TY  - CONF
AU  - Novković, Mirjana
AU  - Vasić, Marko
AU  - Jasnić, Jovana
AU  - Milošević, Emilija
AU  - Milovanović, Mina
AU  - Savić, Slobodan
AU  - Kojić, Snežana
PY  - 2023
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2114
UR  - http://intor.torlakinstitut.com/handle/123456789/806
AB  - Introduction: Ankyrin Repeat Domain 2 (ANKRD2) is expressed in skeletal muscle, where plays a role inmuscle development, differentiation and adaptation to stress. Human skeletal muscle consists of threemajor fiber types: type 1 (slow-twitch, oxidative), type 2A (fast-twitch, oxidative) and type 2X (fast-twitch,glycolytic). ANKRD2 is reported to be primarily expressed in type 1 myofibers. However, recent findingson human single myofibers and our study of chicken muscles have shown that this protein may also beexpressed in type 2A fibers. Hence, our objective was to examine whether ANKRD2 is present in humanfast, type 2A muscle fibers using immunohistochemistry.Methods: Samples of large leg musclessoleus, gastrocnemius, vastusintermedius and vastuslateralis wereobtained from human cadaveric tissue. Serial cryosections were independently stained with anti-ANKRD2and antibodies for different myosin heavy chain isoforms (6H1 for type 2X, BF35 for type 1 and 2A, antiMHCs for type 1 and anti-MHCf for type 2A and 2X fibers). Immunostained tissues were analyzed by fluorescent microscopy.Results: In addition to slow, type 1, ANKRD2 wasfound expressed in fast, type 2A myofibers, which bothhave oxidative metabolism. Further, we did not observe ANDRD2 expression in glycolytic, type 2Xmyiofibers. This pattern of ANKRD2 expression was consistent across all examined muscles.Conclusion: Our resultsimplicate that the regulatory mechanism of ANKRD2 expression in human skeletal muscle is associated with oxidative metabolism, rather than muscle contraction speed.
PB  - Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade
C3  - CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
T1  - Determination of muscle fiber types expressing ANKRD2
EP  - 155
SP  - 155
UR  - https://hdl.handle.net/21.15107/rcub_intor_806
ER  - 

@conference{
author = "Novković, Mirjana and Vasić, Marko and Jasnić, Jovana and Milošević, Emilija and Milovanović, Mina and Savić, Slobodan and Kojić, Snežana",
year = "2023",
abstract = "Introduction: Ankyrin Repeat Domain 2 (ANKRD2) is expressed in skeletal muscle, where plays a role inmuscle development, differentiation and adaptation to stress. Human skeletal muscle consists of threemajor fiber types: type 1 (slow-twitch, oxidative), type 2A (fast-twitch, oxidative) and type 2X (fast-twitch,glycolytic). ANKRD2 is reported to be primarily expressed in type 1 myofibers. However, recent findingson human single myofibers and our study of chicken muscles have shown that this protein may also beexpressed in type 2A fibers. Hence, our objective was to examine whether ANKRD2 is present in humanfast, type 2A muscle fibers using immunohistochemistry.Methods: Samples of large leg musclessoleus, gastrocnemius, vastusintermedius and vastuslateralis wereobtained from human cadaveric tissue. Serial cryosections were independently stained with anti-ANKRD2and antibodies for different myosin heavy chain isoforms (6H1 for type 2X, BF35 for type 1 and 2A, antiMHCs for type 1 and anti-MHCf for type 2A and 2X fibers). Immunostained tissues were analyzed by fluorescent microscopy.Results: In addition to slow, type 1, ANKRD2 wasfound expressed in fast, type 2A myofibers, which bothhave oxidative metabolism. Further, we did not observe ANDRD2 expression in glycolytic, type 2Xmyiofibers. This pattern of ANKRD2 expression was consistent across all examined muscles.Conclusion: Our resultsimplicate that the regulatory mechanism of ANKRD2 expression in human skeletal muscle is associated with oxidative metabolism, rather than muscle contraction speed.",
publisher = "Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade",
journal = "CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia",
title = "Determination of muscle fiber types expressing ANKRD2",
pages = "155-155",
url = "https://hdl.handle.net/21.15107/rcub_intor_806"
}

Novković, M., Vasić, M., Jasnić, J., Milošević, E., Milovanović, M., Savić, S.,& Kojić, S.. (2023). Determination of muscle fiber types expressing ANKRD2. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade., 155-155.
https://hdl.handle.net/21.15107/rcub_intor_806

Novković M, Vasić M, Jasnić J, Milošević E, Milovanović M, Savić S, Kojić S. Determination of muscle fiber types expressing ANKRD2. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia. 2023;:155-155.
https://hdl.handle.net/21.15107/rcub_intor_806 .

Novković, Mirjana, Vasić, Marko, Jasnić, Jovana, Milošević, Emilija, Milovanović, Mina, Savić, Slobodan, Kojić, Snežana, "Determination of muscle fiber types expressing ANKRD2" in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia (2023):155-155,
https://hdl.handle.net/21.15107/rcub_intor_806 .

TY  - JOUR
AU  - Miljković, Marija
AU  - Strahinić, Ivana
AU  - Tolinački, Maja
AU  - Živković, Milica
AU  - Kojić, Snežana
AU  - Golić, Nataša
AU  - Kojić, Milan
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/805
UR  - http://intor.torlakinstitut.com/handle/123456789/685
AB  - Eleven Lactobacillus strains with strong aggregation abilities were selected from a laboratory collection. In two of the strains, genes associated with aggregation capability were plasmid located and found to strongly correlate with collagen binding. The gene encoding the auto-aggregation-promoting protein (AggLb) of Lactobacillus paracasei subsp. paracasei BGNJ1-64 was cloned using a novel, wide-range-host shuttle cloning vector, pAZILSJ. The clone pALb35, containing a 11377-bp DNA fragment, was selected from the SacI plasmid library for its ability to provide carriers with the aggregation phenotype. The complete fragment was sequenced and four potential ORFs were detected, including the aggLb gene and three surrounding transposase genes. AggLb is the largest known cell-surface protein in lactobacilli, consisting of 2998 aa (318,611 Da). AggLb belongs to the collagen-binding superfamily and its C-terminal region contains 20 successive repeats that are identical even at the nucleotide level. Deletion of aggLb causes a loss of the capacity to form cell aggregates, whereas overexpression increases cellular aggregation, hydrophobicity and collagen-binding potential. PCR screening performed with three sets of primers based on the aggLb gene of BGNJ1-64 enabled detection of the same type of aggLb gene in five of eleven selected aggregation-positive Lactobacillus strains. Heterologous expression of aggLb confirmed the crucial role of the AggLb protein in cell aggregation and specific collagen binding, indicating that AggLb has a useful probiotic function in effective colonization of host tissue and prevention of pathogen colonization.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro
IS  - 5
VL  - 10
DO  - 10.1371/journal.pone.0126387
ER  - 

@article{
author = "Miljković, Marija and Strahinić, Ivana and Tolinački, Maja and Živković, Milica and Kojić, Snežana and Golić, Nataša and Kojić, Milan",
year = "2015",
abstract = "Eleven Lactobacillus strains with strong aggregation abilities were selected from a laboratory collection. In two of the strains, genes associated with aggregation capability were plasmid located and found to strongly correlate with collagen binding. The gene encoding the auto-aggregation-promoting protein (AggLb) of Lactobacillus paracasei subsp. paracasei BGNJ1-64 was cloned using a novel, wide-range-host shuttle cloning vector, pAZILSJ. The clone pALb35, containing a 11377-bp DNA fragment, was selected from the SacI plasmid library for its ability to provide carriers with the aggregation phenotype. The complete fragment was sequenced and four potential ORFs were detected, including the aggLb gene and three surrounding transposase genes. AggLb is the largest known cell-surface protein in lactobacilli, consisting of 2998 aa (318,611 Da). AggLb belongs to the collagen-binding superfamily and its C-terminal region contains 20 successive repeats that are identical even at the nucleotide level. Deletion of aggLb causes a loss of the capacity to form cell aggregates, whereas overexpression increases cellular aggregation, hydrophobicity and collagen-binding potential. PCR screening performed with three sets of primers based on the aggLb gene of BGNJ1-64 enabled detection of the same type of aggLb gene in five of eleven selected aggregation-positive Lactobacillus strains. Heterologous expression of aggLb confirmed the crucial role of the AggLb protein in cell aggregation and specific collagen binding, indicating that AggLb has a useful probiotic function in effective colonization of host tissue and prevention of pathogen colonization.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro",
number = "5",
volume = "10",
doi = "10.1371/journal.pone.0126387"
}

Miljković, M., Strahinić, I., Tolinački, M., Živković, M., Kojić, S., Golić, N.,& Kojić, M.. (2015). AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro. in PLoS One
Public Library Science, San Francisco., 10(5).
https://doi.org/10.1371/journal.pone.0126387

Miljković M, Strahinić I, Tolinački M, Živković M, Kojić S, Golić N, Kojić M. AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro. in PLoS One. 2015;10(5).
doi:10.1371/journal.pone.0126387 .

Miljković, Marija, Strahinić, Ivana, Tolinački, Maja, Živković, Milica, Kojić, Snežana, Golić, Nataša, Kojić, Milan, "AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro" in PLoS One, 10, no. 5 (2015),
https://doi.org/10.1371/journal.pone.0126387 . .