Browsing by Subject "Agrin"
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- PublicationOpen AccessDistinctive peri-luminal presence of agrin in murine and human carotid atherosclerotic plaques(Universidad de Murcia. Departamento de Biología Celular e Histología, 2018) Rauch, Uwe; Bengtsson, Eva; Gonçalves, Isabel; Hultgårdh Nilsson, AnnaThe clinical consequences of arterial atherosclerotic lesions depend, apart from their size, on their composition of cellular and extracellular components. While an intact endothelium at the interface of atherosclerotic plaques towards the blood can prevent its erosion, underlying smooth muscle cells within the plaque can reduce the risk of plaque ruptures, due to the deposition of stabilizing extracellular matrix. Basement membranes underlay and support the function of endothelial cells, and embed smooth muscle cells in the media, the source of most smooth muscle cells within atherosclerotic plaques. In the present study mouse atherosclerotic plaques were comparatively analyzed for the basement membrane components laminin, type IV collagen, perlecan, and agrin. Distinct agrin immunofluorescence was found in the peri-luminal area in mouse carotid atherosclerotic plaques. Agrin was also clearly present in the media, with a significant increase in regions directly associated with plaque tissue. In addition, ten human endarterectomy specimens were investigated for this heparan sulfate proteoglycan. No statistically significant differences in agrin immunofluorescence were noticed between five specimens from symptomatic and five from asymptomatic patients. In all these plaques agrin was present in a distinctive manner in a narrow zone partially or almost completely surrounding the lumen. Additionally it was also present around the small lumina of the CD31-positive neovessels. The presence of agrin at locations with particular importance for the growth and stability of atherosclerotic plaques renders this molecule strategically positioned to influence plaque development and vulnerability.
- PublicationOpen AccessDistribution of components of basal lamina and dystrophin-dystroglycan complex in the rat pineal gland, differences from the rat pineal gland: differences from the brain tissue and between the subdivisions of the gland(Murcia : F. Hernández, 2010) Bagyura, Zsolt; Pócsai, Károly; Kálmán, MihályThe pineal gland is an evagination of the brain tissue, a circumventricular neuroendocrine organ. Our immunohistochemical study investigates basal lamina components (laminin, agrin, perlecan, fibronectin), their receptor, the dystrophin-dystroglycan complex (ß-dystroglycan, dystrophin utrophin), aquaporins (-4,-9) and cellular markers (S100, neurofilament, GFAP, glutamine synthetase) in the adult rat corpus pineale. The aim was to compare the immunohistochemical features of the cerebral and pineal vessels and their environment, and to compare their features in the distal and proximal subdivisions of the so-called ’superficial pineal gland’. In contrast to the cerebral vessels, pineal vessels proved to be immunonegative to α1-dystrobrevin, but immunoreactive to laminin. An inner, dense, and an outer, loose layer of laminin as two basal laminae were present. The gap between them contained agrin and perlecan. Basal lamina components enmeshed the pinealocytes, too. Components of dystrophin-dystroglycan complex were also distributed along the vessels. Dystrophin, utrophin and agrin gave a ’patchy’ distribution rather than a continuous one. The vessels were interconnected by wing-like structures, composed of basal laminacomponents: a delicate network forming nests for cells. Cells immunostained with glutamine synthetase, S100- protein or neurofilament protein contacted the vessels, as well as GFAP- or aquaporin-immunostained astrocytes. Within the body a smaller, proximal, GFAP-and aquaporin-containing subdivision, and a larger, distal, GFAP-and aquaporin-free subdivision could be distinguished. The vascular localization of agrin and utrophin, as well as dystrophin, delineated vessels unequally, preferring the proximal or distal end of the body, respectively.