Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α

Moss, Marcia L.; Jin, S.-L. Catherine; Milla, Marcos E.; Burkhart, William; Carter, H. Luke; Chen, Wenji; Clay, William C.; Didsbury, John; Hassler, Daniel F.; Hoffman, Christine R.; Kost, Thomas A.; Lambert, Millard H.; Leesnitzer, M. Anthony; McCauley, Philip; McGeehan, Gerard M.; Mitchell, Justin; Moyer, Mary B.; Pahel, Gregory; Rocque, Warren J.; Overton, Laurie K.; Schoenen, Frank J.; Seaton, Theresa; Su, Jing; Warner, Janet; Willard, Derril H.; Becherer, J. David

doi:10.1038/385733a0

Cited by 1,572 publications

(1,167 citation statements)

References 22 publications

Supporting

Mentioning

1,133

Contrasting

Unclassified

Order By: Relevance

“…This is exemplified by both ADAM17 and ADAM19, which are both capable of shedding TNF-alpha. ADAM17 plays a key role in this release of soluble TNF-alpha by cleavage of the membraneanchored precursor of TNF-alpha [16][17][18]. TNF-alpha is a proinflammatory cytokine and a key mediator in immune defense with a role in induction and amplification of inflammation, as a response to external, potential threatening stimuli.…”

Section: Discussionmentioning

confidence: 99%

Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung

et al. 2009

View full text Add to dashboard Cite

In view of the associations of "a disintegrin and metalloprotease" (ADAM) with respiratory diseases, we assessed the expression of various ADAMs in human lung tissue. Lung tissue was obtained from nine individuals who underwent surgery for lung cancer or underwent lung transplantation for emphysema. Also, 16HBE 14o-(human bronchial epithelial) and A549 (alveolar type II epitheliumlike) cell lines were used. Immunohistochemistry was performed with antibodies recognizing different ADAM domains. The ADAMs were typically distributed over the bronchial epithelium. ADAM8 and ADAM10 were expressed diffusely in all layers of the epithelium. ADAM9, ADAM17, and ADAM19 were predominantly expressed in the apical part of the epithelium, and ADAM33 was predominantly and strongly expressed in basal epithelial cells. In smooth muscle, ADAM19 and ADAM17 were strongly expressed, as was ADAM33, though this expression was weaker. ADAM33 was strongly expressed in vascular endothelium. All ADAMs were generally expressed in inflammatory cells. The typical distribution of ADAMs in the lung, especially in the epithelium, is interesting and suggests a localized function. As most ADAMs are involved in release of (pro-) inflammatory mediators and growth factors, they may play an important role in the first line of defense and in initiation of repair events in the airways.

show abstract

Section: Discussionmentioning

confidence: 99%

Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung

et al. 2009

View full text Add to dashboard Cite

show abstract

“…RANKL exists in 2 forms: a cell membrane-bound variant that is produced by the majority of tissues and a secreted form. The latter may be generated from cleavage of a cellular form by TACE 25 or may be a primary secreted form that has been described in activated T lymphocytes as well as in a squamous carcinoma cell line. 26 Our findings demonstrated that in SH-SY5Y both RANKL forms were detectable and active: indeed, osteoclast formation was induced not only by the juxtacrine cell-cell interaction but also by the paracrine activity of the culture medium.…”

Section: Discussionmentioning

confidence: 99%

In vitro blockade of receptor activator of nuclear factor‐κB ligand prevents osteoclastogenesis induced by neuroblastoma cells

Granchi

Amato

Battistelli

et al. 2004

Intl Journal of Cancer

View full text Add to dashboard Cite

Proliferation and differentiation of osteoclasts are regulated by a cytokine system that includes RANKL, which binds 2 receptors: RANK, which activates osteoclast differentiation, and osteoprotegerin (OPG), a decoy receptor that limits RANKL action. We investigated the role of the OPG/ RANKL/RANK network in the pathogenesis of skeletal metastasis in neuroblastoma. Four different neuroblastoma cell lines (NB100, CHP212, SH-SY5Y, SJ-NK-P) showed a large amount of OPG and RANKL transcripts. Soluble RANKL was detectable in all cell lines, but poor release of OPG was observed. SH-SY5Y showed the lowest OPG-to-RANKL ratio and promoted osteoclastic differentiation of FLG29.1 and peripheral mononuclear cells, inducing expression of the osteoclast markers RANK, c-src, c-fos, cathepsin-K and TRAP. SJ-N-KP, which released both OPG and RANKL, did not show the same capability. OPG, neutralizing anti-RANKL antibody and antisense oligonucleotides were evaluated for their ability to inhibit RANKL activity. The neutralizing antibody hampered osteoclastic differentiation by blocking both the juxtacrine and the paracrine activity of RANKL. Our findings confirm that neuroblastoma cells induce osteoclastogenesis via RANKL and suggest that the RANKL expression associated with lack of the decoy receptor OPG could be a peculiarity of some tumors that makes them able to induce metastatic osteolysis. Moreover, our results suggest that RANKL could be a relevant target in the adjuvant therapy of bone metastatic neuroblastoma as proper neutralization revokes completely osteoclastic differentiation. © 2004 Wiley-Liss, Inc. Key words: neuroblastoma; bone metastasis; osteoclast; RANKL; osteoprotegerinMetastasis is the most relevant prognostic factor for survival in neuroblastoma patients, and bone is one of the target organs of metastasis in advanced neuroblastoma. Patients with bone metastasis are classified as stage IV, regardless of other clinical manifestations, since the presence of bone/bone marrow metastasis is responsible for poor prognosis despite high-dose chemotherapy and autologous hematopoietic stem cell transplantation. 1 One possible reason for this ominous prognosis is the difficulty in reaching cancer cells that have colonized the bone/bone marrow microenvironment. This suggests the need for effective therapeutic modalities for patients with skeletal metastases based on a precise understanding of the pathophysiology of bone colonization in neuroblastoma. Two classical theories are generally advocated to explain the invasion of tumor cells in bone, i.e., the soil hypothesis 2 and the circulation theory. 3 The first suggests that proper factors favor the implantation of metastatic cells, including nutrients, oxygen tension, hormonal environment and hydrogen ion concentrations. The second assumes that development of cancer metastases is dependent on the blood volume inside a target organ. This hemodynamic theory alone cannot explain the high frequency of skeletal metastasis from some neoplasms because blood flow in bone is very p...

show abstract

“…Hence they can modulate cell responses to various signals by acting as cell surface sheddases. Of particular relevance is the activity of ADAM-17 (TACE) as a sheddase of membrane-bound pro-TNF-α [37,38] and of EGF receptor ligands leading to the release of active ligands [39]. Another illustrative example is the activation of NOTCH signalling by Notch ligand Delta shedding from the cell surface by ADAM-10 [40][41][42].…”

Section: Implication Of Adams and Adamtss In Physiology And Pathologymentioning

confidence: 99%

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

et al. 2008

View full text Add to dashboard Cite

A disintegrin and metalloproteinases (ADAMs) are a recently discovered family of proteins that share the metalloproteinase domain with matrix metalloproteinases (MMPs). Among this family, structural features distinguish the membrane-anchored ADAMs and the secreted ADAMs with thrombospondin motifs referred to as ADAMTSs. By acting on a large panel of membrane-associated and extracellular substrates, they control several cell functions such as adhesion, fusion, migration and proliferation. The current review addresses the contribution of these proteinases in the positive and negative regulation of cancer progression as mainly mediated by the regulation of growth factor activities and integrin functions.

show abstract

Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α

Cited by 1,572 publications

References 22 publications

Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung

Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung

In vitro blockade of receptor activator of nuclear factor‐κB ligand prevents osteoclastogenesis induced by neuroblastoma cells

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

Contact Info

Product

Resources

About