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Acta Morphologica Et Anthropologica Volume 24(3-4)

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Acta Morphologica Et Anthropologica Volume 24(3-4) Acta morphologica et anthropologica is the continuation of Acta cytobiologica et morphologica Editor-in-Chief: Prof. Nina Atanassova e-mail: [email protected]; [email protected] +359 2 979 2342 Deputy Editor-in-Chief: Prof. Dimitar Kadiysky e-mail: [email protected]; [email protected] +359 2 979 2311 Executive Secretary: Assoc. Prof. Y. Gluhcheva e-mail: [email protected] +359 2 979 2344 Editorial Board Prof. D. Angelov (Germany) Prof. D. Kordzaya (Georgia) Assoc. Prof. R. Alexandrova (Bulgaria) Prof. N. Lazarov (Bulgaria) Prof. B. Bilinska (Poland) Prof. Ts. Marinova (Bulgaria) Prof. A. Buzhilova (Russia) Prof. W. Ovtscharoff (Bulgaria) Prof. M. Davidoff (Germany) Assoc. Prof. M. Quartu (Italy) Prof. M. Dimitrova (Bulgaria) Prof. S. Sivkov (Bulgaria) Prof. E. Godina (Russia) Prof. A. Vodenicharov (Bulgaria) Editorial Correspondence Institute of Experimental Morphology, Pathology and Anthropology with Museum Bulgarian Academy of Sciences Acta morphologica et anthropologica Acad. Georgi Bonchev Str., Bl. 25 1113 Sofia Bulgaria e-mail: [email protected] Tel.: +359 2 979 2311 © Institute of Experimental Morphology, Pathology and Anthropology with Museum, Bulgarian Academy of Sciences, 2017 Prof. Marin Drinov Publishing House of Bulgarian Academy of Sciences Bulgaria, 1113 Sofia, Acad. Georgi Bonchev Str., Bl. 6 Graphic designer Daniela Miceva Format 70×100/16 Printed sheets 7.88 Printing Office of Prof. Marin Drinov Publishing House of BulgarianAcademy of Sciences Bulgaria, 1113 Sofia, Acad. Georgi Bonchev Str., Bl. 5 ISSN 1311-8773 (print) ISSN 2535-0811 (online) Acta morphologica et anthropologica 24(3-4) 24 (3-4) • Sofia • 2017 Institute of Experimental Morphology, Pathology and Anthropology with Museum Bulgarian Anatomical Society C o n t e n t s Morphology M. Dimitrova, I. Iliev, D. Tasheva, V. Lozanov, I. Ivanov – Novel Substrates for Determina- tion of the Fibroblast Activation Protein-α Activity. 3 E. Pavlova, D. Dimova, E. Petrova, Y. Gluhcheva, N. Atanassova – Comparative Evaluation of the Effect of Sodium Nitrite on Reproductive Organ Weights and Sperm Count in Rats and Mice. 10 M. Pencheva Y. Koeva, A. Tosheva, D. Ankova – Lifestyle and Environmental Factors Affect- ing Fertility in Men. 15 V. Dakova, M. Panayotova-Pencheva – Morphometric Features of Three Lungworms in Ma- terials from Wild Boars from Bulgaria. 21 V. Dakova, M. Panayotova-Pencheva – Morphometric Features of Oesophagostomum den- tatum, O. quadrispinulatum and Ascarops strongylina in Materials from Wild Boars from Bulgaria. 30 V. Broshtilova, Mary Gantcheva – Primary Apocrine Carcinoma of the Skin – a Case Report 40 V. Valtchev, Mary Gantcheva – HIV-Associated Sarcoma Kaposi in an Athlete. 44 V. Kolyovska, S. Ivanova, K. Kmetska, S. Todorov, D. Maslarov – Serum IgG Antibodies to GM1 and GD1a Gangliosides in a Patient with Relapsing-Remitting Multiple Sclerosis under Treatment with Glatiramer Acetate. A 15-year Longitudinal Study. 47 Anthropology and Anatomy Y. Zhecheva, I. Yankova – Prevalence of Underweight and Overweight among Preschool Chil- dren from Sofia Assessed through Different International References. 53 A. Dimitrova, I. Yankova-Pandourska – Asymmetry of Lean Body Mass Accumulation in 12-Year-Old Tennis Players (Preliminary Results). 63 V. Russeva – Degenerative Joint Disease Incidence and Spinal Column Joint Pathologies in the Paleopopulation from Medieval Anchialos, Excavated in Gladston Street, Pomorie. (Pre- liminary Results). 68 G. P. Georgiev, V. Karabinov, B. Matev, Al. Iliev, G. Kotov, B. Landzhov – Carpal Tunnel Syndrome Treatment with Open Surgical Release: a Study in 292 Patients. 76 1 St. Stanchev, Al. Iliev, L. Malinova, B. Landzhov – A Rare Case of Unusual Origin of Extensor Medii Proprius Muscle and its Clinical Significance. 82 I. N. Dimitrova, D. Trendafilova, Al. Iliev, B. Landzhov – Transradial Catheterization Failure due to High-Bifurcating Hypoplastic Radial Artery: Case Report. 86 Review Articles I. Ivanova, D. Sivrev, I. Stefanov – Human Pulmonary Mast Cells. 89 D. Dimova, E. Pavlova, N. Atanassova – The Role of Diabetes Mellitus in Male Reproductive Function. 99 G. Kotov, Al. Iliev, G. P. Georgiev, V. Karabinov, B. Landzhov – Clinical Significance of Anatomical Variations in the Carpal Tunnel. 109 I. Ilieva, I. Sainova, E. Zvetkova – Sperm Mitochondria-Associated Male Infertility: Sperm Quality Defects and Mitochondria (mtDNA) Anomalies. 114 2 Institute of Experimental Morphology, Pathology and Anthropology with Museum Bulgarian Anatomical Society Acta morphologica et anthropologica, 24 (3-4) Sofia • 2017 Morphology Novel Substrates for Determination of the Fibroblast Activation Protein-α Activity Mashenka Dimitrova1*, Ivan Iliev1, Donka Tasheva2, Valentin Lozanov3, Ivaylo Ivanov3 1Institute of Experimental Morphology, Pathology and Anthropology with Museum, Bulgarian Academy of Sciences, Sofia, Bulgaria 2Faculty of Chemistry and Pharmacy, University of Sofia St. Kl. Ohridsky, Sofia, Bulgaria 3Department of Medical Chemistry and Biochemistry, Medical University, Sofia, Bulgaria *Corresponding author: e-mail: [email protected] Fibroblast activation protein-α (FAP- α) is a membrane-associated serine protease of the S9b family of post-proline cleaving enzymes. It is usually expressed in reactive stromal fibroblasts in many types of diseases connected with extensive pathological alterations of the connective tissue like arthritis, fibro- ses, carcinomas and sarcomas. That is why the enzyme is considered a valuable marker for those enti- ties. Design and development of specific FAP-α substrates are rather challenging due to the enzyme’s structural similarity with the other proline-specific enzymes. In this paper we present the design of three novel substrates for the determination of FAP-α activity as well as the assessment of their efficacy and specificity. According to the obtained results, one of the newly developed substrates has a potential to be used as a highly specific substrate for FAP-α. Key words: fibroblast activation protein-α, molecular modeling, enzyme substrate, substrate speci- ficity Introduction Fibroblast activation protein-α (FAP-α; EC 3.4.21.B28) is a membrane-bound post- proline cleaving serine protease. It represents a 97 kDa glycoprotein existing as 170 kDa homodimer in its native form [15]. The enzyme hydrolyzes polypeptide substrates possessing Pro in P1 position. It can act both as exo- and endopeptidase but is more ef- ficient as an endopeptidase [14]. Some of the well-known enzyme`s natural substrates are collagen type I, neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY [9]. FAP-α is involved in normal processes like tissue remodeling during the embry- 3 onic development, wound healing, etc. However, normal adult human and mammalian tissues do not express FAP-α [18]. Otherwise, the enzyme is highly induced in many diseases such as rheumatoid arthritis and osteoarthritis, liver and pulmonary fibrosis and in cancer [reviewed in 11]. It is expressed mostly by reactive stromal fibroblasts but has also been found in certain types of tumor cells [5, 11]. Many studies have shown that FAP-α participates in the mechanisms of tumor growth, angiogenesis and inhibition of the antitumor immune response [12, 17]. Studies on the enzyme activity in norm and pathology need the application of highly selective substrates [6]. However, the design of FAP-α specific substrates is very difficult due to its close structural similarity with the other proline-specific enzymes [reviewed in 5]. In the present paper we describe the design and development of three novel sub- strates intended for the biochemical assays of FAP-α activity in tissue homogenates and/or cell lysates. Additionally, we present the assessment of these substrates’ efficacy and selectivity. Materials and Methods Molecular modeling. Using the crystal structure of human FAP-α (Protein Data Bank ID: 1Z68), obtained by Aertgeerts et al. [1], we modeled the structure of the enzyme- substrate complex with isonicotinoyl-D-Ala-Pro-4-nitroanilide by Dreiding forcefield method [13]. FAP-α substrates. We synthesized, purified (recrystallization, high performance liquid chromatography) and analyzed (nuclear magnetic resonance, mass spectromet- ry) the following substrates: β-Ala-D-Ala-Pro-4-nitroanilide (AAP), β-Ala-Nle-Pro- 4-nitroanilide (ANP) and isonicotinoyl-D-Ala-Pro-4-nitroanilide (IAP). The synthetic methods, substrates purification and spectral analyses will soon be published elsewhere. Cell culturing. Three permanent cell lines were used – MCF-10A (normal im- mortalized human epithelial cells from mammary gland), MCF-7 (human tumor cells obtained from mammary gland carcinoma of low invasiveness) and MDA-MB-231 (human tumor cells from mammary gland carcinoma of high invasiveness). The can- cer cells were cultured in 75 cm2 tissue culture flasks in Dulbecco’s Modified Eagle’s Medium – high glucose 4.5‰ (DMEM), supplemented with 10% fetal calf serum and antibiotics in usual concentrations. Normal cells were cultivated in the same conditions but with the addition of 20 mg/l human epidermal growth factor (EGF), 0.5 mg/l hydro- cortisone, 0.1 mg/l cholera toxin and 10 mg/l insulin. Cell cultures were maintained at 37.5 °C in a humidified atmosphere and 5% CO2 until 95% confluence was achieved. Biochemical assays. For the estimation of FAP-α activity towards different sub- strates, aliquots of human recombinant FAP-α (Enzo Life Sciences, Inc.) were incu- bated with 0.1 mM of the respective substrate in 0.1 М phosphate buffer
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