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Plasmalemma vesicle protein-1 (PV-1) is an integral membrane protein associated with endothelial cell caveolae and fenestrae. Since endocrine glands are enriched with fenestrated endothelium, we examined the distribution of PV-1 mRNA and protein in endocrine glands and determined its cellular localization. A single transcript was detected by RT-PCR in all endocrine glands examined. A synthetic peptide was used to generate antibodies for Western blotting and immunohistochemistry (IHC). Western blotting of membrane fractions from lung, pituitary, adrenal, testis and PV-1-transfected Cos-1 cells revealed a major 65 kDa protein. This protein binds to heparin with high affinity. Using IHC, PV-1 was localized to both endothelial cells of the adrenal zona reticularis and chromaffin cells of the medulla. In the pancreas, PV-1 expression was restricted to a few cells in the islets of Langerhans that partially overlap with somatostatin-positive delta-cells. In both neonatal and adult pituitaries, strong PV-1 immunoreactivity was detected in neural lobe pituicytes in a pattern similar to that of glial fibrillary acidic protein (GFAP). PV-1 and GFAP expression was seen in the adult, but not neonatal, intermediate lobe. Endothelial cells throughout the neonatal anterior lobe were PV-1 positive, but PV-1 in the adult was restricted to some endothelial and endocrine cells localized near the margins of lobe. In the adult testis, strong PV-1 expression was seen in germ cells within the seminiferous tubules that varied with the stage of spermatogenesis. In contrast, PV-1 in the neonatal testis was localized to the interstitial cells but not seminiferous tubules. In the ovary, PV-1 was expressed in stromal endothelial cells as well as the thecal layer of developing follicles. Over half the corpus luteal cells were positive for PV-1. Our data have shown that PV-1 is not restricted to endothelial cells but is localized in many types of endocrine and non-endocrine cells. Furthermore, PV-1 expression in the pituitary and testis is developmentally regulated.
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Parathyroid hormone (PTH)-related protein (PTHrP) is produced in smooth muscles and endothelial cells and is believed to participate in the local regulation of vascular tone. No direct evidence for the activation of endothelium-derived nitric oxide (NO) signaling pathway by PTHrP has been found despite attempts to identify it. Based on direct in situ measurements, it is reported here for the first time that the human PTH/PTHrP receptor analogs, hPTH(1--34) and hPTHrP(1--34), stimulate NO release from a single endothelial cell. A highly sensitive porphyrinic microsensor with a response time of 0.1 ms and a detection limit of 1 nmol/l was used for the measurement of NO. Both hPTH(1--34) and hPTHrP(1--34) stimulated NO release at nanomolar concentrations. The peak concentration of 0.1 micromol/l hPTH(1--34)- and 0.1 micromol/l hPTHrP(1--34)-stimulated NO release was 175+/-9 and 248+/-13 nmol/l respectively. This represents about 30%--40% of maximum NO concentration recorded in the presence of (0.1 micromol/l) calcium ionophore. Two competitive PTH/PTHrP receptor antagonists, 10 micromol/l [Leu(11),d -Trp(12)]-hPTHrP(7--34)amide and 10 micromol/l [Nle(8,18),Tyr(34)]-bPTH(3--34)amide, were equipotent in antagonizing hPTH(1--34)-stimulated NO release; [Leu(11),d -Trp(12)]-hPTHrP(7--34)amide was more potent than [Nle(8,18),Tyr(34)]-bPTH(3--34)amide in inhibiting hPTHrP(1--34)-stimulated NO release. The PKC inhibitor, H-7 (50 micromol/l), did not change hPTH(1--34)- and hPTHrP(1--34)-stimulated NO release, whereas the combined effect of 10 micromol/l of the cAMP antagonist, Rp-cAMPS, and 50 micromol/l of the calmodulin inhibitor, W-7, was additive. The present studies show that both hPTH(1--34) and hPTHrP(1--34) activate NO production in endothelial cells. The activation of NO release is through PTH/PTHrP receptors and is mediated via the calcium/calmodulin pathway.
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Angiogenesis is an important component in the development of thyroid goitre. Vascular endothelial growth factor (VEGF) represents a family of specific endothelial cell mitogens involved in normal angiogenesis and in tumour development. The purpose of this study was to determine the distribution of VEGF in thyroid tissues during goitre formation, and to study the actions of VEGF on the regulation of thymidine incorporation and iodine uptake by thyroid follicular cells. Goitre was induced in adult rats by administration of methimazole together with a low iodine diet. Thyroid from normal or goitrous rats was removed, fixed and sectioned. Immunocytochemistry performed for VEGF using the avidin-biotin system showed that VEGF is present in normal thyroid and is located mainly in the vascular endothelium and interfollicular stromal tissue. After administration of goitrogen for 2 weeks, which caused a two- to threefold increase in thyroid weight, staining of VEGF was less apparent within the interfollicular stroma, but strongly increased throughout the thyroid follicular and endothelial cells. Uptake of [125I] and incorporation of [3H]thymidine by Fisher rat thyroid cells (FRTL-5) were measured after 72 h culture with or without TSH or VEGF, or both. In the absence of TSH, incubation with VEGF caused a significant reduction in [3H]thymidine incorporation, but did not significantly alter [125I] uptake. Incubation with TSH (1 mU/ml) caused a fourfold increase in [3H]thymidine incorporation that was diminished by co-incubation with 10 ng/ml or greater VEGF. Similarly, 10 ng/ml or greater VEGF significantly reduced the ability of TSH to increase [125I] uptake. The antagonistic effects of VEGF on TSH-stimulated [3H]thymidine incorporation or [125I] uptake were significantly reduced in the presence of an anti-VEGF antiserum. A DNA fragment representing mRNA encoding the VEGF receptor, flt-1, was identified in FRTL-5 cells by reverse transcription PCR analysis, and the abundance of this fragment was increased in FRTL-5 cells cultured in the medium containing TSH (1 mU/ml) or fibroblast growth factor (FGF)-2 (25 ng/ml). These results indicated that VEGF and one of its receptors, Flt-1, are present in epithelial cells of the thyroid, and that VEGF could contribute to the regulation of development and function of thyroid epithelial cells.
Department of Internal Medicine, Department of Cardiology, Molecular Internal Medicine, University of New Mexico Health Sciences Center, 915 Camino de Salud NE, Albuquerque, New Mexico 87131, USA
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& Davidge 2012 , Meyer et al . 2012 a , b , 2014 a ), although the mechanisms involved are only partially understood. The endothelium is a key regulator of vascular tone through the release of multiple vasoactive substances, including both relaxing
Section of Pharmacology, Section of Pharmacology, Department of Clinical and Experimental Medicine and Pharmacology, University of Messina, Torre Biologica 5th floor, c/o AOU Policlinico G. Martino, Via C. Valeria Gazzi, 98125 Messina, Italy
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integrity of endothelium was assessed by a relaxant response to ACh (100 nM). The tissue was then washed occasionally for 30 min. Endothelium response was evaluated with cumulative concentrations of ACh (10 nM–1 μM) in aortic rings precontracted with
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exposed to 75 mM KCl to check their functional integrity. After a washout period, the presence of vascular endothelium was tested by the ability of 10 μM ACh to relax segments precontracted with 1 μM noradrenaline (NA). The segments were rinsed
Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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mast cells of the human lung ( Gaston et al. 1994 ) and the skin vascular endothelium ( Abd-El-Aleem et al. 2000 ) suggesting that both of these sites are potential sources of NO in human skin. In our study the inhibition of NOS using N ω -nitro- l
Cátedra de Bioquímica Clínica II, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur, San Juan 670, B8000ICN Bahía Blanca, Argentina
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Cátedra de Bioquímica Clínica II, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur, San Juan 670, B8000ICN Bahía Blanca, Argentina
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Cátedra de Bioquímica Clínica II, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur, San Juan 670, B8000ICN Bahía Blanca, Argentina
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monocytes) and vascular cells ( Villar et al . 2008 ). Vascular endothelium plays a critical role in the maintenance of antiatherogenic and antithrombotic properties of blood vessels. Besides acting as a selective diffusion barrier, endothelium allows the
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readjusted every 15 min during a 90-min equilibration period before drug administration. After this, the vessels were exposed to 75 mM KCl to check their functional integrity. After a washout period, the presence of vascular endothelium was confirmed by the
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Introduction As the primary barrier to the movement of circulating endocrine factors from the bloodstream to the interstitial space, the endothelium plays a critical role in hormone action ( Kolka & Bergman 2012 , Yoon et al . 2014
