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

@article{Walker1983CalelectrinAC,
  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},
  year={1983},
  volume={41}
}
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… 

Calmodulin Binding Proteins of the Cholinergic Electromotor Synapse: Synaptosomes, Synaptic Vesicles, Receptor‐Enriched Membranes, and Cytoskeleton

TLDR
Calmodulin binding proteins (CBPs) have been identified using a gel overlay technique for fractions isolated from Torpedo electromotor nerve endings using data from Triton X‐100‐insoluble cytoskeleton of synaptosomes and calelectrin does not bind calmodulin.

Isolation of mammalian calelectrins: a new class of ubiquitous Ca2+-regulated proteins.

TLDR
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)

TLDR
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

Characterization of Calelectrin, a Ca2+‐Binding Protein Isolated from the Electric Organ of Torpedo marmorata

TLDR
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.

Calcium-sensitive, lipid-binding cytoskeletal proteins of the human placental microvillar region

TLDR
A group of Ca2+-sensitive proteins located in the microvillar region of the human placental syncytiotrophoblast are described that associate with both the cytoskeleton and lipid at high concentrations of free Ca2+.

Collagen‐Binding proteins of mammary epithelial cells are related to Ca2+‐and phospholipid‐binding annexins

TLDR
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.

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