Expression of Prostacyclin-Stimulating Factor, a Novel Protein, in Tissues of Wistar Rats and in Cultured Cells

Ono, Yasuhiro; Hashimoto, Yoko; Umeda, Fumio; Masakado, Mitsunori; Yamauchi, Tatsuya; Mizushima, Seiichi; Isaji, Mitsuko; Nawata, Hajime

doi:10.1006/bbrc.1994.2099

Cited by 19 publications

(16 citation statements)

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“…PSF mRNA is readily detectable from total retina both in rats and neonatal mice. PSF mRNA and protein are expressed in numerous ocular cell types in vitro at levels comparable to those observed in AECs and SMCs (4,5,(7)(8)(9)(10)(11). We demonstrate that the constitutive expression in retinal microvascular pericytes is greater than threefold high- The ability of PSF in RPC-conditioned media to increase REC PGI2 production.…”

Section: Discussionmentioning

confidence: 60%

Retinal expression, regulation, and functional bioactivity of prostacyclin-stimulating factor

Hata¹,

Clermont²,

Yamauchi³

et al. 2000

J. Clin. Invest.

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Section: Discussionmentioning

confidence: 60%

Retinal expression, regulation, and functional bioactivity of prostacyclin-stimulating factor

Hata¹,

Clermont²,

Yamauchi³

et al. 2000

J. Clin. Invest.

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“…The disadvantage of Fetuin-A is that a defect in the method of separation and its detection and the sensitivity, efficiency, and quantification limits its clinical application [130]. The low separation and detection sensitivity and the shortcomings in the current methods of efficiency, identification, and quantification may all limit its clinical application [131].…”

Section: Fetuin-amentioning

confidence: 99%

Early Predictors of Acute Kidney Injury: A Narrative Review

Liu

Guan

et al. 2016

Kidney Blood Press Res

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Accompanied with the broad application of interventional therapy, the incidence of acute kidney injury (AKI) has been recently increasing in clinical renal medicine. The pathogenesis of AKI is diverse and complex. In the context of the requirements for the diagnosis and treatment of a renal disorder, a large number of studies have explored biological markers and their usefulness to the early diagnosis and treatment of AKI, including glomerular injury, renal tubular injury, and others. These biomarkers provide an important basis for early monitoring of AKI, but are still not quite sufficient. More ideal biomarkers are needed to be identified. Therefore, future studies are necessary to explore more effective biomarkers for AKI clinical practice, which would play an important role in the early diagnosis and intervention treatment of AKI. This review summarizes the important biomarkers identified by previous studies and aims to highlight the advancements that might provide new methods for early clinical diagnosis and effective therapeutic options, along with prediction of response to treatment for AKI.

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“…Diabetes 55: 2333-2339, 2006 T he IGF-binding protein (IGFBP) family of carriers of IGFs in biological fluids was recently expanded to include the IGFBP-related proteins (IGFBP-rPs), which not only share the conserved NH 2 -terminal domain of the IGFBPs, but also show some degree of affinity for IGFs in several, but not all, assay systems (1). IGFBP-rP1 (also known as MAC25, prostacyclin stimulating factor, and tumor-derived adhesion factor/angiomodulin), is a 30-kDa modular glycoprotein known to be secreted by endothelial cells, vascular smooth muscle cells, fibroblasts, and epithelial cells (2)(3)(4). Northern blot studies revealed a wide expression of this gene in humans, including heart, brain, placenta, liver, skeletal muscle, and pancreas (5), most probably because the protein is detected in the basement membrane of capillary vessels (6,7).…”

mentioning

confidence: 99%

Insulin Resistance Is Associated With Increased Serum Concentration of IGF-Binding Protein–Related Protein 1 (IGFBP-rP1/MAC25)

López‐Bermejo

Khosravi²,

Fernández-Real

et al. 2006

Diabetes

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IGF-binding protein (IGFBP)-related protein 1 (IGFBP-rP1) has been shown to bind both IGFs and insulin, albeit with low affinity, and to inhibit insulin signaling. We hypothesized that IGFBP-rP1 is associated with insulin resistance and components of the IGF system in humans. To this aim, a cross-sectional study was conducted in 113 nondiabetic and 43 type 2 diabetic men. Insulin sensitivity (insulin sensitivity index [S i ] from intravenous glucose tolerance tests in nondiabetic subjects, or the rate constant for disappearance of glucose [K ITT ] from insulin tolerance tests in type 2 diabetic subjects), circulating IGFBP-rP1 (from enzyme-linked immunosorbent assay), adiponectin (from radioimmunoassay), C-reactive protein (CRP; from immunoturbidimetry), soluble tumor necrosis factor receptor 2 (sTNFR2; from enzyme-amplified sensitivity immunoassay), and IGF system parameters (IGF-I, free IGF-I, and IGFBP-1 from immunoradiometric assay) were assessed in all subjects. Among nondiabetic men, those in the highest quartile for circulating IGFBP-rP1 exhibited decreased S i and adiponectin (both P < 0.01) as well as increased CRP and sTNFR2 (both P < 0.05). Circulating IGFBP-rP1 was also found to be increased in previously undiagnosed type 2 diabetic patients (P ‫؍‬ 0.01) but not in known type 2 diabetic patients receiving pharmacological therapy. Although no changes in IGF system components were evident by IGFBP-rP1 quartiles in nondiabetic subjects, independent positive associations of IGFBP-rP1 with circulating fasting IGFBP-1 were evident after adjustment for insulin resistance parameters in both nondiabetic and type 2 diabetic subjects, with IGFBP-rP1 explaining 2 and 11% of IGFBP-1 variance, respectively. In additional multivariate analyses, S i , sTNFR2, and age stood as independent predictive variables of IGFBP-rP1 (together explaining 18% of its variance) in nondiabetic subjects, and BMI became the only independent predictive variable of IGFBP-rP1 (explaining 26% of its variance) in type 2 diabetic men. These findings show for the first time that circulating IGFBP-rP1 is increased with insulin resistance, and they also suggest novel interactions between IGFBP-rP1 and the IGF system in humans.

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Expression of Prostacyclin-Stimulating Factor, a Novel Protein, in Tissues of Wistar Rats and in Cultured Cells

Cited by 19 publications

References 0 publications

Retinal expression, regulation, and functional bioactivity of prostacyclin-stimulating factor

Retinal expression, regulation, and functional bioactivity of prostacyclin-stimulating factor

Early Predictors of Acute Kidney Injury: A Narrative Review

Insulin Resistance Is Associated With Increased Serum Concentration of IGF-Binding Protein–Related Protein 1 (IGFBP-rP1/MAC25)

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