Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures

Glomski, Krzysztof; Monette, Sébastien; Manova, Katia; Strooper, Bart De; Säftig, Paul; Blobel, Carl P.

doi:10.1182/blood-2011-04-348557

Cited by 71 publications

(104 citation statements)

References 51 publications

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“…Notch receptor activation after ligand binding requires a series of proteolytic cleavage processes, one of which is mediated by the ADAM family metalloprotease ADAM10. Accordingly, the loss of ADAM10 in ECs also leads to impaired bone growth and growth plate defects (Glomski et al, 2011), consistent with the phenotypes seen in other EC-specific Notch loss-of-function mutants .…”

Section: Notch Signaling During Bone Angiogenesissupporting

confidence: 52%

Blood vessel formation and function in bone

2016

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In addition to their conventional role as a conduit system for gases, nutrients, waste products or cells, blood vessels in the skeletal system play active roles in controlling multiple aspects of bone formation and provide niches for hematopoietic stem cells that reside within the bone marrow. In addition, recent studies have highlighted roles for blood vessels during bone healing. Here, we provide an overview of the architecture of the bone vasculature and discuss how blood vessels form within bone, how their formation is modulated, and how they function during development and fracture repair.

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Section: Notch Signaling During Bone Angiogenesissupporting

confidence: 52%

Blood vessel formation and function in bone

2016

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“…1B), has also emerged as a major player in the field of ectodomain shedding. 3,[49][50][51] Although these two ADAM proteins appear to have common target molecules, it is becoming clear that each has specific substrates and functions. Emerging data suggest that ADAM10 plays central roles in the activation of Notch signaling and the processing of amyloid precursor protein and cadherins.…”

Section: Discussionmentioning

confidence: 99%

A Brief History of Tumor Necrosis Factor α – converting Enzyme: An Overview of Ectodomain Shedding

Horiuchi

2013

Keio J. Med.

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Many membrane-bound molecules are cleaved at the cell surface, thereby releasing their extracellular domains. This process, often referred to as ectodomain shedding, has emerged as a critical post-translational mechanism for various membrane-bound ligands, receptors, and adhesion molecules. Tumor necrosis factor α (TNFα)-converting enzyme (TACE/ADAM17) was originally identified as an enzyme responsible for releasing the membrane-bound TNFα precursor. However, subsequent studies found an exceptionally large number of target molecules of TACE, including the ligands for epidermal growth factor receptor, L-selectin, CD44, and vascular growth factor receptor 2. Furthermore, in vivo studies using TACE-conditional knockout mice demonstrated the crucial roles of TACE and ectodomain shedding under both physiological and pathological conditions. However, the potential clinical application of the manipulation of TACE activity remains to be investigated.

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“…A disintegrin and metalloprotease 10 (ADAM10) 2 is a type 1 transmembrane protein that is ubiquitously expressed and functions as an ectodomain sheddase for over 40 transmembrane target proteins (4). ADAM10-deficient mice die at embryonic day 9.5, consistent with the essential role of ADAM10 in the cleavage and activation of Notch, which is central to most cell fate decision-making processes during metazoan development (5).…”

Section: A Disintegrin and Metalloprotease 10 (Adam10) Is A Ubiquitoumentioning

confidence: 99%

“…The proteolytic cleavage, or "shedding," of the extracellular regions (ectodomains) of transmembrane proteins is emerging as an important mechanism for the regulation of cell development and function (1)(2)(3). A disintegrin and metalloprotease 10 (ADAM10) 2 is a type 1 transmembrane protein that is ubiquitously expressed and functions as an ectodomain sheddase for over 40 transmembrane target proteins (4).…”

Section: A Disintegrin and Metalloprotease 10 (Adam10) Is A Ubiquitoumentioning

confidence: 99%

The TspanC8 Subgroup of Tetraspanins Interacts with A Disintegrin and Metalloprotease 10 (ADAM10) and Regulates Its Maturation and Cell Surface Expression

Haining

Yang

Bailey

et al. 2012

Journal of Biological Chemistry

142

201

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Background: ADAM10 is a transmembrane metalloprotease that regulates development, inflammation, cancer, and Alzheimer disease. Results: The TspanC8 subgroup of tetraspanin membrane proteins interacts with and promotes ADAM10 maturation and cell surface localization. Conclusion: This study defines the TspanC8 tetraspanins as essential regulators of ADAM10. Significance: Focusing on specific TspanC8-ADAM10 complexes may allow ADAM10 therapeutic targeting in a cell typeand/or substrate-specific manner.

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Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures

Cited by 71 publications

References 51 publications

Blood vessel formation and function in bone

Blood vessel formation and function in bone

A Brief History of Tumor Necrosis Factor α – converting Enzyme: An Overview of Ectodomain Shedding

The TspanC8 Subgroup of Tetraspanins Interacts with A Disintegrin and Metalloprotease 10 (ADAM10) and Regulates Its Maturation and Cell Surface Expression

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