The ADAMs family of metalloproteases: multidomain proteins with multiple functions.

By D. Seals, S. Courtneidge. 2003

1,130 citations recorded by the source corpus.

The ADAMs family of transmembrane proteins belongs to the zinc protease superfamily. Members of the family have a modular design, characterized by the presence of metalloprotease and integrin receptor-binding activities, and a cytoplasmic domain that in many family members specifies binding sites for various signal transducing proteins. The ADAMs family has been implicated in the control of membrane fusion, cytokine and growth factor shedding, and cell migration, as well as processes such as muscle development, fertilization, and cell fate determination. Pathologies such as inflammation and cancer also involve ADAMs family members. Excellent reviews covering various facets of the ADAMs literature-base have been published over the years and we recommend their examination (Black and White 1998; Schlondorff and Blobel 1999; Primakoff and Myles 2000; Evans 2001; Kheradmand and Werb 2002). In this review, we will first discuss the properties of each of the domains of the ADAMs. We will then go on to describe the involvement of ADAMs in selected biological processes. Then, we will highlight recent interesting findings suggesting roles for ADAMs in human disease. Finally, we look to the future and discuss some of the open issues in ADAMs function and regulation.

Subfields: Immunology and Allergy, Molecular Biology, Oncology

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In Immunology and Allergy

1. S. Zhong
2. R. Khalil
3. N. Hynes
4. S. Gill
5. W. Parks
6. C. Blobel

In Molecular Biology

1. R. Khalil
2. S. Zhong
3. N. Hynes
4. D. Edwards
5. S. Eguchi
6. H. Ohtsu
7. P. Dempsey
8. M. Handsley

In Oncology

1. R. Khalil
2. S. Zhong
3. N. Hynes
4. D. Edwards
5. S. Eguchi
6. H. Ohtsu
7. P. Dempsey
8. M. Handsley

Citations in the corpus

• A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “Additionally, some ADAMs and ADAMTS have been suggested as potential factors in pathological conditions such as oncogenesis, autoimmune diseases, inflammation and cardiovascular diseases [5].”
• ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors. (2006, background): “In mammals, ADAM2, 7, 18, 20, 21, 29, and 30 are predominantly expressed in the testis and associated structures, whereas ADAM8, 9, 10, 11, 12, 15, 17, 19, 22, 23, 28, and 33 show more broad somatic distribution (87).”
• ERBB receptors and cancer: the complexity of targeted inhibitors (2005, background): “40 ), or the clustering of a protease with its substrat”
• Expression and cellular localization of metalloproteases ADAMs in high graded carotid artery lesions (2012, background): “Furthermore, some studies have already associated expression of ADAMs with progressive tumours [13,15].”
• ErbB receptors: directing key signaling networks throughout life. (2004, background): “Recently, the ADAMs have been shown to play pivotal roles in proligand cleavage following treatment with GPCR agonists (12, 61, 62).”
• The ADAM metalloproteinases (2008, background): “For the majority of the ADAMs, pro-domain removal likely involves the action of pro-protein convertases (PCs) such as furin and takes place intracellularly in the secretory pathway (Endres et al., 2003; Seals and Courtneidge, 2003).”
• A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions (2016, background): “lternative splicing of s produces proteins ith different localization and activity [6].”
• ADAMs family and relatives in cardiovascular physiology and pathology. (2016, background): “Although a number of ADAMs are restricted to the reproductive system, ADAMs 9, 10, 12, 15, 17 and 19 exhibit a broader somatic expression distribution and some have been shown to be involved in cardiovascular development [3].”
• Deficits in spatial learning and motor coordination in ADAM11-deficient mice (2006, background): “Approximately half of the ADAMs are catalytically active metalloproteases that shed a broad range of substrates, such as cytokines, growth factors, receptors, adhesion molecules [1, 2 ].”
• Metalloproteinases and their inhibitors: regulators of wound healing. (2008, background): “…domain in MMPs (Kheradmand & Werb, 2002) They are transmembrane proteases and their primary function is cleavage of extracellular domains of many membrane proteins from the cell surface, a process termed ectodomain shedding (Kheradmand & Werb, 2002; Moss & Bartsch, 2004; Seals & Courtneidge, 2003).”