An evaluation of STROBE reporting compliance in cross-sectional studies published in the Journal of Korean Biological Nursing Science (2011-2024): a methodological review.

The first member of the ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) family was first identified in 1997 []. Along with ADAM and ADAMTSL, it belongs to the zinc metalloproteinase superfamily. All three family members contain a signal peptide, a propeptide, a metalloproteinase domain, a disintegrin-like domain, and a cysteine-rich domain () [,]. Structurally, ADAM possesses a unique EGF-like domain, a transmembrane domain, and a cytoplasmic tail, and is primarily localized to the cell membrane. Approximately half of its members (e.g., ADAM8, 10, 12, 15, 17) possess catalytic activity, mediate the shedding of membrane-bound proteins, and are involved in cell adhesion, migration, and signaling regulation []. ADAMTS contains central thrombospondin type 1 repeats (TSRs). As secreted proteases, they are primarily responsible for the degradation and remodeling of the extracellular matrix, playing important roles in the maintenance of tissue homeostasis, inflammatory responses, and disease progression. ADAMTSL lacks the metalloproteinase domain but retains multiple thrombospondin type 1 repeats as well as a cysteine-rich/spacer domain, functioning in a non-enzymatic manner to participate in matrix assembly, cell adhesion, and microenvironmental stability. These three families are highly homologous in structure, and functionally distinct yet synergistic with one another, collectively constituting an important molecular network that regulates the extracellular microenvironment. Studies have reported that ADAM10 and ADAM17 are primarily responsible for the cleavage of various bioactive substrates, including cytokine receptors, adhesion molecules and growth factors [,,,]. Notably, the absence of ADAM15 leads to increased expression of integrin α7 protein while integrin β1 expression remains unchanged. This expression imbalance disrupts the interaction between cardiomyocyte integrin α7/β1 and laminin, thereby inducing cardiac hypertrophy in mice []. Functional studies of the ADAMTS family have primarily focused on their involvement in extracellular matrix remodeling, organ development, inflammatory regulation, cardiovascular diseases, cancer, and fibrotic diseases, among others [,,,,]. Specifically, deficiency of ADAMTS6 leads to pulmonary hypoplasia, skeletal deformities, and congenital heart defects in the developing embryo []; ADAMTS4 expression is elevated in human atherosclerotic plaques and in the plasma of patients with acute coronary syndrome, where it compromises vascular structural integrity by degrading matrix components such as vascular wall proteoglycans []. ADAMTS8 is frequently silenced via promoter methylation in multiple tumor types, and its overexpression inhibits tumor cell proliferation, migration, and invasion by antagonizing the EGFR-MEK-ERK and Wnt/β-catenin pathways [,,,]; knockout of ADAMTS18 results in spontaneous fibrosis of the submandibular salivary gland in adult mice []. Furthermore, the ADAMTSL family, which lacks protease activity, serves as structural components and signaling hubs in the extracellular matrix. For instance, ADAMTSL2 contributes to cardiac repair following myocardial infarction by activating the LRP6/β-catenin signaling pathway [], and promotes proliferation, migration, and lipid metabolism of colorectal cancer cells via the Notch signaling pathway []. In summary, members of the ADAM, ADAMTS, and ADAMTSL families are extensively involved in extracellular matrix remodeling, regulation of signaling pathways, and various pathophysiological processes in either protease-dependent or protease-independent manners. Although the functions of some members of the above-mentioned family have been elucidated with considerable clarity, the biological functions and mechanisms of action of many others remain to be further explored. ADAMTS16, as a member of the ADAMTS family that has not been thoroughly studied, was first identified by Cal et al. in 2002 using bioinformatics methods []. Over the past two decades, only about 70 related articles have been published, and no systematic review has yet summarized its physiological and pathological roles. Current evidence suggests that ADAMTS16 may play important roles in reproductive system development, renal morphogenesis, and cardiovascular diseases. However, its specific substrate repertoire, regulatory networks, and pathophysiological significance still need to be elucidated. Therefore, on the basis of summarizing the ADAMTS family, this review mainly focuses on the potential roles of ADAMTS16 in various tissues and related diseases, aiming to provide a reference for future research. Based on substrate specificity and enzymatic activity, the 19 members of the ADAMTS family are traditionally divided into five classes []: the proteoglycanases (ADAMTS1, 4, 5, 8, 9, 15, 20), the procollagen N-peptidases (ADAMTS2, 3, 14), the von Willebrand factor-cleaving protease (ADAMTS13), the cartilage oligomeric matrix protein-cl