic and ischemic dilated cardiomyopathy patients groups. These patient groups exhibit the same histopathological feature of fi brosis (25). A decreased prolidase activity was shown in advanced chronic obstructive pulmonary disease.…”

Section: Fibrosis and Prolidasementioning

confidence: 64%

Prolidase

Namiduru¹

2016

BLL

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Prolidase (EC.3.4.13.9) or proline dipeptidase, is one of the unique enzyme capable of degrading dipeptides, in which a proline or hydroxyproline residue is located at the C-terminal position. Prolidase has a unique function in all cell types; therefore, the mechanisms and parameters involved in prolidase activity regulation are of special interest. Could prolidase be a good biomarker in different physiologic and pathologic conditions? This is an important question. There is no consensus on the answer to this question. It is of great importance during collagen turnover, infl ammation, tissue fi brosis and skeletal abnormalities. Prolidase itself without other biochemical markers may not provide information to clinicians about disease activity. So, I think it should be evaluated together with other serum biochemical markers. This review will serve to discuss many in vivo functions of prolidase, as well as level prolidase activity in diagnosis and monitoring of treatment in the various diseases (Ref. 50). Text in PDF www.elis.sk.

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Serum prolidase activity in idiopathic and ischemic cardiomyopathy patients

Cited by 25 publications

References 23 publications

Prolidase function in proline metabolism and its medical and biotechnological applications

Prolidase function in proline metabolism and its medical and biotechnological applications

Oxidative stress and prolidase activity in women with uterine fibroids

Prolidase

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