T lymphocytes conditioned with Interferon β induce membrane and soluble VCAM on human brain endothelial cells

Calabresi, Peter A.; Prat, Alexandre; Biernacki, Katherine; Rollins, Jessica; Antel, Jack P.

doi:10.1016/s0165-5728(01)00253-3

Cited by 36 publications

(20 citation statements)

References 30 publications

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“…It is upregulated on brain microvascular endothelial cells in acute MS lesions [4] and its expression is downregulated by IFN beta [6]. In vitro studies with human cerebral endothelial cells demonstrated that biologically active, soluble forms of VCAM are released from the surface of these cells upon stimulation with tumor necrosis factor-alpha and interferon beta [3,11]. This process is probably mediated by the matrix metalloproteases, which are released from the endothelium upon activation [10].…”

Section: Discussionmentioning

confidence: 99%

“…Here we assessed potential markers of biological and therapeutic response sequentially in patients with SPMS under treatment with IFNβ-1b for up to 36 months. We were particularly interested in adhesion molecules as they are involved in early lesion formation associated with gadolinium enhancement on MRI and soluble forms have been described as possible regulators of brain inflammation [3,11].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Soluble vascular cell adhesion molecule (VCAM) is associated with treatment effects of Interferon beta-1b in patients with Secondary Progressive Multiple Sclerosis

Rieckmann¹,

Kruse²,

Nagelkerken

et al. 2005

J Neurol

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Soluble vascular cell adhesion molecule (VCAM) is associated with treatment effects of Interferon beta-1b in patients with Secondary Progressive Multiple Sclerosis

Rieckmann¹,

Kruse²,

Nagelkerken

et al. 2005

J Neurol

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“…ADAMs 9 (meltrin-␥), 10 (kuzbian), and 17 (tissue necrosis factor-␣-converting enzyme) have been shown to function in ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor, amyloid precursor protein, and tissue necrosis factor-␣, respectively (6 -10). These ADAMs and other members of this protein family have also been implicated in the shedding of other proteins such as L-selectin, FasL, and VCAM-1 (11)(12)(13). In addition to the proteolytic functions mentioned, several ADAMs have been shown to interact with the integrin family of cell surface receptors.…”

mentioning

confidence: 99%

The Lymphocyte Metalloprotease MDC-L (ADAM 28) Is a Ligand for the Integrin α4β1

Bridges

Tani

Hanson

et al. 2002

Journal of Biological Chemistry

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A disintegrin and metalloprotease (ADAM) 1 is a family of recently identified cell surface and secreted glycoproteins that possess both proteolytic and adhesive properties (1, 2). Prototypical members of this family are composed of a prodomain, metalloprotease, disintegrin-like, cysteine-rich, EGF-like, transmembrane, and cytoplasmic domains. The metalloprotease domain is homologous to the reprolysins, members of the metazincin superfamily that include the matrix metalloproteases, the astacins, and serralysins (3). Although the ADAMs may serve other proteolytic functions, their role in the ectodomain shedding of specific cell surface proteins has been well documented (4, 5). ADAMs 9 (meltrin-␥), 10 (kuzbian), and 17 (tissue necrosis factor-␣-converting enzyme) have been shown to function in ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor, amyloid precursor protein, and tissue necrosis factor-␣, respectively (6 -10). These ADAMs and other members of this protein family have also been implicated in the shedding of other proteins such as L-selectin, FasL, and VCAM-1 (11-13). In addition to the proteolytic functions mentioned, several ADAMs have been shown to interact with the integrin family of cell surface receptors. Integrins are a widely distributed superfamily of noncovalent heterodimeric glycoproteins that play a vital role in cellular adhesion, migration, and signal transduction (14, 15). The ADAM disintegrin-like domains are homologous to small non-enzymatic peptides isolated from the venom of snakes that function as antagonists of integrins (16,17). The direct interaction of the snake venom disintegrin peptides with integrins led to the hypothesis that the disintegrin-like domains of ADAMs may function as integrin ligands. The disintegrin-like domains of ADAMs 1-3 expressed on the surface of sperm interact with the integrin ␣ 6 ␤ 1 in association with CD9 and CD98 on the egg surface (18 -23). Recognition of ADAMs 2 and 3 by ␣ 6 ␤ 1 requires the residues DECD located within a region of the disintegrin domain, designated the disintegrin loop, that corresponds to an extended loop in the snake venom peptides that typically contains an RGD sequence required for integrin binding (21-23). Human ADAM 15 contains an RGD sequence within the disintegrin loop region and is recognized by the integrins ␣ v ␤ 3 and ␣ 5 ␤ 1 (24 -26). However, mouse ADAM 15 lacks the RGD sequence found in the human homologue. Both human and mouse ADAM 15 as well as ADAM 12 were shown to be recognized by the integrin ␣ 9 ␤ 1 via residues outside the disintegrin loop (27). Other ADAM disintegrin-like domains reported to bind integrins are ADAM 9, which is recognized by ␣ 6 ␤ 1 and ␣ v ␤ 5 (28, 29), and ADAM 23, which is recognized by ␣ v ␤ 3 (30). * This work was supported by National Institutes of Health Grant AI47314. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section...

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“…We have shown that the MCEC-1 endothelial cell line exhibits ectodomain release of VCAM-1 and that 24 h stimulation with TNFa and IL-1h up-regulates both sVCAM-1 generation and expression of VCAM-1. Up-regulation of cell surface VCAM-1 expression in response to TNFa and IL-1 is seen in endothelial cells derived from a variety of vascular beds [3,[25][26][27]. The responses to TNFa may vary between different endothelial cell types, with microvascular endothelial cells reported to have a relatively transient increase in VCAM-1 expression compared to human umbilical vein endothelial cells, whilst iliac arterial endothelial cells exhibit no increased VCAM-1 expression [25,27].…”

Section: Discussionmentioning

confidence: 99%

“…VCAM-1 up-regulation has been shown to be important in inflammatory diseases including atherosclerosis, where induction precedes leukocyte adhesion and transmigration across the vascular endothelium [1][2][3].…”

Section: Introductionmentioning

confidence: 99%

Cytokine stimulated vascular cell adhesion molecule-1 (VCAM-1) ectodomain release is regulated by TIMP-3

Singh

Mason

Lidington

et al. 2005

Cardiovascular Research

102

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T lymphocytes conditioned with Interferon β induce membrane and soluble VCAM on human brain endothelial cells

Cited by 36 publications

References 30 publications

Soluble vascular cell adhesion molecule (VCAM) is associated with treatment effects of Interferon beta-1b in patients with Secondary Progressive Multiple Sclerosis

Soluble vascular cell adhesion molecule (VCAM) is associated with treatment effects of Interferon beta-1b in patients with Secondary Progressive Multiple Sclerosis

The Lymphocyte Metalloprotease MDC-L (ADAM 28) Is a Ligand for the Integrin α4β1

Cytokine stimulated vascular cell adhesion molecule-1 (VCAM-1) ectodomain release is regulated by TIMP-3

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