Characterisation of insulin-like growth factor receptors and insulin receptors in the human placenta using lectin affinity methods

Masnikosa, Romana; Baricevic, Ivona; Jones, David R.; Nedić, Olgica

doi:10.1016/j.ghir.2006.04.001

Cited by 26 publications

(27 citation statements)

References 43 publications

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“…[32][33][34][35][36][37][38][39][40][41][42][43] Proteolytic degradation of existing elastic fibers 28,[75][76][77] and the impaired formation of new elastic fibers have been Results of cell counting and DNA assays performed in time course fashion indicate that subconfluent cultures of AoSMCs maintained in serum-free medium rapidly (within the first 24 hours) up-regulate their proliferation rate in response to either 10 ng/ml of PDGF-BB or 100 ng/ml of IGF-2. In contrast, parallel cultures that were pretreated with 50 mU/ml of exogenous Nase and subsequently treated with the same concentrations of tested growth factors did not increase their proliferation rate as compared with untreated control cultures.…”

Section: Discussionmentioning

confidence: 99%

Neuraminidase-1, a Subunit of the Cell Surface Elastin Receptor, Desialylates and Functionally Inactivates Adjacent Receptors Interacting with the Mitogenic Growth Factors PDGF-BB and IGF-2

Hinek

Bodnaruk

Bunda

et al. 2008

The American Journal of Pathology

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We recently established that the elastin-binding protein, which is identical to the spliced variant of ␤-galactosidase, forms a cell surface-targeted complex with two proteins considered "classic lysosomal enzymes": protective protein/cathepsin A and neuraminidase-1 (Neu1). We also found that cell surface-residing Neu1 can desialylate neighboring microfibrillar glycoproteins and facilitate the deposition of insoluble elastin, which contributes to the maintenance of cellular quiescence. Here we provide evidence that cell surfaceresiding Neu1 contributes to a novel mechanism that limits cellular proliferation by desialylating cell membrane-residing sialoglycoproteins that directly propagate mitogenic signals. We demonstrated that treatment of cultured human aortic smooth muscle cells (SMCs) with either a sialidase inhibitor or an antibody that blocks Neu1 activity induced significant up-regulation in SMC proliferation in response to fetal bovine serum. Conversely, treatment with Clostridium perfringens neuraminidase (which is highly homologous to Neu1) decreased SMC proliferation, even in cultures that did not deposit elastin. Further, we found that pretreatment of aortic SMCs with exogenous neuraminidase abolished their mitogenic responses to recombinant platelet-derived growth factor (PDGF)-BB and insulin-like growth factor (IGF)-2 and that sialidosis fibroblasts (which are exclusively deficient in Neu1) were more responsive to PDGF-BB and IGF-2 compared with normal fibroblasts. Furthermore , we provide direct evidence that neuraminidase caused the desialylation of both PDGF and IGF-1 receptors and diminished the intracellular signals induced by the mitogenic ligands

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Section: Discussionmentioning

confidence: 99%

Neuraminidase-1, a Subunit of the Cell Surface Elastin Receptor, Desialylates and Functionally Inactivates Adjacent Receptors Interacting with the Mitogenic Growth Factors PDGF-BB and IGF-2

Hinek

Bodnaruk

Bunda

et al. 2008

The American Journal of Pathology

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“…The solubilised membrane preparation of human placental IGF and insulin receptors was obtained following the procedure described in the work of Masnikosa et al (8,9).…”

Section: Methodsmentioning

confidence: 99%

“…These receptors are heavily glycosylated (7). We have previously found certain differences in glycosylation between IGF and insulin receptors isolated from placentas of healthy mothers (8). The aim of this study was to investigate the N-glycans of IGF and insulin receptors originating from placentas of mothers with pregestational insulin de pendent diabetes mellitus (IDDM).…”

Section: Introductionmentioning

confidence: 99%

N-Glycosylation Pattern of Human Placental Insulin-Like Growth Factor and Insulin Receptors in Well-Controlled Pregestational Diabetes Mellitus

Robajac¹,

Masnikosa²,

Filimonović³

et al. 2012

Journal of Medical Biochemistry

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Summary: Diabetes mellitus is a complex disease that leads to alterations in the glycosylation of proteins. Insulin-like growth factor and insulin receptors are involved in the regulation of fetal and placental growth and development. In this work the N-glycans of these receptors, originating from placentas obtained from pregnancies complicated by pregestational insulin dependent diabetes mellitus, were studied. Dia betic mothers were under regular insulin therapy. Solubilised membrane samples from healthy and diabetic placentas were analysed using lectin-affinity chromatography. N-glycans bound to insulin-like growth factor and insulin receptors were studied in terms of their interaction with eleven aga rose--immobilised lectins: wheat germ agglutinin, succinyla ted wheat germ agglutinin, Ricinus communis agglutinin I, Sambucus nigra agglutinin, Erythrina cristagalli lectin, Ulex europaeus agglutinin, Lens culinaris agglutinin, Canavalia en siformis lectin, Phaseolus vulgaris erythro-and leukoagglutinin and Maackia amurensis agglutinin. A very similar type of N-glycans and content of the terminal saccharide residues were found in both groups of placentas. The results of this work suggest that the tight glycemic control may prevent alterations in the glycosylation of insulin-like growth factor and insulin receptors, thus maintaining physiological homeostasis during pregnancy and fetal growth.Keywords: diabetes mellitus, insulin-like growth factor receptors, insulin receptor, N-glycosylation, placenta Kratak sadr`aj: Dijabetes melitus je kompleksno oboljenje koje uzrokuje promene u na~inu glikozilovanja prote ina. Receptori za insulin i insulinu sli~ne faktore rasta u~es -tvuju u regulaciji rasta i razvitka fetusa i placente. U ovom radu ispitivani su N-glikani vezani kovalentnom vezom za pome nute receptore. Receptori za insulin i insulinu sli~ne faktore rasta dobijeni su iz placenti majki sa pregestacijskim insu lin-zavisnim dijabetesom. Dijabeti~ne majke bile su na re dov noj terapiji insulinom. Uzorci }elijskih membrana, izolovani i solubilizovani iz placenti zdravih majki i majki sa dijabetesom, analizirani su primenom lektinske afinitetne hromatografije. Ispitivana je interakcija N-glikana vezanih za receptore sa jedanaest razli~itih lektina, imobilisanih na agaroznom gelu: lektin iz p{eni~nih klica, sukcinilovani lektin iz p{eni~nih klica, Ricinus communis lektin I, lektin iz kore zove, lektin iz koralnog drveta, lektin iz Ulex europaeus-a, lektin iz so~iva, konkanavalin A, dva lektina iz pasulja i lektin iz Maackia amurensis-a. Rezultati ovog rada pokazali su da receptori za insulin i insulinu sli~ne faktore rasta poreklom iz humane placente zdravih majki i onih sa pregestacijskim dijabetesom imaju veoma sli~an tip N-glikana kao i sastav terminalnih ostataka saharida, {to ukazuje na to da se dobrom kontrolom glikemije kod trudnica sa dijabetesom mogu spre~iti promene u na~inu gliko zilova nja ovih receptora, ~ime bi se pomoglo odr`avanju fiziolo{ke homeostaze za vreme rasta fetusa.

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“…Experiments were performed in triplicate. Ligand binding to different membrane proteins was expressed as the percentage of the total radioactivity eluted and was used as a measure of receptor and IGFBP abundance in the solubilised membranes for each 125 I-ligand (28).…”

Section: Gel Filtrationmentioning

confidence: 99%

Receptors and Binding Proteins for Insulin and Insulin-Like Growth Factors in the Placenta of Healthy Mothers and Mothers with Insulin-Dependent Diabetes Mellitus

Weber¹,

Baričević-Jones²,

Masnikosa³

et al. 2009

Journal of Medical Biochemistry

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Receptors and Binding Proteins for Insulin and Insulin-Like Growth Factors in the Placenta of Healthy Mothers and Mothers with Insulin-Dependent Diabetes Mellitus The IGF system of human placenta consists of insulin-like growth factors (IGF)-I and -II, their receptors (IGF-1R and IGF-2R), and binding proteins (IGFBP-1 to -6). Due to many structural and metabolic similarities with insulin, the IGF system cannot be examined separately from insulin and its receptor (IR). In this study gel filtration was used to detect solubilized membrane proteins of the placenta obtained from healthy mothers and mothers with IDDM. In order to detect placental membrane proteins that bind IGF molecules (and insulin), the solubilized membranes were incubated with each of the three 125I-labelled ligands: 125I-IGF-I, 125I-IGF-II and 125I-insulin prior to gel filtration chromatography. The biochemical evidence of the presence of receptors for insulin and IGFs, as well as that of IGFBP-1 were obtained by immunoblotting. Herein we demonstrated that, considering IGF and insulin receptor content, the placental tissue obtained from mothers with IDDM was not different from that obtained from healthy mothers. However, the concentration of IGFBP-1 differed between the examined placentas. IDDM in mothers caused an increase in the amount of IGFBP-1 in their placentas and, consequently, the amount of the labelled ligand bound to it. The redistribution of IGFs between the receptors and IGFBP-1 may be involved in regulatory mechanisms in the placenta of mothers with IDDM.

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Characterisation of insulin-like growth factor receptors and insulin receptors in the human placenta using lectin affinity methods

Cited by 26 publications

References 43 publications

Neuraminidase-1, a Subunit of the Cell Surface Elastin Receptor, Desialylates and Functionally Inactivates Adjacent Receptors Interacting with the Mitogenic Growth Factors PDGF-BB and IGF-2

Neuraminidase-1, a Subunit of the Cell Surface Elastin Receptor, Desialylates and Functionally Inactivates Adjacent Receptors Interacting with the Mitogenic Growth Factors PDGF-BB and IGF-2

N-Glycosylation Pattern of Human Placental Insulin-Like Growth Factor and Insulin Receptors in Well-Controlled Pregestational Diabetes Mellitus

Receptors and Binding Proteins for Insulin and Insulin-Like Growth Factors in the Placenta of Healthy Mothers and Mothers with Insulin-Dependent Diabetes Mellitus

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