Polymerase chain reaction and focal contact formation indicate integrin expression in mesangial cells

Petermann, Arndt T.; Fees, Hans; Grenz, Harald; Goodman, Simon L.; Sterzel, R. Bernd

doi:10.1038/ki.1993.341

Cited by 23 publications

(13 citation statements)

References 47 publications

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“…Mesangial cells have been found to express the integrin a subunits, al-3, a5 and d. All these a subunits combine with pl (Petermann et al, 1993). In addition, we found that the integrins expressed by mesangial cells include avp5 and m p 6 in vivo, and avp3 and avp5 in vitro.…”

Section: Integrins and Integrin Subunitsmentioning

confidence: 49%

Glomerular Extracellular Matrix Components and Integrins

Kramer

et al. 1998

Cell Adhesion and Communication

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It has become apparent that extracellular matrix components and their cellular receptors, the integrins, are important regulators of glomerular development and function. In this rapidly evolving field we studied the production of extracellular matrix components and integrins by rat glomerular visceral epithelial and mesangial cells, using molecular probes and antibodies that have recently become available. Special attention was paid to laminin isoforms and to splice variants of the integrin subunits a 3 and a6. Results were compared to the in vivo expression in human fetal, newborn and adult kidneys. The mesangial cells were found to produce laminin-1, nidogen and two as yet unidentified laminin isoforms with putative (Y chains of about 395 (m) and of 375 kDa (cry), tentatively described before as bovine kidney laminin. Furthermore, they expressed the integrins d p l , cu2p1, a3Ap1, a5p1, cwp3, mp5, and small amounts of d A p l and a6Bpl. The glomerular visceral epithelial cells produced the two new laminin isoforms mentioned above, laminin-5, but no laminin-1 or nidogen. The integrins (~2p1, (~3Ap1, &Am, a 6 B P and the integrin subunit av were found to be expressed. We show that during nephrogenesis, the laminin a 1 chain disappears and is replaced by another (Y chain, possibly one of the two as yet unidentified (Y chains mentioned above. The laminin pl chain is replaced by the p2 chain somewhat later in glomerular development. In general, the integrins found to be expressed in glomeruli of adult kidney were consistent with those found in cultured glomerular visceral epithelial and mesangial cells. No splice variant switch of the integrin a 3 or a6 subunits could be demonstrated during nephrogenesis.Our results suggest an important role for the mesangial cell in providing nidogen as a crucial component of the supramolecular stucture of the glomerular basement membrane. Furthermore our results indicate that laminin axp2yl and ayp2yl isoforms are important in the glomerulus of adult kidney and that the integrin a3Apl is the main integrin receptor for laminin isoforms on glomerular visceral epithelial and mesangial cells, both in vitro and in vivo.

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Section: Integrins and Integrin Subunitsmentioning

confidence: 49%

Glomerular Extracellular Matrix Components and Integrins

Kramer

et al. 1998

Cell Adhesion and Communication

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“…It has been suggested that structures resembling focal contacts exist between mesangial cells and GBM both in vivo and in cultured mesangial cells [24,32]. This is thought to mean that any alterations in these contacts will alter the regulatory action of mesangial cells on glomerular haemodynamics [9].…”

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confidence: 98%

Distribution of renal integrin receptors and their ligands in congenital nephrotic syndrome of the finnish type

Ljungberg

Virtanen

Holmberg

et al. 1996

Vichows Archiv A Pathol Anat

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The aim of this study was to examine the distribution of beta 1 and alpha v integrins (Ints) and some of their ligands in the kidneys of patients with congenital nephrotic syndrome of the Finnish type (CNF) and in controls using indirect immunofluorescence with monoclonal antibodies. The mesangial reactivity of Int alpha 1 and Int beta 1 subunits was more variable and an increased glomerular reactivity with Int alpha 3 and Int-alpha 6 antibodies was found in CNF kidneys than in controls. Int alpha 2 subunit was either completely missing from or found in significantly lesser amounts in CNF kidney glomeruli. The immunoreactivity for Int alpha v was more variable, fainter and also more granular in CNF samples than in control kidneys. The glomerular reactivity for Int beta 5 was more diffuse and weaker, and in sclerotic Bowman's capsules more intense in CNF kidneys than in controls. Immunoreactivity for Int beta 6 was restricted and was comparable in extent in CNF and control kidneys. Of the extracellular matrix components studied, the expression of EDAFn, EDBFn, OncFn, Ln alpha 2 chain, Ln beta 1 chain and tenascin was increased. This is also seen in several glomerular diseases with inflammation and sclerosis. Immunoreactivity for vitronectin was decreased. Several differences were found in the intensity or location of the immunostaining for the beta 1 and alpha v Ints and their ligands in CNF kidneys compared with controls, which have not been found in any other proteinuric disease. Disturbed Int expression pattern in CNF may specifically reflect the disturbance of glomerular function caused by the primary defect in this disease.

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“…In addition, the β 1 integrins α 3 and α 5 as well as α v β 3 are observed on parietal and visceral epithelial cells. Cultured human and rat MCs express α 1 , α 2 , α 3 A, α 5 , α 8 , α v , β 1 , β 3 , β 5 and weakly α 6 at mRNA and protein levels [2, 8, 9, 10, 11, 12, 13, 14](table 1). In general, the integrin expression pattern of cultured MCs is comparable to that observed in renal tissue sections.…”

Section: Mesangial Ecm and Receptors In Normal Glomeruli And Culturedmentioning

confidence: 99%

“…As anchorage-dependent cells, MCs in culture form focal contacts. Immunocytochemical analysis of rat and human MCs in culture revealed that β 1 , α 1 , α 3 , α 5 , α 8 and α v can be organized in focal adhesions [13, 14](fig. 2).…”

Section: Regulation Of MC Adhesionmentioning

confidence: 99%

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Mesangial Cells and Their Adhesive Properties

Pröls

Hartner²,

Ho³

et al. 1999

Nephron Exp Nephrol

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Glomerular mesangial cells play a central role in maintaining structure and function of the glomerular capillary ultrafiltration apparatus. Under physiological and pathological conditions, mesangial cells regulate amount and composition of the surrounding extracellular matrix. Conversely, components of the embedding matrix affect the mesangial cell phenotype. These interactions are mediated via specific cell surface receptors, the best studied group of which is the β₁ integrin family. The β₁ integrins play a role in mesangial cell adhesion, migration, survival and proliferation. Expression and abundance of integrins in healthy and diseased glomeruli and their functions and mediation of signals are discussed in this review. Other factors modulating mesangial cell-matrix interactions, such as antiadhesive proteins, cytokines, disintegrins and nitric oxide, are also considered. The available evidence from in vitro and in vivo studies indicates that receptor-mediated interactions between mesangial cells and the normal or abnormal extracellular matrix regulate the mesangial cell phenotype and thus contribute to normal maintenance of the glomerulus and to remodeling and repair of the glomerular capillary tuft in response to injury.

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Polymerase chain reaction and focal contact formation indicate integrin expression in mesangial cells

Cited by 23 publications

References 47 publications

Glomerular Extracellular Matrix Components and Integrins

Glomerular Extracellular Matrix Components and Integrins

Distribution of renal integrin receptors and their ligands in congenital nephrotic syndrome of the finnish type

Mesangial Cells and Their Adhesive Properties

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