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  1. Article: Improvement of electrophoretic detection of antitrypsin activity in fish blood and seminal plasma.

    Wojtczak, Mariola / Ciereszko, Andrzej

    Electrophoresis

    2005  Volume 26, Issue 3, Page(s) 514–516

    Abstract: The original method of Uriel and Berges for detection of trypsin inhibitors lacks specificity due to masking effects of nonspecific esterases. We report a modification of this method based on inhibition of esterases in samples by phenylmethylsulfonyl ... ...

    Abstract The original method of Uriel and Berges for detection of trypsin inhibitors lacks specificity due to masking effects of nonspecific esterases. We report a modification of this method based on inhibition of esterases in samples by phenylmethylsulfonyl fluoride (PMSF). This method can be particularly useful for characterization profiles of antitrypsin activity in seminal plasma of salmonid fish where esterases and inhibitors migrate at the same mobility.
    MeSH term(s) Animals ; Carboxylesterase/antagonists & inhibitors ; Electrophoresis/methods ; Fishes/blood ; Male ; Phenylmethylsulfonyl Fluoride/chemistry ; Semen/chemistry ; Trypsin Inhibitors/blood ; Trypsin Inhibitors/isolation & purification
    Chemical Substances Trypsin Inhibitors ; Phenylmethylsulfonyl Fluoride (57KD15003I) ; Carboxylesterase (EC 3.1.1.1)
    Language English
    Publishing date 2005-02
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 619001-7
    ISSN 1522-2683 ; 0173-0835
    ISSN (online) 1522-2683
    ISSN 0173-0835
    DOI 10.1002/elps.200410180
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  2. Article ; Online: Seminal plasma proteins of Atlantic halibut (Hippoglossus hippoglossus L.).

    Mommens, Maren / Wojtczak, Mariola / Ciereszko, Andrzej / Babiak, Igor

    Fish physiology and biochemistry

    2008  Volume 34, Issue 4, Page(s) 349–355

    Abstract: Protein content and properties in the seminal plasma of Atlantic halibut (Hippoglossus hippoglossus) were assayed using spectrophotometric and electrophoretic methods. The protein concentration ranged from 6.4 +/- 3.1 to 19.4 +/- 3.4 mg ml(-1) and anti- ... ...

    Abstract Protein content and properties in the seminal plasma of Atlantic halibut (Hippoglossus hippoglossus) were assayed using spectrophotometric and electrophoretic methods. The protein concentration ranged from 6.4 +/- 3.1 to 19.4 +/- 3.4 mg ml(-1) and anti-proteolytic activity from 585.2 +/- 104.6 to 2912.4 +/- 367.4 U l(-l). A high correlation between anti-proteolytic activity and protein concentration (r = 0.95), and between sperm concentration and osmolality was found (r = 0.92). There was a significant decrease in anti-proteolytic activity from the first to the second sampling, but not in protein concentration. Anti-proteolytic activity and protein concentration were significantly affected by variations in individual males. Electrophoresis revealed four anti-proteolytic bands and individual differences in bands of proteolytic activity, which were subsequently characterized as metalloproteases and serine proteases.
    MeSH term(s) Animals ; Benzamidines/pharmacology ; Calcium Chloride/pharmacology ; Chelating Agents/pharmacology ; Edetic Acid/pharmacology ; Flounder/metabolism ; Flounder/physiology ; Gelatinases/metabolism ; Male ; Osmolar Concentration ; Semen/drug effects ; Semen/enzymology ; Semen/metabolism ; Seminal Plasma Proteins/metabolism ; Serine Proteinase Inhibitors/pharmacology ; Sperm Count
    Chemical Substances Benzamidines ; Chelating Agents ; Seminal Plasma Proteins ; Serine Proteinase Inhibitors ; Edetic Acid (9G34HU7RV0) ; Gelatinases (EC 3.4.24.-) ; benzamidine (KUE3ZY3J1F) ; Calcium Chloride (M4I0D6VV5M)
    Language English
    Publishing date 2008-12
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 292907-7
    ISSN 1573-5168 ; 0920-1742
    ISSN (online) 1573-5168
    ISSN 0920-1742
    DOI 10.1007/s10695-007-9194-x
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  3. Article: Seminal plasma proteins of Atlantic halibut (Hippoglossus hippoglossus L.)

    Mommens, Maren / Wojtczak, Mariola / Ciereszko, Andrzej / Babiak, Igor

    Fish physiology and biochemistry. 2008 Dec., v. 34, no. 4

    2008  

    Abstract: Protein content and properties in the seminal plasma of Atlantic halibut (Hippoglossus hippoglossus) were assayed using spectrophotometric and electrophoretic methods. The protein concentration ranged from 6.4 ± 3.1 to 19.4 ± 3.4 mg ml⁻¹ and anti- ... ...

    Abstract Protein content and properties in the seminal plasma of Atlantic halibut (Hippoglossus hippoglossus) were assayed using spectrophotometric and electrophoretic methods. The protein concentration ranged from 6.4 ± 3.1 to 19.4 ± 3.4 mg ml⁻¹ and anti-proteolytic activity from 585.2 ± 104.6 to 2912.4 ± 367.4 U l⁻l. A high correlation between anti-proteolytic activity and protein concentration (r = 0.95), and between sperm concentration and osmolality was found (r = 0.92). There was a significant decrease in anti-proteolytic activity from the first to the second sampling, but not in protein concentration. Anti-proteolytic activity and protein concentration were significantly affected by variations in individual males. Electrophoresis revealed four anti-proteolytic bands and individual differences in bands of proteolytic activity, which were subsequently characterized as metalloproteases and serine proteases.
    Keywords Hippoglossus hippoglossus ; blood proteins ; electrophoresis ; males ; metalloproteinases ; osmolality ; protein content ; seminal plasma ; serine proteinases ; spermatozoa
    Language English
    Dates of publication 2008-12
    Size p. 349-355.
    Publisher Springer Netherlands
    Publishing place Dordrecht
    Document type Article
    ZDB-ID 292907-7
    ISSN 1573-5168 ; 0920-1742
    ISSN (online) 1573-5168
    ISSN 0920-1742
    DOI 10.1007/s10695-007-9194-x
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  4. Article: Transferrin and antiproteases are major proteins of common carp seminal plasma.

    Wojtczak, Mariola / Dietrich, Grzegorz J / Ciereszko, Andrzej

    Fish & shellfish immunology

    2005  Volume 19, Issue 4, Page(s) 387–391

    MeSH term(s) Amino Acid Sequence ; Animals ; Carps/metabolism ; Chromatography, Ion Exchange ; Electrophoresis, Polyacrylamide Gel ; Male ; Molecular Sequence Data ; Poland ; Protease Inhibitors/analysis ; Semen/chemistry ; Sequence Analysis, Protein ; Transferrin/analysis ; Transferrin/genetics
    Chemical Substances Protease Inhibitors ; Transferrin
    Language English
    Publishing date 2005-10
    Publishing country England
    Document type Comparative Study ; Journal Article
    ZDB-ID 1067738-0
    ISSN 1095-9947 ; 1050-4648
    ISSN (online) 1095-9947
    ISSN 1050-4648
    DOI 10.1016/j.fsi.2005.01.009
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  5. Article: Polymorphism of transferrin of carp seminal plasma: relationship to blood transferrin and sperm motility characteristics.

    Wojtczak, Mariola / Dietrich, Grzegorz J / Irnazarow, Ilgiz / Jurecka, Patrycja / Słowińska, Mariola / Ciereszko, Andrzej

    Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology

    2007  Volume 148, Issue 4, Page(s) 426–431

    Abstract: Transferrin (Tf) is a major protein of carp (Cyprinus carpio) seminal plasma. Its relationship with milt quality is unknown. In this study, we sought to determine if Tf is polymorphic in carp seminal plasma and if this polymorphism is related to sperm ... ...

    Abstract Transferrin (Tf) is a major protein of carp (Cyprinus carpio) seminal plasma. Its relationship with milt quality is unknown. In this study, we sought to determine if Tf is polymorphic in carp seminal plasma and if this polymorphism is related to sperm motility characteristics. We screened males of purebred common carp line (Polish line R6) for Tf polymorphism in blood plasma. The majority of Tf genotypes represented only DD and DG variants. We then collected milt from preselected DD and DG genotypes and tested their sperm motility characteristics using computer-aided sperm analysis (CASA). Tf polymorphism in seminal plasma was found to be identical with that of blood. However, the relationships between Tf polymorphism and iron metabolic parameters were different for blood and semen. These data suggest different regulation of Tf in liver and testis. We found substantial differences in sperm motility characteristics between both genotypes. Spermatozoa of DG males were characterized by lower curvilinear velocity (VCL), amplitude of lateral head displacement (ALH), higher linearity (LIN) and straightness (STR) of movement as compared to DD males. No differences were found in other sperm characteristics such as sperm concentration and percentage of sperm motility. Our results suggest that sperm motility parameters are related to Tf polymorphism and therefore this polymorphism may be related to sperm competitive ability.
    MeSH term(s) Animals ; Carps/genetics ; Carps/physiology ; Cattle ; Electrophoresis ; Genotype ; Humans ; Iron/blood ; Iron/metabolism ; Linear Models ; Male ; Mice ; Polymorphism, Genetic ; Rats ; Semen/metabolism ; Semen/secretion ; Sperm Motility/genetics ; Transferrin/analysis ; Transferrin/genetics
    Chemical Substances Transferrin ; Iron (E1UOL152H7)
    Language English
    Publishing date 2007-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 121247-3
    ISSN 1879-1107 ; 1096-4959 ; 0305-0491
    ISSN (online) 1879-1107
    ISSN 1096-4959 ; 0305-0491
    DOI 10.1016/j.cbpb.2007.07.011
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  6. Article: Effects of different surfactants on motility and DNA integrity of brown trout (Salmo trutta fario) and common carp (Cyprinus carpio) spermatozoa.

    Dietrich, Grzegorz J / Zabowska, Marta / Wojtczak, Mariola / Słowińska, Mariola / Kucharczyk, Dariusz / Ciereszko, Andrzej

    Reproductive biology

    2007  Volume 7, Issue 2, Page(s) 127–142

    Abstract: In this study we evaluated effects of surfactants on motility parameters and DNA integrity of spermatozoa of freshwater teleost fish. Common carp (Cyprinus carpio) and brown trout (Salmo trutta fario) spermatozoa were exposed to either sodium dodecyl ... ...

    Abstract In this study we evaluated effects of surfactants on motility parameters and DNA integrity of spermatozoa of freshwater teleost fish. Common carp (Cyprinus carpio) and brown trout (Salmo trutta fario) spermatozoa were exposed to either sodium dodecyl sulphate (SDS, anionic surfactant) or octoxynol 9 ( Triton X-100, nonionic surfactant). Both surfactants added at activation caused a decrease in sperm motility characteristics measured by computer-assisted sperm analysis (CASA). Intraspecific differences in speed and trajectory of movement were detected. Triton X-100 and SDS when added to non activated sperm were also effective in the decrease of sperm motility and caused an increase of DNA fragmentation. Our results suggest that not only sperm motility apparatus but also DNA are targets for surfactant action. Therefore any exposure of spermatozoa to surfactants, in aquaculture conditions or natural environment, would have a negative impact on fish reproduction.
    MeSH term(s) Animals ; Carps/physiology ; DNA Fragmentation ; Male ; Octoxynol/pharmacology ; Semen/physiology ; Sodium Dodecyl Sulfate/pharmacology ; Sperm Count ; Sperm Motility/drug effects ; Sperm Motility/physiology ; Spermatozoa/cytology ; Spermatozoa/drug effects ; Spermatozoa/physiology ; Surface-Active Agents/pharmacology ; Trout/physiology
    Chemical Substances Surface-Active Agents ; Sodium Dodecyl Sulfate (368GB5141J) ; Octoxynol (9002-93-1)
    Language English
    Publishing date 2007-07
    Publishing country Poland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2189316-0
    ISSN 1642-431X
    ISSN 1642-431X
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  7. Article: Isolation, characterization and cDNA sequencing of a Kazal family proteinase inhibitor from seminal plasma of turkey (Meleagris gallopavo).

    Słowińska, Mariola / Olczak, Mariusz / Wojtczak, Mariola / Glogowski, Jan / Jankowski, Jan / Watorek, Wiesław / Amarowicz, Ryszard / Ciereszko, Andrzej

    Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology

    2008  Volume 150, Issue 2, Page(s) 207–215

    Abstract: The turkey reproductive tract and seminal plasma contain a serine proteinase inhibitor that seems to be unique for the reproductive tract. Our experimental objective was to isolate, characterize and cDNA sequence the Kazal family proteinase inhibitor ... ...

    Abstract The turkey reproductive tract and seminal plasma contain a serine proteinase inhibitor that seems to be unique for the reproductive tract. Our experimental objective was to isolate, characterize and cDNA sequence the Kazal family proteinase inhibitor from turkey seminal plasma and testis. Seminal plasma contains two forms of a Kazal family inhibitor: virgin (Ia) represented by an inhibitor of moderate electrophoretic migration rate (present also in the testis) and modified (Ib, a split peptide bond) represented by an inhibitor with a fast migration rate. The inhibitor from the seminal plasma was purified by affinity, ion-exchange and reverse phase chromatography. The testis inhibitor was purified by affinity and ion-exchange chromatography. N-terminal Edman sequencing of the two seminal plasma inhibitors and testis inhibitor were identical. This sequence was used to construct primers and obtain a cDNA sequence from the testis. Analysis of a cDNA sequence indicated that turkey proteinase inhibitor belongs to Kazal family inhibitors (pancreatic secretory trypsin inhibitors, mammalian acrosin inhibitors) and caltrin. The turkey seminal plasma Kazal inhibitor belongs to low molecular mass inhibitors and is characterized by a high value of the equilibrium association constant for inhibitor/trypsin complexes.
    MeSH term(s) Amino Acid Sequence ; Animals ; Avian Proteins/chemistry ; Avian Proteins/genetics ; Avian Proteins/isolation & purification ; Base Sequence ; Cloning, Molecular ; DNA, Complementary/chemistry ; Male ; Molecular Sequence Data ; Semen/chemistry ; Sequence Alignment ; Testis/chemistry ; Trypsin Inhibitor, Kazal Pancreatic/chemistry ; Trypsin Inhibitor, Kazal Pancreatic/genetics ; Trypsin Inhibitor, Kazal Pancreatic/isolation & purification ; Turkeys/genetics
    Chemical Substances Avian Proteins ; DNA, Complementary ; Trypsin Inhibitor, Kazal Pancreatic (50936-63-5)
    Language English
    Publishing date 2008-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 121247-3
    ISSN 1879-1107 ; 1096-4959 ; 0305-0491
    ISSN (online) 1879-1107
    ISSN 1096-4959 ; 0305-0491
    DOI 10.1016/j.cbpb.2008.03.003
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  8. Article ; Online: Acrosome staining and motility characteristics of sterlet spermatozoa after cryopreservation with use of methanol and DMSO.

    Psenicka, Martin / Dietrich, Grzegorz J / Wojtczak, Mariola / Nynca, Joanna / Rodina, Marek / Linhart, Otomar / Cosson, Jacky / Ciereszko, Andrzej

    Cryobiology

    2008  Volume 56, Issue 3, Page(s) 251–253

    Abstract: In this study we describe acrosome staining and motility characteristics of fresh and cryopreserved sterlet (Acipenser ruthenus L.) spermatozoa using soybean trypsin inhibitor-Alexa conjugate fluorescent staining and computer-aided sperm analysis (CASA), ...

    Abstract In this study we describe acrosome staining and motility characteristics of fresh and cryopreserved sterlet (Acipenser ruthenus L.) spermatozoa using soybean trypsin inhibitor-Alexa conjugate fluorescent staining and computer-aided sperm analysis (CASA), respectively. Methanol or dimethylsulfoxide (DMSO) were used as cryoprotectants. After cryopreservation a decline in sperm motility characteristics occurred, but no differential effect between cryoprotectant was observed. Cryopreservation caused a significant increase in the percentage of spermatozoa with acrosome stained by SBTI-Alexa for samples cryopreserved using DMSO compared to methanol. These data suggest that the low usefulness of DMSO for cryopreservation of sturgeon spermatozoa is related to its harmful specific effect towards the acrosome, probably by causing its precocious triggering, much before any egg contact.
    MeSH term(s) Acrosome/physiology ; Animals ; Cryopreservation ; Cryoprotective Agents/toxicity ; Dimethyl Sulfoxide/toxicity ; Fishes ; Fluorescent Dyes ; Male ; Methanol/toxicity ; Sperm Motility/drug effects ; Spermatozoa/cytology ; Spermatozoa/physiology ; Staining and Labeling
    Chemical Substances Cryoprotective Agents ; Fluorescent Dyes ; Methanol (Y4S76JWI15) ; Dimethyl Sulfoxide (YOW8V9698H)
    Language English
    Publishing date 2008-06
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80098-3
    ISSN 1090-2392 ; 0011-2240
    ISSN (online) 1090-2392
    ISSN 0011-2240
    DOI 10.1016/j.cryobiol.2008.03.006
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  9. Article: Application of biochemical markers for identification of biological properties of animal semen.

    Fraser, Leyland / Wysocki, Paweł / Ciereszko, Andrzej / Płucienniczak, Grazyna / Kotłowska, Mariola / Kordan, Władysław / Wojtczak, Mariola / Dietrich, Grzegorz / Strzezek, Jerzy

    Reproductive biology

    2006  Volume 6 Suppl 1, Page(s) 5–20

    Abstract: The use of biochemical markers for identification of biological properties of semen will help to develop new criteria that are accurate and objective in predicting and improving male fertility. Understanding and controlling the mechanisms involved in ... ...

    Abstract The use of biochemical markers for identification of biological properties of semen will help to develop new criteria that are accurate and objective in predicting and improving male fertility. Understanding and controlling the mechanisms involved in fertility is a key challenge, which is of fundamental importance in successful animal reproductive performance. Moreover, unraveling the unique molecular mechanism associated with sperm function might have considerable diagnostic value in the evaluation of male infertility. This review offered insights into some recent achievements and provided perspectives for possible applications of the biochemical markers of semen.
    MeSH term(s) 1-Alkyl-2-acetylglycerophosphocholine Esterase/analysis ; Acid Phosphatase/analysis ; Animals ; Biomarkers/analysis ; Cryopreservation ; DNA Fragmentation ; Male ; Oxidative Stress ; Semen/chemistry ; Spermatozoa/chemistry ; Spermatozoa/radiation effects
    Chemical Substances Biomarkers ; 1-Alkyl-2-acetylglycerophosphocholine Esterase (EC 3.1.1.47) ; Acid Phosphatase (EC 3.1.3.2)
    Language English
    Publishing date 2006
    Publishing country Poland
    Document type Journal Article ; Review
    ZDB-ID 2189316-0
    ISSN 1642-431X
    ISSN 1642-431X
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