IGFBP-1 forms associated with placental cell membranes

Masnikosa, Romana; Živković, Bogovid; Nedić, Olgica

doi:10.2298/jsc0907707m

Cited by 4 publications

(4 citation statements)

References 27 publications

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“…Tissue multimers were shown to have a very low binding capacity for IGF-I ( Sakai et al, 2001b ). In a ligand-blotting experiment with 125 I-IGF-I that we have carried out no protein bands were seen in the region of 60 -100 kDa ( Masnikosa 2009 ). A characteristic IGFBP-1 multimer pattern for each group studied in this work may have resulted from a diff erential presence of non-phosphorylated and several phosphorylated IGFBP-1 isoforms within multimers.…”

Section: Results ▼mentioning

confidence: 63%

“…Covalently linked IGFBP-1 multimers were detected in some tissues, a formation of which was catalyzed by transglutaminase ( Sakai et al, 2001b ). NpIGFBP-1 seems to polymerize more rapidly and to a greater extent compared to pIGFBP-1 ( Sakai et al, 2001b, Masnikosa 2009. A predominant multimeric IGFBP-1 form has a mass of 60 kDa, and a minor form of 90 -100 kDa ( Sakai et al, 2001b ).…”

Section: Results ▼mentioning

confidence: 99%

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Association between the Pattern of IGFBP-1 Alteration and the Glucose/Insulin Metabolic Control

Nedić

Masnikosa²,

Lagundžin³

2010

Exp Clin Endocrinol Diabetes

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Little is known on the possible association between impaired glucose/insulin metabolism, the pattern of IGFBP-1 phosphorylation and the complex formation with other serum proteins. In this study, the concentration, isoform, multimer and complex pattern of IGFBP-1 was compared in healthy persons and patients with type 2 diabetes mellitus or with hypoglycemia. Concentrations of insulin and IGFBP-1 were determined by radioimmunoassay. Metal affinity and immunoaffinity chromatography were used for the separation of molecular forms of IGFBP-1, which were detected by immunoblotting and SELDI. The counter directional change in insulin and IGFBP-1 concentrations, expressed as a factor that takes into consideration the rate of insulin increase and IGFBP-1 decrease after glucose intake was approximately twice more pronounced in patients with diabetes than in healthy and hypoglycemic persons. The alteration in the phosphorylation pattern of IGFBP-1 due to diabetes or hypoglycemia was not observed. IGFBP-1 multimers found in the circulation of patients with diabetes type 2 differed from those detected in the circulation of others: there were 3 molecular forms between 90 and 100 kDa (compared to one in patients with hypoglycemia or 2 in healthy persons), 2 of which were α (2)M-reactive and one not. These results suggest a possible greater involvement of IGF system in glucose regulation in patients with diabetes type 2.

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Section: Results ▼mentioning

confidence: 63%

Section: Results ▼mentioning

confidence: 99%

Association between the Pattern of IGFBP-1 Alteration and the Glucose/Insulin Metabolic Control

Nedić

Masnikosa²,

Lagundžin³

2010

Exp Clin Endocrinol Diabetes

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“…These complexes might contain polymers of IGFBP-1 or its connection to ALS subunit, and even less specific proteins, e.g. cell membrane proteins (Puche and Castilla-Cortàzar 2012;Masnikosa et al 2009). After the reduction in disulfide bonds, followed by decay of the complex, a new wide band of lower molecular weight (about 30 kDa) appeared, corresponding to a molecular weight of IGF-I or IGF-II connected to BP-1, and a few bands in the range of 65-120 kDa (Fig.…”

Section: Resultsmentioning

confidence: 99%

IGFs and IGF-Binding Proteins in the Synovial Fluid of Patients with Rheumatoid Arthritis and Osteoarthritis

Bączyk

Gogiel

Wolańska

et al. 2019

Int J Pept Res Ther

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The progressive damage of human articular cartilage is associated with loss of integrity of its extracellular matrix components. Their metabolism is under the control of cytokines produced locally. It is known that peptide growth factors stimulate chondrocytes to synthesize matrix components, and other cytokines, such as interleukins, promote their catabolism by stimulation of chondrocytes to the production of enzymes degrading components of cartilage. The aim of this study was evaluation the presence of inulin-like growth factors (IGFs) in synovial fluid and blood serum of patients with rheumatoid arthritis and osteoarthritis and their binding proteins and matrix metalloproteinases that regulate their bioavailability using Western Immunoblot, ELISA test and zymography technique. The results showed that both IGFs were present, first of all, in the form of high molecular complexes with their specific binding proteins. In this way those proteins prolonged growth factors' half-life but suppressed their bioavailability for receptors and action on target cells. Low content of free IGF-I indicated limitation of its anabolic influence on cartilage metabolism of patients with both diseases.

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“…16 Molecular mass markers were from BioRad Laboratories (Hertfordshire, UK) and the cytosol from human placental cells was used as a source of a physiological marker of IGFBP-1. 17…”

Section: Electrophoresis and Western Immunoblotting (Wib)mentioning

confidence: 99%

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

Lagundžin¹,

Masnikosa²,

Miljuš³

et al. 2010

JSCS

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Insulin-like growth factor-binding protein 1 (IGFBP-1) is a member of a family of six homologous proteins that regulate the action of the insulin-like growth factors. IGFBP-1 is a 25 kDa protein that beside its native form, may exist in several phosphoforms (30 kDa), which are predominant in the circulation of humans. Phosphorylation of IGFBP-1 is a post-translational modification that has a great influence on the IGF-I action. IGFBP-1 forms multimers and complexes with α2-macroglobulin (α2M). Polymerisation of IGFBP-1 was also reported. In order to analyse and separate these IGFBP-1 molecular species, affinity chromatography methods were used in this study. The results demonstrated that most of the IGFBP-1 circulates in complexes with α2M, which can be isolated by affinity chromatography using immobilised anti-α2M antibodies. IGFBP- 1/α2M complexes may be differentiated from IGFBP-1 dimer and multimers using lectin-affinity chromatography, since the latter do not interact with lectins. It seems that the complexes contain not only monomeric IGFBP-1, but also its multimers. Dimer and multimers are stable under reducing conditions, suggesting covalent linkage between units. Free IGFBP-1 monomer can be separated from multimers using Con A-affinity chromatography. The concentration of free IGFBP-1 is relatively low in the circulation

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IGFBP-1 forms associated with placental cell membranes

Cited by 4 publications

References 27 publications

Association between the Pattern of IGFBP-1 Alteration and the Glucose/Insulin Metabolic Control

Association between the Pattern of IGFBP-1 Alteration and the Glucose/Insulin Metabolic Control

IGFs and IGF-Binding Proteins in the Synovial Fluid of Patients with Rheumatoid Arthritis and Osteoarthritis

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

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