Detection of vitronectin mRNA in tissues and cells of the mouse.

Seiffert, Dietmar; Keeton, M; Eguchi, Yawara; Sawdey, Mike; Loskutoff, David J.

doi:10.1073/pnas.88.21.9402

Cited by 110 publications

(94 citation statements)

References 46 publications

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“…A possibility that these vitronectins are specifically synthesized in atherosclerotic aorta is not likely, since we failed to detect mRNA of vitronectin in the arterial wall in normal and WHHL rabbits either by an in situ hybridization technique or by northern blot analysis (data not shown). Recently, Seiffert et al reported that mouse vitronectin mRNA could not be detected in mouse aorta by northern blot analysis (21). However, there remains a possibility that these polypeptides may be derived from platelets deposited in the arterial wall (22).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Vitronectins in Atherosclerotic Lesions

Mori

Iwasaki

Sato

et al. 1996

J Atheroscler Thromb

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Vitronectin is one of the major extracellular matrix proteins that accumulates in atherosclerotic lesions. A monoclonal antibody (EMR1a/212D) specifically stained the extracellular regions in thickened intima which colocalized well with lipid deposition. The antigenic glycoprotein with a molecular weight of 66KDa was revealed to be rabbit vitronectin. When homogenates of WHHL rabbit atheroma were subjected to immunoblot analysis using EMR1a/212D, four molecules with molecular weight 66, 56, 50 and 47KDa were detected.To confirm whether these smaller immunopositive bands were derived from mature vitronectin, another monoclonal antibody (EMR1b/244H) recognizing the polypeptide region of vitronectin was prepared. All four molecules were detected by EMR1b/244H as well as by EMR1a/212D. Two smaller vitronectins (56KDa and 5OKDa) were found in atherosclerotic lesions and increased markedly during the development of atherosclerosis.On the other hand, the vitronectin detected in normal rabbit aorta was mainly of the mature type, while 56KDa and 47KDa forms were not detected. The total amount of the four vitronectins in atherosclerotic lesions was 38.5kigou+5.0 ng/mg wet weight tissue, a value approximately 9.5 fold higher than that found in normal aorta. In conclusion, we found massive accumulation of these vitronectins concomitant with atherosclerotic development in rabbit aorta.

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Section: Discussionmentioning

confidence: 99%

Characterization of Vitronectins in Atherosclerotic Lesions

Mori

Iwasaki

Sato

et al. 1996

J Atheroscler Thromb

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“…These results indicate that significant amounts of Vn mRNA are produced at extrahepatic sites. Although the hepatocyte appears to be the primary Vn-producing cell type in the liver (Seiffert et al, 1991), the Vn-producing cells in the other tissues were not identified. The regulation of both cell adhesion and of cell-mediated proteolytic enzyme cascades by Vn suggests that it may play a critical role in development.…”

Section: Introductionmentioning

confidence: 99%

“…In situ hybridization was carried out essentially as described on paraffin-embedded sections (Wilcox et al, 1989;Seiffert et al, 1991). After hybridization, slides were washed in 0.1 x SSC/lO mM 2-mercaptoethanol/l mM EDTA for 2 hr at 60°C.…”

Section: In Situ Hybridizationmentioning

confidence: 99%

Distribution of vitronectin mRNA during murine development

Seiffert

Iruela‐Arispe

Sage

et al. 1995

Developmental Dynamics

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Vitronectin (Vn) is not only a major adhesive glycoprotein in plasma but also regulates cell-mediated proteolytic enzyme cascades, including the complement, coagulation, and fibrinolytic systems. This broad functional activity suggests that Vn may also play a critical role in development. To begin to investigate this possibility, we studied Vn gene expression during murine embryogenesis. In situ hybridization analysis of embryonic tissues revealed Vn mRNA primarily in the liver and the central nervous system (CNS). In the liver, Vn mRNA was detected by day 10, the level increasing at later developmental stages. In the CNS, Vn mRNA was also detected as early as day 10 and was confined to the floor plate. However, as development proceeded, high levels of Vn transcripts became prominent in the meninges of the cortex and spinal cord, and in close proximity to brain capillaries. The perikarya of most neurons lacked Vn mRNA. Unexpectedly, high levels of Vn mRNA were associated with capillaries of the CNS, but not with blood vessels of peripheral organs. These results indicate that Vn is expressed in a spatially and temporally distinct pattern during murine embryogenesis, and suggest that the Vn transcript may be a CNS-specific vascular marker. o 1995 WiIey-Liss, Inc.

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“…Vitronectin deposition into the matrix is tightly regulated, occurring at specific times during development and disease progression. In the adult animal, vitronectin synthesis occurs primarily in the liver (71,72,78), however, induction of vitronectin synthesis by tissue cells and its increased deposition into surrounding 86 C. E. WILKINS-PORT ET AL. tissues has been observed in association with tumor progression (6,7,26,27,80), atherosclerosis (17,83), rheumatoid arthritis (79), macular degeneration (29,57), and differentiation of neuroectodermal and mesenchymal structures (16,40,48,71). Vitronectin has a relatively short half life in the matrix as it is actively removed by integrin receptor mediated endocytosis and subsequently degraded by lysosomal enzymes (49,59).…”

Section: Introductionmentioning

confidence: 99%

Vitronectin's Basic Domain is a Syndecan Ligand which Functionsin transto Regulate Vitronectin Turnover

Wilkins-Port

Sanderson²,

Tominna-Sebald³

et al. 2003

Cell Communication & Adhesion

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During the process of tissue remodeling, vitronectin (Vn) is deposited in the extracellular matrix where it plays a key role in the regulation of pericellular proteolysis and cell motility. In previous studies we have shown that extracellular levels of vitronectin are controlled by receptormediated endocytosis and that this process is dependent upon vitronectin binding to sulfated proteoglycans. We have now identified vitronectin's 12 amino acid "basic domain" which is contained within the larger 40 amino acid heparin binding domain, as a syndecan binding site. Recombinant vitronectins representing wild type vitronectin (rVn) and vitronectin with the basic domain deleted (rVn 347-358) were prepared in a baculoviral expression system. The rVn as well as a glutathione S-transferase (GST) fusion protein, consisting of vitronectin's 40 amino acid heparin binding domain (GST-VnHBD), exhibited dose dependent binding to HT-1080 cell surfaces, which was attenuated following deletion of the basic domain. In addition, GST-VnHBD supported both HT-1080 and dermal fibroblast cell adhesion, which was also dependent upon the basic domain. Similarly, ARH-77 cells transfected with syndecans -1, -2, or -4, but not Glypican-1, adhered to GST-VnHBD coated wells, while adhesion of these same cells was lost following deletion of the basic domain. HT-1080 cells were unable to degrade rVn 347-358. Degradation of rVn 347-358 was completely recovered in the presence of GST-VnHBD but not in the presence of GST-VnHBD 347-358. These results indicate that turnover of soluble vitronectin requires ligation of vitronectin's basic domain and that this binding event can work in trans to regulate vitronectin degradation.

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Detection of vitronectin mRNA in tissues and cells of the mouse.

Cited by 110 publications

References 46 publications

Characterization of Vitronectins in Atherosclerotic Lesions

Characterization of Vitronectins in Atherosclerotic Lesions

Distribution of vitronectin mRNA during murine development

Vitronectin's Basic Domain is a Syndecan Ligand which Functionsin transto Regulate Vitronectin Turnover

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