A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions
نویسندگان
چکیده
Since the discovery of the first disintegrin protein from snake venom and the following identification of a mammalian membrane-anchored metalloprotease-disintegrin implicated in fertilization, almost three decades of studies have identified additional members of these families and several biochemical mechanisms regulating their expression and activity in the cell. Most importantly, new in vivo functions have been recognized for these proteins including cell partitioning during development, modulation of inflammatory reactions, and development of cancers. In this review, we will overview the a disintegrin and metalloprotease (ADAM) family of proteases highlighting some of the major research achievements in the analysis of ADAMs' function that have underscored the importance of these proteins in physiological and pathological processes over the years.
منابع مشابه
ADAM Gene Expression in The Adult CNS and Genetic Aberrations in Cancer Cells
ADAM metalloprotease-disintegrins share a common modular structure of functional domains for proteolytic, cell adhesion, and signaling interactions. The metalloprotease domain of oughly half of the known ADAMs contain an intact consensus metzincin catalytic site, and they are thus thought to function as active metalloproteases. The types of interactions mediated by ADAMs are expressly conspicu...
متن کاملA Role for the Disintegrin Domain of Cyritestin, a Sperm Surface Protein Belonging to the ADAM Family, in Mouse Sperm–Egg Plasma Membrane Adhesion and Fusion
Sperm-egg plasma membrane fusion is preceded by sperm adhesion to the egg plasma membrane. Cell-cell adhesion frequently involves multiple adhesion molecules on the adhering cells. One sperm surface protein with a role in sperm-egg plasma membrane adhesion is fertilin, a transmembrane heterodimer (alpha and beta subunits). Fertilin alpha and beta are the first identified members of a new family...
متن کاملADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell- matrix interactions
C ELL--cell and cell-matrix adhesion, as well as proteolysis of the extracellular matrix, are vital for normal processes such as tissue morphogenesis and wound healing, as well as for pathologies such as tumor cell invasion and metastasis. A variety of cell surface adhesion proteins and proteases are important players in these events. Families of membrane-anchored cell surface adhesion molecule...
متن کاملMetalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells.
ADAM 12, a member of the ADAM (protein containing a disintegrin and metalloprotease) family of metalloprotease-disintegrins, has been implicated in the differentiation and fusion of skeletal myoblasts, and its expression is dramatically up-regulated in many cancer cells. While the extracellular portion of ADAM 12 contains an active metalloprotease and a cell-adhesion domain, the function of the...
متن کاملBiomarker to distinguish hepatocellular carcinoma from cholangiocarcinoma by serum a disintegrin and metalloprotease 12
INTRODUCTION The "a distintegrin and metalloprotease" (ADAM) family contributes to regulation of the cell-cell and cell-matrix interaction that are critical determinants of malignancy. It also plays important roles in the degradation of the basement membrane during tumor invasion. To evaluate a distinguishing biomarker for hepatocellular carcinoma from cholangiocarcinoma, a disintegrin and meta...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره 8 شماره
صفحات -
تاریخ انتشار 2016