Investigation of different molecular forms of IGFBP-1 using immobilised metal-, immuno- and lectin-affinity chromatography

Lagundžin, Dragana; Masnikosa, Romana; Miljuš, Goran; Robajac, Dragana; Nedić, Olgica

doi:10.2298/jsc100330090l

Cited by 3 publications

(1 citation statement)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Electrophoresis under reducing conditions (SDS-PAGE, 12% gel) and immunoblotting were used for protein detection in sera (Lagundžin et al, 2010). Polyclonal affinity-purified goat anti-IGFBP-1 antibody (Santa Cruz Biotechnology) and HRP-conjugated swine antigoat antibody (Biosource, Camarillo, CA, USA) were used for the IGFBP-1 detection.…”

Section: Electrophoresis and Immunoblottingmentioning

confidence: 99%

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

Lagundžin

Vučić²,

Glibetić³

et al. 2013

International Journal of Sport Nutrition and Exercise Metabolism

View full text Add to dashboard Cite

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.

show abstract

Section: Electrophoresis and Immunoblottingmentioning

confidence: 99%

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

Lagundžin

Vučić²,

Glibetić³

et al. 2013

International Journal of Sport Nutrition and Exercise Metabolism

View full text Add to dashboard Cite

show abstract

Influence of placental mannose/N-acetyl glucosamine-binding proteins on the interaction of insulin and insulin-like growth factors with their receptors

Nedić

Filimonović

Miković

et al. 2011

Biochemistry Moscow

View full text Add to dashboard Cite

Placenta is a source of carbohydrate-binding proteins that function as molecular scavengers, but they could also be involved in interactions that assist in metabolic control. Mannose/N-acetyl-glucosamine (Man/GlcNAc)-binding proteins from placenta were isolated and their reactivity towards placental insulin and insulin-like growth factor receptors (IR and IGF-Rs) was analyzed. The lectins reduced the binding of insulin and IGF-I in a dose-dependent manner, while almost no effect was observed on the binding of IGF-II. The shape of the inhibition curves changed, suggesting altered binding specificity. The presence of sugar could not reverse completely the effect of the lectins, implicating both lectin-sugar and protein-protein conformational recognition. Since biological molecules in our experimental system were those that are in close relation in vivo, placental Man/GlcNAc-specific lectins may be regarded as potential allosteric modulators of ligand-receptor interactions in a system of homologous ligands, selectively affecting only binding to tyrosine kinase type receptors (IR and IGF-1R).

show abstract

Interaction between fibrinogen and insulin-like growth factor-binding protein-1 in human plasma under physiological conditions

Gligorijević¹,

Nedić²

2016

Biochemistry Moscow

View full text Add to dashboard Cite

Fibrinogen is a plasma glycoprotein and one of the principle participants in blood coagulation. It interacts with many proteins during formation of a blood clot, including insulin-like growth factors (IGFs) and their binding proteins (IGFBP). Fibrinogen complexes were found as minor fractions in fibrinogen preparations independently of the coagulation process, and their presence influences the kinetics of polymerization. The idea of this work was to investigate whether fibrinogen in human plasma interacts with IGFBPs independently of the tissue injury or coagulation process. The results have shown that fibrinogen forms complexes with IGFBP-1 under physiological conditions. Several experimental approaches have confirmed that complexes are co-isolated with fibrinogen from plasma, they are relatively stable, and they appear as a general feature of human plasma. Several other experiments excluded the possibility that alpha-2 macroglobulin/IGFBP-1 complexes or IGFBP-1 oligomers contributed to IGFBP-1 immunoreactivity. The role of fibrinogen/IGFBP-1 complexes is still unknown. Further investigation in individuals expressing both impaired glucose control and coagulopathy could contribute to identification and understanding of their possible physiological role.

show abstract

Investigation of different molecular forms of IGFBP-1 using immobilised metal-, immuno- and lectin-affinity chromatography

Cited by 3 publications

References 24 publications

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

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

Influence of placental mannose/N-acetyl glucosamine-binding proteins on the interaction of insulin and insulin-like growth factors with their receptors

Interaction between fibrinogen and insulin-like growth factor-binding protein-1 in human plasma under physiological conditions

Contact Info

Product

Resources

About