Stone A L, Kroeger M, Sang Q X
Department of Chemistry and Institute of Molecular Biophysics, Florida State University, Tallahassee 32306-4390, USA.
J Protein Chem. 1999 May;18(4):447-65. doi: 10.1023/a:1020692710029.
The ADAMs belong to a disintegrin-like and metalloproteinase-containing protein family that are zinc-dependent metalloproteinases. These proteins share all or some of the following domain structure: a signal peptide, a propeptide, a metalloproteinase, a disintegrin, a cysteine-rich, and an epidermal growth factor (EGF)-like domains, a transmembrane region, and a cytoplasmic tail. ADAMs are widely distributed in many organs, tissues, and cells, such as brain, testis, epididymis, ovary, breast, placenta, liver, heart, lung, bone, and muscle. These proteins are capable of four potential functions: proteolysis, adhesion, fusion, and intracellular signaling. Because the number of ADAM genes has grown rapidly and the biological functions of most members are unclear, this review analyzes the protein structures and functions, their activation and processing, their known and potential activities, and their evolutionary relationships. A sequence alignment of human ADAMs is compiled and their homology and physical data are calculated. The conceivable functions of ADAMs in reproduction, development, and diseases are also discussed.
ADAMs属于一个含解整合素样和金属蛋白酶的蛋白质家族，是锌依赖性金属蛋白酶。这些蛋白质具有全部或部分以下结构域：信号肽、前肽、金属蛋白酶、解整合素、富含半胱氨酸结构域、表皮生长因子（EGF）样结构域、跨膜区和胞质尾。ADAMs广泛分布于许多器官、组织和细胞中，如脑、睾丸、附睾、卵巢、乳腺、胎盘、肝脏、心脏、肺、骨骼和肌肉。这些蛋白质具有四种潜在功能：蛋白水解、黏附、融合和细胞内信号传导。由于ADAM基因数量迅速增加且大多数成员的生物学功能尚不清楚，本综述分析了其蛋白质结构与功能、激活与加工过程、已知和潜在活性以及进化关系。编制了人类ADAMs的序列比对，并计算了它们的同源性和物理数据。还讨论了ADAMs在生殖、发育和疾病中的可能功能。
