TY  - JOUR
AU  - Pallavicini, A
AU  - Kojić, Snežana
AU  - Bean, C
AU  - Vainzof, M
AU  - Salamon, M
AU  - Ievolella, C
AU  - Bortoletto, G
AU  - Pacchioni, B
AU  - Zatz, M
AU  - Lanfranchi, G
AU  - Faulkner, G
AU  - Valle, G
PY  - 2001
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/148
AB  - Human Ankrd2 transcript encodes a 37-kDa protein that is similar to mouse Ankrd2 recently shown to be involved in hypertrophy of skeletal muscle. These novel ankyrin-rich proteins are related to C-193/CARP/MARP, a cardiac protein involved in the control of cardiac hypertrophy. A human genomic region of 14,300 bp was sequenced revealing a gene organization similar to mouse Ankrd2 with nine exons, four of which encode ankyrin repeats. The intracellular localization of Ankrd2 was unknown since no protein studies had been reported. In this paper we studied the intracellular localization of the protein and its expression on differentiation using polyclonal and monoclonal antibodies produced to human Ankrd2. In adult skeletal muscle Ankrd2 is found in slow fibers; however, not all of the slow fibers express Ankrd2 at the same level. This is particularly evident in dystrophic muscles, where the expression of Ankrd2 in slow fibers seems to be severely reduced.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Biochemical and Biophysical Research Communications
T1  - Characterization of human skeletal muscle Ankrd2
EP  - 386
IS  - 2
SP  - 378
VL  - 285
DO  - 10.1006/bbrc.2001.5131
ER  - 

@article{
author = "Pallavicini, A and Kojić, Snežana and Bean, C and Vainzof, M and Salamon, M and Ievolella, C and Bortoletto, G and Pacchioni, B and Zatz, M and Lanfranchi, G and Faulkner, G and Valle, G",
year = "2001",
abstract = "Human Ankrd2 transcript encodes a 37-kDa protein that is similar to mouse Ankrd2 recently shown to be involved in hypertrophy of skeletal muscle. These novel ankyrin-rich proteins are related to C-193/CARP/MARP, a cardiac protein involved in the control of cardiac hypertrophy. A human genomic region of 14,300 bp was sequenced revealing a gene organization similar to mouse Ankrd2 with nine exons, four of which encode ankyrin repeats. The intracellular localization of Ankrd2 was unknown since no protein studies had been reported. In this paper we studied the intracellular localization of the protein and its expression on differentiation using polyclonal and monoclonal antibodies produced to human Ankrd2. In adult skeletal muscle Ankrd2 is found in slow fibers; however, not all of the slow fibers express Ankrd2 at the same level. This is particularly evident in dystrophic muscles, where the expression of Ankrd2 in slow fibers seems to be severely reduced.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Biochemical and Biophysical Research Communications",
title = "Characterization of human skeletal muscle Ankrd2",
pages = "386-378",
number = "2",
volume = "285",
doi = "10.1006/bbrc.2001.5131"
}

Pallavicini, A., Kojić, S., Bean, C., Vainzof, M., Salamon, M., Ievolella, C., Bortoletto, G., Pacchioni, B., Zatz, M., Lanfranchi, G., Faulkner, G.,& Valle, G.. (2001). Characterization of human skeletal muscle Ankrd2. in Biochemical and Biophysical Research Communications
Academic Press Inc Elsevier Science, San Diego., 285(2), 378-386.
https://doi.org/10.1006/bbrc.2001.5131

Pallavicini A, Kojić S, Bean C, Vainzof M, Salamon M, Ievolella C, Bortoletto G, Pacchioni B, Zatz M, Lanfranchi G, Faulkner G, Valle G. Characterization of human skeletal muscle Ankrd2. in Biochemical and Biophysical Research Communications. 2001;285(2):378-386.
doi:10.1006/bbrc.2001.5131 .

Pallavicini, A, Kojić, Snežana, Bean, C, Vainzof, M, Salamon, M, Ievolella, C, Bortoletto, G, Pacchioni, B, Zatz, M, Lanfranchi, G, Faulkner, G, Valle, G, "Characterization of human skeletal muscle Ankrd2" in Biochemical and Biophysical Research Communications, 285, no. 2 (2001):378-386,
https://doi.org/10.1006/bbrc.2001.5131 . .

TY  - JOUR
AU  - Faulkner, G
AU  - Pallavicini, A
AU  - Comelli, A
AU  - Salamon, M
AU  - Bortoletto, G
AU  - Ievolella, C
AU  - Trevisan, S
AU  - Kojić, Snežana
AU  - Dalla Vecchia, F
AU  - Laveder, P
AU  - Valle, G
AU  - Lanfranchi, G
PY  - 2000
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/142
AB  - We report the identification and characterization of a novel 32-kDa protein expressed in skeletal muscle and located in the Z-disc of the sarcomere. We found that this protein binds to three other Z-disc proteins; therefore, we have-named it FATZ, gamma -filamin/ABP-L, alpha -actinin and telethonin binding protein of the Z-disc. From yeast two-hybrid experiments we are able to show that the SR3-SR4 domains of alpha -actinin 2 are required to bind the COOH-terminal region of the FATZ as does gamma -filamin/ABP-L, Furthermore, by using a glutathione S-transferase overlay assay we find that FATZ also binds telethonin. The level of FATZ protein in muscle cells increases during differentiation, being clearly detectable before the onset of myosin, Although FATZ has no known interaction domains, it would appear to be involved in a complex network of interactions with other Z-band components. On the basis of the information known about its binding partners, we could envisage a central role for FATZ in the: myofibrillogenesis, After screening our muscle expressed sequence tag data base and the public expressed sequence tag data bases, we were able to assemble two other muscle transcripts that show a high level of identity with FATZ in two different domains. Therefore, FATZ may be the first member of a small family of novel muscle proteins.
PB  - Amer Soc Biochemistry Molecular Biology Inc, Rockville
T2  - Journal of Biological Chemistry
T1  - FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle
EP  - 41242
IS  - 52
SP  - 41234
VL  - 275
DO  - 10.1074/jbc.M007493200
ER  - 

@article{
author = "Faulkner, G and Pallavicini, A and Comelli, A and Salamon, M and Bortoletto, G and Ievolella, C and Trevisan, S and Kojić, Snežana and Dalla Vecchia, F and Laveder, P and Valle, G and Lanfranchi, G",
year = "2000",
abstract = "We report the identification and characterization of a novel 32-kDa protein expressed in skeletal muscle and located in the Z-disc of the sarcomere. We found that this protein binds to three other Z-disc proteins; therefore, we have-named it FATZ, gamma -filamin/ABP-L, alpha -actinin and telethonin binding protein of the Z-disc. From yeast two-hybrid experiments we are able to show that the SR3-SR4 domains of alpha -actinin 2 are required to bind the COOH-terminal region of the FATZ as does gamma -filamin/ABP-L, Furthermore, by using a glutathione S-transferase overlay assay we find that FATZ also binds telethonin. The level of FATZ protein in muscle cells increases during differentiation, being clearly detectable before the onset of myosin, Although FATZ has no known interaction domains, it would appear to be involved in a complex network of interactions with other Z-band components. On the basis of the information known about its binding partners, we could envisage a central role for FATZ in the: myofibrillogenesis, After screening our muscle expressed sequence tag data base and the public expressed sequence tag data bases, we were able to assemble two other muscle transcripts that show a high level of identity with FATZ in two different domains. Therefore, FATZ may be the first member of a small family of novel muscle proteins.",
publisher = "Amer Soc Biochemistry Molecular Biology Inc, Rockville",
journal = "Journal of Biological Chemistry",
title = "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle",
pages = "41242-41234",
number = "52",
volume = "275",
doi = "10.1074/jbc.M007493200"
}

Faulkner, G., Pallavicini, A., Comelli, A., Salamon, M., Bortoletto, G., Ievolella, C., Trevisan, S., Kojić, S., Dalla Vecchia, F., Laveder, P., Valle, G.,& Lanfranchi, G.. (2000). FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. in Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc, Rockville., 275(52), 41234-41242.
https://doi.org/10.1074/jbc.M007493200

Faulkner G, Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojić S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G. FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. in Journal of Biological Chemistry. 2000;275(52):41234-41242.
doi:10.1074/jbc.M007493200 .

Faulkner, G, Pallavicini, A, Comelli, A, Salamon, M, Bortoletto, G, Ievolella, C, Trevisan, S, Kojić, Snežana, Dalla Vecchia, F, Laveder, P, Valle, G, Lanfranchi, G, "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle" in Journal of Biological Chemistry, 275, no. 52 (2000):41234-41242,
https://doi.org/10.1074/jbc.M007493200 . .