Developmental regulation of calcium‐binding proteins (calelectrins and calpactin I) in mammary glands
- 1 March 1989
- journal article
- research article
- Published by Wiley in Journal of Cellular Physiology
- Vol. 138 (3) , 503-510
- https://doi.org/10.1002/jcp.1041380309
Abstract
We recently showed that mammary glands contain a novel class of calcium‐binding proteins (CBPs) that bind to membranes in a calcium‐dependent manner. We have also established that these mammary CBPs are equivalent to the calelectrins and calpactin I/p36. Since it has been suggested that these proteins might be involved in exocytosis, we examined mammary glands for these CBPs during secretory differentiation. Immunohistochemical examination showed, glands from virgin animals to be rich in calelectrins and calpactin I/p36, while glands from lactating animals contained little immunoreactive material. In addition, silver‐staining and immunoblot estimation of the CBPs in lysates from collagenase harvested secretory epithelia showed these proteins to be significantly reduced compared to nonsecretory epithelia. Close examination of the CBP immunoreactive cells of the mammary gland shows that ductal cells are prominent in their staining and that the immunoreactive material is associated with the cell surface. Also, in juvenile glands the.myoepithelial stem cells (cap cells) of the elongating end bud are devoid of the CBPs. In contrast to the in vivo data, epithelia cultivated on collagen gels demonstrate comparable levels of the CBPs in both nonsecretory and secretory monolayers. The in vivo data indicate that the CBPs are developmentally regulated during mammary gland differentiation such that secretory epithelia are essentially devoid of these novel proteins. Furthermore, a role for calelectrin and calpactin I/p36 in exocytotic casein secretion is questioned.This publication has 40 references indexed in Scilit:
- Calpactins: two distinct Ca++-regulated phospholipid- and actin-binding proteins isolated from lung and placenta.The Journal of cell biology, 1987
- High-level expression of the 32.5-kilodalton calelectrin in ductal epithelia as revealed by immunocytochemistryDifferentiation, 1986
- Basal lamina inhibition suppresses synthesis of calcium-dependent proteins associated with mammary epithelial cell spreadingExperimental Cell Research, 1986
- Casein production during differentiation of mammary epithelial cells in collagen gel cultureExperimental Cell Research, 1985
- Synthesis of novel calcium-dependent proteins associated with mammary epithelial cell migration and differentiationExperimental Cell Research, 1984
- Calelectrins are a ubiquitous family of Ca2+-binding proteins purified by Ca2+-dependent hydrophobic affinity chromatography by a mechanism distinct from that of calmodulinBiochemical and Biophysical Research Communications, 1984
- The 34 kd pp60src substrate is located at the inner face of the plasma membraneCell, 1983
- Glycosaminoglycans in the basal lamina and extracellular matrix of the developing mouse mammary ductDevelopmental Biology, 1982
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970