The Experts below are selected from a list of 3285 Experts worldwide ranked by ideXlab platform
Pavel Kozak - One of the best experts on this subject based on the ideXlab platform.
-
protein modification in the post mating Spermatophore of the signal crayfish pacifastacus leniusculus insight into the tyrosine phosphorylation in a non motile spermatozoon
Animal Reproduction Science, 2016Co-Authors: Hamid Niksirat, Liselotte Andersson, Marie Vancova, Antonin Kouba, Peter James, Pavel KozakAbstract:After mating, Spermatophores of signal crayfish are stored on the body of the female for a period before fertilization. This study compared the post-mating protein profile and pattern of protein tyrosine phosphorylation of the signal crayfish Spermatophore to that of the freshly ejaculated Spermatophore and found substantial differences. Two major bands of tyrosine-phosphorylated proteins of molecular weights 10 and 50 kDa were observed in the freshly ejaculated Spermatophore of the signal crayfish. While the tyrosine-phosphorylated protein band with molecular weight 10 kDa was formed by protein(s) of similar pH, the band with molecular weight of 50 kDa consisted of proteins of varying pH. In the post-mating Spermatophore, the band with molecular weight of 50 kDa was not detected, and an increase in the level of protein tyrosine phosphorylation was observed in the 10 kDa band. The microtubular radial arms of the spermatozoon showed a positive reaction to an anti-tyrosine antibody conjugated with gold particles in both the freshly ejaculated and post-mating Spermatophores. In conclusion, the male gamete of the signal crayfish undergoes molecular modification during post-mating storage on the body of the female including changes in the level of protein expression and protein tyrosine phosphorylation. Structural similarity of the radial arms in the crayfish immotile spermatozoon with flagellum, which is the main site of protein tyrosine phosphorylation in the mammalian motile spermatozoa, raises questions regarding evolution and function of such organelles across the animal kingdom that must be addressed in the future studies.
-
label free protein quantification in freshly ejaculated versus post mating Spermatophores of the noble crayfish astacus astacus
Journal of Proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p<0.05, fold change ≥2). The highest rate of up-regulation was observed in sodium/hydrogen exchanger, which may indicate the importance of intracellular pH adjustment for final maturation of the crayfish spermatozoon. The highest rate of down-regulation was observed in histone H2A. This may increase chromatin flexibility and facilitate its transfer into the oocyte during fertilization. The vitellogenin protein was identified in the crayfish Spermatophore and its level changed during storage on the body surface of female. Extensive proteomic modification of male gametes during storage on the body surface of the female suggests post-mating final maturation of the crayfish spermatozoon. (Less)
-
Label-free protein quantification in freshly ejaculated versus post-mating Spermatophores of the noble crayfish Astacus astacus.
Journal of proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p
Hamid Niksirat - One of the best experts on this subject based on the ideXlab platform.
-
protein modification in the post mating Spermatophore of the signal crayfish pacifastacus leniusculus insight into the tyrosine phosphorylation in a non motile spermatozoon
Animal Reproduction Science, 2016Co-Authors: Hamid Niksirat, Liselotte Andersson, Marie Vancova, Antonin Kouba, Peter James, Pavel KozakAbstract:After mating, Spermatophores of signal crayfish are stored on the body of the female for a period before fertilization. This study compared the post-mating protein profile and pattern of protein tyrosine phosphorylation of the signal crayfish Spermatophore to that of the freshly ejaculated Spermatophore and found substantial differences. Two major bands of tyrosine-phosphorylated proteins of molecular weights 10 and 50 kDa were observed in the freshly ejaculated Spermatophore of the signal crayfish. While the tyrosine-phosphorylated protein band with molecular weight 10 kDa was formed by protein(s) of similar pH, the band with molecular weight of 50 kDa consisted of proteins of varying pH. In the post-mating Spermatophore, the band with molecular weight of 50 kDa was not detected, and an increase in the level of protein tyrosine phosphorylation was observed in the 10 kDa band. The microtubular radial arms of the spermatozoon showed a positive reaction to an anti-tyrosine antibody conjugated with gold particles in both the freshly ejaculated and post-mating Spermatophores. In conclusion, the male gamete of the signal crayfish undergoes molecular modification during post-mating storage on the body of the female including changes in the level of protein expression and protein tyrosine phosphorylation. Structural similarity of the radial arms in the crayfish immotile spermatozoon with flagellum, which is the main site of protein tyrosine phosphorylation in the mammalian motile spermatozoa, raises questions regarding evolution and function of such organelles across the animal kingdom that must be addressed in the future studies.
-
subcellular localization of calcium deposits in the noble crayfish astacus astacus Spermatophore implications for post mating Spermatophore hardening and spermatozoon maturation
Journal of Morphology, 2016Co-Authors: Hamid Niksirat, Antonin KoubaAbstract:The freshly ejaculated Spermatophore of crayfish undergoes a hardening process during post-mating storage on the body surface of female. The ultrastructural distribution of calcium deposits were studied and compared in freshly ejaculated and post-mating noble crayfish Spermatophores, using the oxalate-pyroantimonate technique, to determine possible roles of calcium in post-mating Spermatophore hardening and spermatozoon maturation. Small particles of sparsely distributed calcium deposits were visible in the wall of freshly ejaculated Spermatophore. Also, large amount of calcium deposits were visible in the membranes of the freshly ejaculated spermatozoon. Five minutes post-ejaculation, granules in the Spermatophore wall appeared as porous formations with numerous electron lucent spaces. Calcium deposits were visible within the spaces and scattered in the Spermatophore wall matrix, where smaller calcium deposits combined to form globular calcium deposits. Large numbers of the globular calcium deposits were visible in the wall of the post-mating Spermatophore. Smaller calcium deposits were detected in the central area of post-mating Spermatophore, which contains the sperm mass, and in the extracellular matrix and capsule. While the density of calcium deposits decreased in the post-mating spermatozoon membranes, numerous small calcium deposits appeared in the subacrosomal zone and nucleus. Substantial changes in calcium deposit distribution in the crayfish Spermatophore during post-mating storage on the body of female may be involved in the processes of the Spermatophore hardening and spermatozoon maturation. J. Morphol. 277:445–452, 2016. © 2016 Wiley Periodicals, Inc.
-
label free protein quantification in freshly ejaculated versus post mating Spermatophores of the noble crayfish astacus astacus
Journal of Proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p<0.05, fold change ≥2). The highest rate of up-regulation was observed in sodium/hydrogen exchanger, which may indicate the importance of intracellular pH adjustment for final maturation of the crayfish spermatozoon. The highest rate of down-regulation was observed in histone H2A. This may increase chromatin flexibility and facilitate its transfer into the oocyte during fertilization. The vitellogenin protein was identified in the crayfish Spermatophore and its level changed during storage on the body surface of female. Extensive proteomic modification of male gametes during storage on the body surface of the female suggests post-mating final maturation of the crayfish spermatozoon. (Less)
-
Label-free protein quantification in freshly ejaculated versus post-mating Spermatophores of the noble crayfish Astacus astacus.
Journal of proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p
Antonin Kouba - One of the best experts on this subject based on the ideXlab platform.
-
protein modification in the post mating Spermatophore of the signal crayfish pacifastacus leniusculus insight into the tyrosine phosphorylation in a non motile spermatozoon
Animal Reproduction Science, 2016Co-Authors: Hamid Niksirat, Liselotte Andersson, Marie Vancova, Antonin Kouba, Peter James, Pavel KozakAbstract:After mating, Spermatophores of signal crayfish are stored on the body of the female for a period before fertilization. This study compared the post-mating protein profile and pattern of protein tyrosine phosphorylation of the signal crayfish Spermatophore to that of the freshly ejaculated Spermatophore and found substantial differences. Two major bands of tyrosine-phosphorylated proteins of molecular weights 10 and 50 kDa were observed in the freshly ejaculated Spermatophore of the signal crayfish. While the tyrosine-phosphorylated protein band with molecular weight 10 kDa was formed by protein(s) of similar pH, the band with molecular weight of 50 kDa consisted of proteins of varying pH. In the post-mating Spermatophore, the band with molecular weight of 50 kDa was not detected, and an increase in the level of protein tyrosine phosphorylation was observed in the 10 kDa band. The microtubular radial arms of the spermatozoon showed a positive reaction to an anti-tyrosine antibody conjugated with gold particles in both the freshly ejaculated and post-mating Spermatophores. In conclusion, the male gamete of the signal crayfish undergoes molecular modification during post-mating storage on the body of the female including changes in the level of protein expression and protein tyrosine phosphorylation. Structural similarity of the radial arms in the crayfish immotile spermatozoon with flagellum, which is the main site of protein tyrosine phosphorylation in the mammalian motile spermatozoa, raises questions regarding evolution and function of such organelles across the animal kingdom that must be addressed in the future studies.
-
subcellular localization of calcium deposits in the noble crayfish astacus astacus Spermatophore implications for post mating Spermatophore hardening and spermatozoon maturation
Journal of Morphology, 2016Co-Authors: Hamid Niksirat, Antonin KoubaAbstract:The freshly ejaculated Spermatophore of crayfish undergoes a hardening process during post-mating storage on the body surface of female. The ultrastructural distribution of calcium deposits were studied and compared in freshly ejaculated and post-mating noble crayfish Spermatophores, using the oxalate-pyroantimonate technique, to determine possible roles of calcium in post-mating Spermatophore hardening and spermatozoon maturation. Small particles of sparsely distributed calcium deposits were visible in the wall of freshly ejaculated Spermatophore. Also, large amount of calcium deposits were visible in the membranes of the freshly ejaculated spermatozoon. Five minutes post-ejaculation, granules in the Spermatophore wall appeared as porous formations with numerous electron lucent spaces. Calcium deposits were visible within the spaces and scattered in the Spermatophore wall matrix, where smaller calcium deposits combined to form globular calcium deposits. Large numbers of the globular calcium deposits were visible in the wall of the post-mating Spermatophore. Smaller calcium deposits were detected in the central area of post-mating Spermatophore, which contains the sperm mass, and in the extracellular matrix and capsule. While the density of calcium deposits decreased in the post-mating spermatozoon membranes, numerous small calcium deposits appeared in the subacrosomal zone and nucleus. Substantial changes in calcium deposit distribution in the crayfish Spermatophore during post-mating storage on the body of female may be involved in the processes of the Spermatophore hardening and spermatozoon maturation. J. Morphol. 277:445–452, 2016. © 2016 Wiley Periodicals, Inc.
-
label free protein quantification in freshly ejaculated versus post mating Spermatophores of the noble crayfish astacus astacus
Journal of Proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p<0.05, fold change ≥2). The highest rate of up-regulation was observed in sodium/hydrogen exchanger, which may indicate the importance of intracellular pH adjustment for final maturation of the crayfish spermatozoon. The highest rate of down-regulation was observed in histone H2A. This may increase chromatin flexibility and facilitate its transfer into the oocyte during fertilization. The vitellogenin protein was identified in the crayfish Spermatophore and its level changed during storage on the body surface of female. Extensive proteomic modification of male gametes during storage on the body surface of the female suggests post-mating final maturation of the crayfish spermatozoon. (Less)
-
Label-free protein quantification in freshly ejaculated versus post-mating Spermatophores of the noble crayfish Astacus astacus.
Journal of proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p
Peter James - One of the best experts on this subject based on the ideXlab platform.
-
protein modification in the post mating Spermatophore of the signal crayfish pacifastacus leniusculus insight into the tyrosine phosphorylation in a non motile spermatozoon
Animal Reproduction Science, 2016Co-Authors: Hamid Niksirat, Liselotte Andersson, Marie Vancova, Antonin Kouba, Peter James, Pavel KozakAbstract:After mating, Spermatophores of signal crayfish are stored on the body of the female for a period before fertilization. This study compared the post-mating protein profile and pattern of protein tyrosine phosphorylation of the signal crayfish Spermatophore to that of the freshly ejaculated Spermatophore and found substantial differences. Two major bands of tyrosine-phosphorylated proteins of molecular weights 10 and 50 kDa were observed in the freshly ejaculated Spermatophore of the signal crayfish. While the tyrosine-phosphorylated protein band with molecular weight 10 kDa was formed by protein(s) of similar pH, the band with molecular weight of 50 kDa consisted of proteins of varying pH. In the post-mating Spermatophore, the band with molecular weight of 50 kDa was not detected, and an increase in the level of protein tyrosine phosphorylation was observed in the 10 kDa band. The microtubular radial arms of the spermatozoon showed a positive reaction to an anti-tyrosine antibody conjugated with gold particles in both the freshly ejaculated and post-mating Spermatophores. In conclusion, the male gamete of the signal crayfish undergoes molecular modification during post-mating storage on the body of the female including changes in the level of protein expression and protein tyrosine phosphorylation. Structural similarity of the radial arms in the crayfish immotile spermatozoon with flagellum, which is the main site of protein tyrosine phosphorylation in the mammalian motile spermatozoa, raises questions regarding evolution and function of such organelles across the animal kingdom that must be addressed in the future studies.
-
label free protein quantification in freshly ejaculated versus post mating Spermatophores of the noble crayfish astacus astacus
Journal of Proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p<0.05, fold change ≥2). The highest rate of up-regulation was observed in sodium/hydrogen exchanger, which may indicate the importance of intracellular pH adjustment for final maturation of the crayfish spermatozoon. The highest rate of down-regulation was observed in histone H2A. This may increase chromatin flexibility and facilitate its transfer into the oocyte during fertilization. The vitellogenin protein was identified in the crayfish Spermatophore and its level changed during storage on the body surface of female. Extensive proteomic modification of male gametes during storage on the body surface of the female suggests post-mating final maturation of the crayfish spermatozoon. (Less)
-
Label-free protein quantification in freshly ejaculated versus post-mating Spermatophores of the noble crayfish Astacus astacus.
Journal of proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p
Liselotte Andersson - One of the best experts on this subject based on the ideXlab platform.
-
protein modification in the post mating Spermatophore of the signal crayfish pacifastacus leniusculus insight into the tyrosine phosphorylation in a non motile spermatozoon
Animal Reproduction Science, 2016Co-Authors: Hamid Niksirat, Liselotte Andersson, Marie Vancova, Antonin Kouba, Peter James, Pavel KozakAbstract:After mating, Spermatophores of signal crayfish are stored on the body of the female for a period before fertilization. This study compared the post-mating protein profile and pattern of protein tyrosine phosphorylation of the signal crayfish Spermatophore to that of the freshly ejaculated Spermatophore and found substantial differences. Two major bands of tyrosine-phosphorylated proteins of molecular weights 10 and 50 kDa were observed in the freshly ejaculated Spermatophore of the signal crayfish. While the tyrosine-phosphorylated protein band with molecular weight 10 kDa was formed by protein(s) of similar pH, the band with molecular weight of 50 kDa consisted of proteins of varying pH. In the post-mating Spermatophore, the band with molecular weight of 50 kDa was not detected, and an increase in the level of protein tyrosine phosphorylation was observed in the 10 kDa band. The microtubular radial arms of the spermatozoon showed a positive reaction to an anti-tyrosine antibody conjugated with gold particles in both the freshly ejaculated and post-mating Spermatophores. In conclusion, the male gamete of the signal crayfish undergoes molecular modification during post-mating storage on the body of the female including changes in the level of protein expression and protein tyrosine phosphorylation. Structural similarity of the radial arms in the crayfish immotile spermatozoon with flagellum, which is the main site of protein tyrosine phosphorylation in the mammalian motile spermatozoa, raises questions regarding evolution and function of such organelles across the animal kingdom that must be addressed in the future studies.
-
label free protein quantification in freshly ejaculated versus post mating Spermatophores of the noble crayfish astacus astacus
Journal of Proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p<0.05, fold change ≥2). The highest rate of up-regulation was observed in sodium/hydrogen exchanger, which may indicate the importance of intracellular pH adjustment for final maturation of the crayfish spermatozoon. The highest rate of down-regulation was observed in histone H2A. This may increase chromatin flexibility and facilitate its transfer into the oocyte during fertilization. The vitellogenin protein was identified in the crayfish Spermatophore and its level changed during storage on the body surface of female. Extensive proteomic modification of male gametes during storage on the body surface of the female suggests post-mating final maturation of the crayfish spermatozoon. (Less)
-
Label-free protein quantification in freshly ejaculated versus post-mating Spermatophores of the noble crayfish Astacus astacus.
Journal of proteomics, 2015Co-Authors: Hamid Niksirat, Liselotte Andersson, Antonin Kouba, Peter James, Pavel KozakAbstract:Crayfish Spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus Spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the Spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating Spermatophore that showed significant up-regulation and 4 significant down-regulations (p
