1,720,973 research outputs found
Intratunical Injection of Genetically Modified Adipose Tissue-Derived Stem Cells with Human Interferon alpha-2b for Treatment of Erectile Dysfunction in a Rat Model of Tunica Albugineal Fibrosis
Conclusion. This study documents that transplantation of genetically modified ADSCs, with or without human IFN alpha-2b, attenuated Peyronie's-like changes and enhanced erectile function in a rat model of TAF. Gokce A, Abd Elmageed ZY, Lasker GF, Bouljihad M, Braun SE, Kim H, Kadowitz PJ, Abdel-Mageed AB, Sikka SC, and Hellstrom WJ. Intratunical injection of genetically modified adipose tissue-derived stem cells with human interferon -2b for treatment of erectile dysfunction in a rat model of tunica albugineal fibrosis
Autoradiographic evidence that zona glomerulosa and capsular vessels of the human adrenal cortex are provided with different subtypes of adrenomedullin receptors
Frozen sections of normal adrenal glands, obtained from patients undergoing unilateral nephrectomy for kidney cancer, were labeled in vitro with human [125I]ADM(1-52). Autoradiography and quantitative densitometry showed the presence of abundant ADM(1-52) binding sites in both zona glomerulosa (ZG) and capsular vessels, which were displaced with about the same efficiency by cold ADM(1-52) and rat ADM(1-50). The selective calcitonin gene-related peptide type 1 (CGRPI) ligand CGRP(8-37) eliminated, although less efficiently than ADMs, [125I]ADM(1-52) binding in the ZG, but not in the capsular vessels. These findings suggest the existence of different receptor subtypes for ADM in the human adrenal cortex. The CGRP(8-37)-sensitive receptors located in the ZG may mediate the well-known inhibitory effect of ADM on aldosterone secretion, while the CGRP(8-37)-insensitive receptors present in the capsular vessel may be involved in the ADM-induced rise in adrenal blood flow
Inhibitory effect of adrenomedullin (ADM) on the aldosterone response of human adrenocortical cells to angiotensin-II: role of ADM(22-52)-sensitive receptors.
impact factor 2001=1.75
Proadrenomedullin N-terminal 20 peptide (PAMP), acting through PAMP(12–20)-sensitive receptors, inhibits Ca2+-dependent, agonist-stimulated secretion of human adrenal glands.
Adrenomedullin (ADM) and PAMP inhibit the aldosterone response of normal human adrenocortical (NHAC) and Conn's adenoma (CA) cells to angiotensin-II.
Adrenomedullin and calcitonin gene-related peptide (CGRP) interact with a common recveptor of the CGRP1 subtype in the human adrenal zona glomerulosa.
Frozen sections of normal adrenal glands, obtained from patients undergoing unilateral nephrectomy for kidney cancer, were labeled in vitro with human [125I]ADM(1-52). Autoradiography showed the presence of abundant ADM binding sites in the zona glomerulosa (ZG) and the outermost portion of the zona fasciculata, which were completely displaced by the addition of an excess of cold ADM(1-52). Calcitonin gene-related peptide (CGRP) and the non-selective ligand of the CGRP-receptor subtypes 1 and 2 CGRP(8-37) eliminated [125I]ADM(1-52) binding in the ZG, while the selective ligand of CGRP receptor subtype 2 [Cys(acm)2,7]-CGRP and CGRP(1-8) were ineffective. These findings confirm the presence of ADM binding sites in the human ZG, and provide the first morphological evidence that ADM and CGRP interact with a common receptor of the CGRP1 subtype
Inhibitory effect of adrenomedullin (ADM) on the aldosterone response or normal human adrenocortical (NHAC) and Conn's adenoma (CA) cells to angiotensin-IL
Human adrenomedullin (ADM) is a 52-amino acid hypotensive peptide, which possesses a disulfide bridge-formed six-membered ring in 16-21 position. The ring structure, and both the N- and C-terminal amino-acid sequences seem to play a key role in the vascular effects of ADM(1-52), and we have investigated whether the same is true for the inhibitory effect of this peptide on the aldosterone response of zona glomerulosa (ZG) cells to angiotensin-II (ANG-II). Autoradiography showed the presence of abundant [125I]ADM(1-52) binding sites in the ZG of human adrenals, which were displaced not only by cold ADM(1-52), but also by both ADM(13-52) and ADM(22-52); ADM fragments 1-12, 15-22 and 16-31 were ineffective. ADM(1-52) and ADM(13-52), but not other fragments, concentration-dependently inhibited ANG-II-stimulated aldosterone secretion of dispersed human adrenocortical cells. The aldosterone antisecretagogue actions of ADM(1-52) and ADM(13-52) were counteracted by ADM(22-52) in a concentration-dependent manner, while other ADM fragments were ineffective. In light of these findings the following conclusions could be drawn: (i) human ZG cells are provided with ADM(22-52)-sensitive receptors; (ii) the six-membered ring structure and the C-terminal, but not N-terminal, amino-acid sequence are both essential for ADM(1-52) to exert its antimineralocorticoid action; and probably (iii) the C-terminal sequence is needed for ADM(1-52) to bind its ZG receptors, while the ring structure is required for the receptor activation
Going Beyond Counting First Authors in Author Co-citation Analysis
The present study examines one of the fundamental aspects of author co-citation analysis (ACA) - the way co-citation
counts are defined. Co-citation counting provides the data on which all subsequent statistical analyses and mappings
are based, and we compare ACA results based on two different types of co-citation counting - the traditional type that
only counts the first one among a cited work's authors on the one hand and a non-traditional type that takes into
account the first 5 authors of a cited work on the other hand. Results indicate that the picture produced through this non-traditional author co-citation counting contains more coherent author groups and is therefore considerably clearer. However, this picture represents fewer specialties in the research field being studied than that produced through the traditional first-author co-citation counting when the same number of top-ranked authors is selected and analyzed. Reasons for these effects are discussed
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