Calelectrin, a Calcium‐Dependent Membrane‐Binding Protein Associated with Secretory Granules in Torpedo Cholinergic Electromotor Nerve Endings and Rat Adrenal Medulla

  title={Calelectrin, a Calcium‐Dependent Membrane‐Binding Protein Associated with Secretory Granules in Torpedo Cholinergic Electromotor Nerve Endings and Rat Adrenal Medulla},
  author={J. H. Walker and Jost Obrocki and Thomas C. S{\"u}dhof},
  journal={Journal of Neurochemistry},
Abstract: Calelectrin, a calcium‐dependent membrane‐binding protein of subunit molecular weight 32,000 has been isolated from the electric organ of Torpedo, and shown to occur in cholinergic neurones and in bovine adrenal medulla. In this study a monospecific antiserum against the Torpedo protein has been used to study the localization of calelectrin in the rat adrenal gland. The cortex was not stained, whereas in the medulla the cytoplasm of the chromaffin cells was stained in a particulate… 
Immunocytochemical localization of annexin V (CaBP33), a Ca2+‐dependent phospholipid‐and membrane‐binding protein, in the rat nervous system and skeletal muscles and in the porcine heart
The hypothesis that annexin V might be involved in membrane trafficking is supported and a role for this protein in the regulation of cytoplasmic activities in glial cells is suggested.
Isolation of mammalian calelectrins: a new class of ubiquitous Ca2+-regulated proteins.
It is suggested that the evolutionary conservation and diversification, the high tissue concentrations, and the Ca2+-specific interactions of the calelectrins make them candidates for Ca2-dependent regulators of membrane events in animal cells.
Control of the Amount of a 34K Ca2+‐Dependent Membrane Binding Protein (Calelectrin)
Results support the idea that 34K is an important structural constituent of mature synapses, an observation suggesting the involvement of this protein in the function of the mature synapse.
Calpactins: two distinct Ca++-regulated phospholipid- and actin-binding proteins isolated from lung and placenta
Three forms of calpactin, the 36,000 Mr Ca++-binding cytoskeletal protein, were isolated in large amounts from bovine lung and human placenta using cycles of calcium-dependent precipitation followed
Isolation of a calcium‐sensitive, 35,000‐dalton microfilament‐ and liposome‐binding protein from ascites tumor cell microvilli: Identification as monomeric calpactin
Findings indicate that AMV‐p35 is closely related to the pp60src kinase substrate calpactin I, however, it occurs in the microvilli as a monomer rather than as the heterotetrameric calPactin found in several other cell types.
Characterization of Calelectrin, a Ca2+‐Binding Protein Isolated from the Electric Organ of Torpedo marmorata
It is concluded that calelectrin is a Ca2+‐binding protein whose binding to the lipid moieties of membranes is regulated by physiological changes in theCa2+ concentration.
Collagen‐Binding proteins of mammary epithelial cells are related to Ca2+‐and phospholipid‐binding annexins
Three major proteins of 34, 36, and 38 kDa were isolated from mebrane preparations of chemically induced mammary tumors of the rat by collagen type I affinity chromatography and therefore were termed collagen‐binding proteins (CBP), demonstrated to be immunologically related to CBP.
High-level expression of the 32.5-kilodalton calelectrin in ductal epithelia as revealed by immunocytochemistry.
Due to the presence of high levels of 32.5-kilodalton calelectrin in some cell types, this protein may be used as a histochemical marker for differentiated ductal epithelial cells, some specialized epithelia, myocardial cells, and Paneth cells.


Isolation from Cholinergic Synapses of a Protein That Binds to Membranes in a Calcium‐Dependent Manner
  • J. Walker
  • Biology, Chemistry
    Journal of neurochemistry
  • 1982
A protein that binds to membranes in a calcium‐dependent manner between calcium concentrations of 10−5 and 10−6M has been isolated in large amounts from the entirely cholinergic electric organ of Torpedo marmorata and was localised in the synaptic region of the electric organ by means of immunofluorescence.
Calcium‐Dependent Binding of Cytosolic Proteins by Chromaffin Granules from Adrenal Medulla
Purified chromaffin granules from bovine adrenal medulla bound a small group of medullary cell cytosol proteins at micromolar levels of Ca2+ and physiological levels of K+, Mg2+, and Mg‐ATP, which did not correspond with any previously reported cytosolic components of Chromaffin cells.
Calelectrin self‐aggregates and promotes membrane aggregation in the presence of calcium.
The Ca2+‐induced self‐association of calelectrin and its aggregation enhancing effect may be of great importance to the structural organization of neural and secretory cells and the mechanism of exocytosis.
Abstract— Fluorescein isothiocyanate‐labelled lectins were used to identify lectin‐binding glycoproteins of the chromaffin granule after electrophoresis of the membrane and soluble granule proteins
Chemical composition of cholinergic synaptic vesicles from Torpedo marmorata based on improved purification.
Cholinergic synaptic vesicles from the electric organ of Torpedo marmorata have been purified to a constant composition and a higher transmitter content than previously reported, and characterisation by two-dimensional gel electrophoresis suggested that it is an actin-like polypeptide.
Mechanochemical properties of brain clathrin: interactions with actin and alpha-actinin and polymerization into basketlike structures or filaments.
Because of clathrin's biochemical and biophysical properties, its interaction with contractile proteins, and its presence in the membrane of vesicles of various cell types, it is classified in the group of mechanochemical proteins.
Fodrin: axonally transported polypeptides associated with the internal periphery of many cells
Fodrin is a specific component of the cortical cytoplasm of many cells and the possibilities are considered: (a) that fodrin may be indirectly attached to the plasma membrane via cortical actin filaments; (b) that F-actin could serve to link other proteins and organelles to a submembrane force-generating system.