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 (α2M), 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 α2M, which protects IGFBP-1 from proteolysis, or the amount of IGFBP-1/α2M 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.
Lagundžin and Nedić are with the Institute for the Application of Nuclear Energy, University of Belgrade, Belgrade, Serbia. Vučić and Glibetić are with the Institute for Medical Research, University of Belgrade, Belgrade, Serbia.