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- W2000690165 abstract "Calcium-binding (-dependent) proteins (CBPs) associated with the spreading of mammary epithelial cell cultures have been identified as various calelectrins and calpactins (p36). In immunoblot analysis, the CBPs of 30-36 kD and 68-70 kD variously react with different calelectrin and calpactin I monomer/p36 antisera. The same immunoreactive proteins were shown to be present in virgin mammary glands and collagen gel mouse mammary epithelial cell cultures. The mammary CBPs show extensive immunochemical relatedness; however, they fail to show cross-reaction with antiserum to calpactin II (lipocortin) antiserum. These immunoreactive CBPs comigrate in electrophoresis with 35S-methionine-labeled CBPs isolated from mammary epithelial cell cultures. Unlike calmodulin, the mammary CBPs that correspond to calelectrins and calpactin I monomer/p36 are not stable to thermal denaturation. The mammary CBPs bind to epithelial cell membranes in a Ca2+-dependent manner and are differentially released from ruptured cells, compared with calmodulin, suggesting subcellular localization. Phenothiazine-agarose and phenylagarose are equivalent in their ability to bind the mammary CBPs. Thus, mammary gland CBPs of 30-36 kD and 68-70 kD have been shown to be related or equivalent to the calelectrins and to calpactin I monomer/p36. Since these proteins are known to bind Ca2+, we conclude that the mammary gland CBPs are also Ca2+-binding proteins. The mammary gland CBPs are immunologically related and probably represent members of a larger family of related proteins." @default.
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- W2000690165 date "1988-06-01" @default.
- W2000690165 modified "2023-09-25" @default.
- W2000690165 title "Mammary gland Ca2+-binding (-dependent) proteins: Identification as calelectrins and calpactin I/p36" @default.
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- W2000690165 doi "https://doi.org/10.1002/jcp.1041350310" @default.
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