ArticleDiabetologia2012
Disruption of the association of integrin-associated protein (IAP) with tyrosine phosphatase non-receptor type substrate-1 (SHPS)-1 inhibits pathophysiological changes in retinal endothelial function in a rat model of diabetes.
Article in Diabetologia, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- The Role and Diagnostic Potential of Insulin-like Growth Factor 1 in Diabetic Retinopathy and Diabetic Macular Edema.International journal of molecular sciences · 2025Review
- Metabolic regulation of microglial phagocytosis: Implications for Alzheimer's disease therapeutics.Translational neurodegeneration · 2023Review
- A Potential Role of the CD47/SIRPalpha Axis in COVID-19 Pathogenesis.Current issues in molecular biology · 2021Article
- Thrombospondin 1 in Metabolic Diseases.Frontiers in endocrinology · 2021Review
- IGF-1 and cardiovascular disease.Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society · 2019Review
- Inhibition of Aberrant IGF-I Signaling in Diabetic Male Rat Retina Prevents and Reverses Changes of Diabetic Retinopathy.Journal of diabetes research · 2019Article
- Blocking ligand occupancy of the αVβ3 integrin inhibits the development of nephropathy in diabetic pigs.Endocrinology · 2014Article
- Blocking αVβ3 integrin ligand occupancy inhibits the progression of albuminuria in diabetic rats.Journal of diabetes research · 2014Article
- Endothelial NADPH oxidase 4 mediates vascular endothelial growth factor receptor 2-induced intravitreal neovascularization in a rat model of retinopathy of prematurity.Molecular vision · 2014Article
- Insulin-like growth factor (IGF) binding protein 2 functions coordinately with receptor protein tyrosine phosphatase β and the IGF-I receptor to regulate IGF-I-stimulated signaling.Molecular and cellular biology · 2012Article
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6 authors at 2 institutions in 1 country.
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Abstract
aims/hypothesisWe have previously shown that the association of integrin-associated protein (IAP) with tyrosine phosphatase non-receptor type substrate-1 (SHPS-1) regulates the response of cells, including osteoclasts, osteoblasts, smooth muscle and retinal endothelial cells, to IGF-I. Here we sought to: (1) determine whether the regulation of IGF-I responsiveness by the association of IAP with SHPS-1 is a generalised response of endothelial cells; (2) identify the mechanism by which this association contributes to changes in endothelial cell responses to IGF-I; and (3) determine whether inhibition of this association alters pathophysiological changes occurring in vivo.
methodsEndothelial cells were maintained in 5 mmol/l glucose and at hyperglycaemic levels, and exposed to an anti-IAP antibody that disrupts the association between IAP and SHPS-1. A rodent model of diabetes with endothelial cell dysfunction was used to investigate the role of the association of IAP with SHPS-1 in endothelial cell function in vivo.
resultsEndothelial cells maintained in 5 mmol/l glucose showed constitutive cleavage of the extracellular domain of IAP (which contains the SHPS-1 binding site), with no association between IAP and SHPS-1 being detected. In contrast, hyperglycaemia inhibited IAP cleavage, allowing IAP to associate with SHPS-1 and IGF-I to stimulate SHPS-1 tyrosine phosphorylation. Exposure to the anti-IAP antibody inhibited IGF-I-stimulated tube formation and increased permeability. In the rodent model, basal IAP-SHPS-1 association was not detected in retinal extracts from normal rats, but was fully restored in rats with diabetes. The anti-IAP antibody inhibited the association of IAP with SHPS-1, and reduced retinal vascular permeability and leucocyte adherence to levels similar to those in non-diabetic rats. The antibody also significantly inhibited the aberrant neovascularisation induced by hypoxia. CONCLUSIONS/
interpretationOur results demonstrate that the increased association of IAP with SHPS-1 contributes to the pathophysiological changes in the endothelium that are induced by hyperglycaemia and hypoxia.
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