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Alteration of IGFBP-1 in Soccer Players Due to Intensive Training

Само за регистроване кориснике
2013
Аутори
Lagundzin, Dragana
Vučić, Vesna M.
Glibetić, Marija
Nedić, Olgica
Чланак у часопису (Објављена верзија)
Метаподаци
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Апстракт
Physical activity is accompanied by the changes in Insulin-like Growth Factor I (IGF-I)/IGF-Binding Protein 1 (IGFBP-1) axis. Inconsistent results concerning IGF-I and IGFBP-1 levels were reported. In this study we have raised some questions on the events that occur at the molecular level of the exercise-related IGFBP-1 changes. We have examined the fragmentation pattern of IGFBP-1, IGFBP-1 protease activity, interaction between IGFBP-1 and alpha2-macroglobulin (alpha 2M), and possible existence of minor structural changes of IGFBP-1 in professional soccer players. Athletes had significantly greater amounts of fragmented IGFBP-1, whereas no difference was found in the amount of intact IGFBP-1 compared with controls. An increased activity of matrix metalloprotease-9 (MMP-9) was detected in athletes, causing IGFBP-1 degradation down to the fragment of 9 kDa as the major one. The amount of alpha 2M, which protects IGFBP-1 from proteolysis, or the amount of IGFBP-1/alpha 2M complexes was u...naltered. Finally, we have examined whether IGFBP-1 isolated from soccer players exhibited altered reactivity with several chemical surfaces used in surface-enhanced laser desorption/ionization-time of flight mass spectrometry (SELDI-TOF MS). Different reactivity was detected with anion and cation exchangers, suggesting existence of at least one sequence within IGFBP-1, whose ionization pattern was not equal in athletes and controls. Differences in spectra obtained with ion exchanges may reflect differences in IGFBP-1 phosphorylation. Physiological implications of the events described in this study on the IGF-I availability are, at this time, unknown. It can be hypothesized that IGFBP-1 proteolysis leads to altered distribution of IGF-I among IGFBPs, which may affect the final IGF-associated response.

Кључне речи:
IGFBP-1 / soccer players / proteolysis / SELDI-TOF MS
Извор:
International Journal of Sport Nutrition & Exercise Metabolism, 2013, 23, 5, 449-457
Издавач:
  • Human Kinetics Publ Inc, Champaign
Финансирање / пројекти:
  • Структурне карактеристике везујућих протеина и рецептора за инсулину сличне факторе раста (IGF), њихове интеракције са другим физиолошким молекулима и промене код поремећаја метаболизма (RS-173042)

DOI: 10.1123/ijsnem.23.5.449

ISSN: 1526-484X

PubMed: 23535908

WoS: 000327285200004

Scopus: 2-s2.0-84888807209
[ Google Scholar ]
3
2
URI
http://rimi.imi.bg.ac.rs/handle/123456789/482
Колекције
  • Radovi istraživača / Researchers' publications
Институција/група
Institut za medicinska istraživanja
TY  - JOUR
AU  - Lagundzin, Dragana
AU  - Vučić, Vesna M.
AU  - Glibetić, Marija
AU  - Nedić, Olgica
PY  - 2013
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/482
AB  - Physical activity is accompanied by the changes in Insulin-like Growth Factor I (IGF-I)/IGF-Binding Protein 1 (IGFBP-1) axis. Inconsistent results concerning IGF-I and IGFBP-1 levels were reported. In this study we have raised some questions on the events that occur at the molecular level of the exercise-related IGFBP-1 changes. We have examined the fragmentation pattern of IGFBP-1, IGFBP-1 protease activity, interaction between IGFBP-1 and alpha2-macroglobulin (alpha 2M), and possible existence of minor structural changes of IGFBP-1 in professional soccer players. Athletes had significantly greater amounts of fragmented IGFBP-1, whereas no difference was found in the amount of intact IGFBP-1 compared with controls. An increased activity of matrix metalloprotease-9 (MMP-9) was detected in athletes, causing IGFBP-1 degradation down to the fragment of 9 kDa as the major one. The amount of alpha 2M, which protects IGFBP-1 from proteolysis, or the amount of IGFBP-1/alpha 2M complexes was unaltered. Finally, we have examined whether IGFBP-1 isolated from soccer players exhibited altered reactivity with several chemical surfaces used in surface-enhanced laser desorption/ionization-time of flight mass spectrometry (SELDI-TOF MS). Different reactivity was detected with anion and cation exchangers, suggesting existence of at least one sequence within IGFBP-1, whose ionization pattern was not equal in athletes and controls. Differences in spectra obtained with ion exchanges may reflect differences in IGFBP-1 phosphorylation. Physiological implications of the events described in this study on the IGF-I availability are, at this time, unknown. It can be hypothesized that IGFBP-1 proteolysis leads to altered distribution of IGF-I among IGFBPs, which may affect the final IGF-associated response.
PB  - Human Kinetics Publ Inc, Champaign
T2  - International Journal of Sport Nutrition & Exercise Metabolism
T1  - Alteration of IGFBP-1 in Soccer Players Due to Intensive Training
EP  - 457
IS  - 5
SP  - 449
VL  - 23
DO  - 10.1123/ijsnem.23.5.449
ER  - 
@article{
author = "Lagundzin, Dragana and Vučić, Vesna M. and Glibetić, Marija and Nedić, Olgica",
year = "2013",
abstract = "Physical activity is accompanied by the changes in Insulin-like Growth Factor I (IGF-I)/IGF-Binding Protein 1 (IGFBP-1) axis. Inconsistent results concerning IGF-I and IGFBP-1 levels were reported. In this study we have raised some questions on the events that occur at the molecular level of the exercise-related IGFBP-1 changes. We have examined the fragmentation pattern of IGFBP-1, IGFBP-1 protease activity, interaction between IGFBP-1 and alpha2-macroglobulin (alpha 2M), and possible existence of minor structural changes of IGFBP-1 in professional soccer players. Athletes had significantly greater amounts of fragmented IGFBP-1, whereas no difference was found in the amount of intact IGFBP-1 compared with controls. An increased activity of matrix metalloprotease-9 (MMP-9) was detected in athletes, causing IGFBP-1 degradation down to the fragment of 9 kDa as the major one. The amount of alpha 2M, which protects IGFBP-1 from proteolysis, or the amount of IGFBP-1/alpha 2M complexes was unaltered. Finally, we have examined whether IGFBP-1 isolated from soccer players exhibited altered reactivity with several chemical surfaces used in surface-enhanced laser desorption/ionization-time of flight mass spectrometry (SELDI-TOF MS). Different reactivity was detected with anion and cation exchangers, suggesting existence of at least one sequence within IGFBP-1, whose ionization pattern was not equal in athletes and controls. Differences in spectra obtained with ion exchanges may reflect differences in IGFBP-1 phosphorylation. Physiological implications of the events described in this study on the IGF-I availability are, at this time, unknown. It can be hypothesized that IGFBP-1 proteolysis leads to altered distribution of IGF-I among IGFBPs, which may affect the final IGF-associated response.",
publisher = "Human Kinetics Publ Inc, Champaign",
journal = "International Journal of Sport Nutrition & Exercise Metabolism",
title = "Alteration of IGFBP-1 in Soccer Players Due to Intensive Training",
pages = "457-449",
number = "5",
volume = "23",
doi = "10.1123/ijsnem.23.5.449"
}
Lagundzin, D., Vučić, V. M., Glibetić, M.,& Nedić, O.. (2013). Alteration of IGFBP-1 in Soccer Players Due to Intensive Training. in International Journal of Sport Nutrition & Exercise Metabolism
Human Kinetics Publ Inc, Champaign., 23(5), 449-457.
https://doi.org/10.1123/ijsnem.23.5.449
Lagundzin D, Vučić VM, Glibetić M, Nedić O. Alteration of IGFBP-1 in Soccer Players Due to Intensive Training. in International Journal of Sport Nutrition & Exercise Metabolism. 2013;23(5):449-457.
doi:10.1123/ijsnem.23.5.449 .
Lagundzin, Dragana, Vučić, Vesna M., Glibetić, Marija, Nedić, Olgica, "Alteration of IGFBP-1 in Soccer Players Due to Intensive Training" in International Journal of Sport Nutrition & Exercise Metabolism, 23, no. 5 (2013):449-457,
https://doi.org/10.1123/ijsnem.23.5.449 . .

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