Consensus peptide antibodies reveal a widespread occurrence of Ca2+/lipid-binding proteins of the annexin family.
نویسنده
چکیده
Antibodies generated against synthetic peptides that correspond to highly conserved sequence motifs in the annexins reacted with a variety of annexins from different species. These include Xenopus laevis and Drosophila melanogaster, which contain cross-reacting polypeptides of apparent Mr 34,000 and 30,000. As expected for typical annexins, the two Drosophila proteins interact in a Ca2+-dependent manner with phosphatidylserine liposomes.
منابع مشابه
Serum Factors Induced the Nuclear Location of Annexin V in the Human Osteosarcoma Cell Line (MG-63)
Calcium-binding proteins play essential roles in the cell. One important class of calcium-binding proteins is the annexin family. This is a family of 13 proteins, which binds to phospholipids in a calcium-dependent manner. Osteosarcoma cell line (MG-63) is a transformed cell that has many characteristics of the differentiated cell, such as a considerable serum dependency in its growth rate. Usi...
متن کاملAnnexins: from structure to function.
Annexins are Ca2+ and phospholipid binding proteins forming an evolutionary conserved multigene family with members of the family being expressed throughout animal and plant kingdoms. Structurally, annexins are characterized by a highly alpha-helical and tightly packed protein core domain considered to represent a Ca2+-regulated membrane binding module. Many of the annexin cores have been cryst...
متن کاملStructural requirements for annexin I-S100C complex-formation.
S100C is a member of the S100 family of EF-hand-type Ca(2+)-binding proteins which are thought to bind to and thereby regulate the activity of cellular target proteins in a Ca(2+)-dependent manner. An intracellular ligand for S100C is the Ca2+/phospholipid-binding protein annexin I and we show here that complex-formation is mediated through unique domains within S100C and annexin I. Using a pro...
متن کاملDifferential tissue expression of three 35-kDa annexin calcium-dependent phospholipid-binding proteins.
We have purified three 35-kDa calcium- and phospholipid-binding proteins from rat liver. These three calcimedins bind to phosphatidylserine in a calcium-dependent manner and have been termed 35 alpha, 35 beta, and 35 gamma based on their relative charge as determined by isoelectric focusing. Purification of the three 35-kDa calcimedins is achieved by phenyl-Sepharose, ion exchange, and gel filt...
متن کاملModeling of annexin A2—Membrane interactions by molecular dynamics simulations
The annexins are a family of Ca2+-regulated phospholipid binding proteins that are involved in membrane domain organization and membrane trafficking. Although they are widely studied and crystal structures are available for several soluble annexins their mode of membrane association has never been studied at the molecular level. Here we obtained molecular information on the annexin-membrane int...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- FEBS letters
دوره 258 2 شماره
صفحات -
تاریخ انتشار 1989