Abstract
A disintegrin and metalloprotease like decysin (ADAMDEC1) is a highly conserved secreted metalloprotease that belongs to a family of A disintegrin and metalloprotease (ADAMs). It is expressed exclusively in the gastrointestinal tract of animals and is known to possess a very rare zinc-binding motif (HEXXHXXGXXD) within the metalloprotease domain. The biological function of ADAMDEC1 as well as its true biological substrates remains unknown although its characteristic features reported to date suggest it plays a fundamental role in the physiology of mammals. Historically its expression, in healthy state, was believed to be limited to the monocyte-derived macrophages (MDMs) and dendritic cells within the gastrointestinal tract; however, the recent development of single-cell sequencing has provided evidence supporting its expression in a wider range of cell types. There is an increasing body of evidence linking the alterations in ADAMDEC1 expression and various inflammatory diseases and cancers. Although a detailed mechanistic role of ADAMDEC1 in these conditions remains elusive. In this review, we aim to summarise the characteristic features of this unique metalloprotease, discuss the associations with various human diseases and define the potential mechanistic role of ADAMDEC1 in mammalian physiology.
Highlights
A disintegrin and metalloprotease like decysin 1 (ADAMDEC1) is a unique meta zincin metalloprotease belonging to the A disintegrin and metalloproteases (ADAMs) family
ADAMDEC1 was first discovered through sequencing of mRNA extracted from the dendritic cells of human tonsils in 1997.1 Following its discovery, it was categorised to a family of ADAMs due to its high sequence homology with ADAM28
Within the intestinal tissue of Crohn’s disease, a chronic inflammatory bowel disease, the normally high expression of ADAMDEC1 is reduced which seems to have a mechanistic role in the disease pathogenesis
Summary
A disintegrin and metalloprotease like decysin 1 (ADAMDEC1) is a unique meta zincin metalloprotease belonging to the A disintegrin and metalloproteases (ADAMs) family. Dovepress highly conserved secreted or transmembrane metallopro teases that share a common structural composition, consist ing of an N-terminal signalling peptide, prodomain, metalloprotease, disintegrin-like domain, cysteine-rich region, as well as a transmembrane domain and cytoplasmic tail (Figure 1). ADAMDEC1 is missing the cytoplasmic tail, transmembrane, cysteine-rich domains consisting of only a signalling peptide, prodomain, metalloprotease and disintegrin-like domains.[1] its disintegrin-like domain is truncated resulting in a protein structure com prised 470 amino acids, which is almost half the size of the typical ADAMs (Figure 1).[1] It is believed to be cleaved at the furin-recognition site releasing the signalling peptide intracellularly and secreted as a mature active form as indi cated by the absence of a transmembrane domain. Shown to process and cleave off the signalling peptide of ADAMDEC1 in vitro.[2]
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