The ADAMs family of metalloproteases are transmembrane proteins belonging to the zinc protease superfamily. They have a modular structure, including a metalloprotease domain, a disintegrin domain, and a cytoplasmic tail. ADAMs are involved in various biological processes, such as membrane fusion, cytokine and growth factor shedding, and cell migration. They also play roles in muscle development, fertilization, and cell fate determination. Pathologies such as inflammation and cancer involve ADAMs. ADAMs are found in vertebrates, as well as in Caenorhabditis elegans, Drosophila, and Xenopus, but not in Escherichia coli, Saccharomyces cerevisiae, or plants. There are 19 ADAM genes in humans, and ADAMs are expressed in various tissues and cell types. ADAMs have different isoforms due to alternative splicing, which can affect their subcellular localization and activity. ADAMs are synthesized in the rough endoplasmic reticulum and mature in the late Golgi compartment. The prodomain is essential for ADAM maturation and activation, and its removal allows the metalloprotease domain to become active. ADAMs are also involved in the shedding of cytokines and growth factors, such as TNFα, fractalkine, and HB-EGF. ADAMs can also process growth factor receptors, such as the HER4/erbB4 receptor and the CSF-1 receptor. ADAMs are involved in the processing of other molecules, such as insulin-like growth factor-binding proteins and prions. ADAMs also play a role in the processing of the amyloid precursor protein, which is involved in Alzheimer's disease. ADAMs are regulated by various factors, including metalloprotease inhibitors and TIMPs. The study of ADAMs has revealed their importance in various biological processes and their potential as therapeutic targets in diseases such as cancer and Alzheimer's disease.The ADAMs family of metalloproteases are transmembrane proteins belonging to the zinc protease superfamily. They have a modular structure, including a metalloprotease domain, a disintegrin domain, and a cytoplasmic tail. ADAMs are involved in various biological processes, such as membrane fusion, cytokine and growth factor shedding, and cell migration. They also play roles in muscle development, fertilization, and cell fate determination. Pathologies such as inflammation and cancer involve ADAMs. ADAMs are found in vertebrates, as well as in Caenorhabditis elegans, Drosophila, and Xenopus, but not in Escherichia coli, Saccharomyces cerevisiae, or plants. There are 19 ADAM genes in humans, and ADAMs are expressed in various tissues and cell types. ADAMs have different isoforms due to alternative splicing, which can affect their subcellular localization and activity. ADAMs are synthesized in the rough endoplasmic reticulum and mature in the late Golgi compartment. The prodomain is essential for ADAM maturation and activation, and its removal allows the metalloprotease domain to become active. ADAMs are also involved in the shedding of cytokines and growth factors, such as TNFα, fractalkine, and HB-EGF. ADAMs can also process growth factor receptors, such as the HER4/erbB4 receptor and the CSF-1 receptor. ADAMs are involved in the processing of other molecules, such as insulin-like growth factor-binding proteins and prions. ADAMs also play a role in the processing of the amyloid precursor protein, which is involved in Alzheimer's disease. ADAMs are regulated by various factors, including metalloprotease inhibitors and TIMPs. The study of ADAMs has revealed their importance in various biological processes and their potential as therapeutic targets in diseases such as cancer and Alzheimer's disease.