𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Developmental regulation of calcium-binding proteins (calelectrins and calpactin I) in mammary glands

✍ Scribed by Joseph J. Lozano; Gary B. Silberstein; Soo-In Hwang; Alfred H. Haindl; Victor Rocha


Publisher
John Wiley and Sons
Year
1989
Tongue
English
Weight
925 KB
Volume
138
Category
Article
ISSN
0021-9541

No coin nor oath required. For personal study only.

✦ Synopsis


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.


📜 SIMILAR VOLUMES


Mammary gland Ca2+-binding (-dependent)
✍ Yun Kit Hom; Thomas C. Sudhof; Joseph J. Lozano; Alfred H. Haindl; Victor Rocha 📂 Article 📅 1988 🏛 John Wiley and Sons 🌐 English ⚖ 876 KB

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 monom

Purification, characterization, and loca
✍ Joseph J. Lozano; Alfred H. Haindl; Victor Rocha 📂 Article 📅 1989 🏛 John Wiley and Sons 🌐 English ⚖ 804 KB

Mammary glands contain a group of calcium-sensitive proteins that bind to membranes in a calcium-dependent manner. Using the calcium-dependent binding to hydrophobic surfaces in combination with conventional techniques, we have purified the 70 kDa mammary calcium-binding protein (70 kDa M-CBP) to ho

Activity-dependent regulation of calcium
✍ Philpot, Benjamin D.; Lim, Jae H.; Brunjes, Peter C. 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 694 KB

Intracellular calcium, important in a variety of second messenger cascades, is regulated in part by calcium-binding proteins such as calretinin, parvalbumin, and calbindin. These proteins are highly concentrated in the rat main olfactory bulb and are localized in distinct neuronal populations. In th

1α, 25 dihydroxyvitamin D3-dependent up-
✍ Maria E. Alexianu; Stanley H. Appel; Elaine Robbins; Susan Carswell 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 511 KB

Our understanding of selective neuronal vulnerability as well as etiopathogenesis of sporadic neurodegenerative diseases is extremely limited. In ALS, altered calcium homeostasis appears to contribute significantly to selective neuronal injury. Further in ALS, the absence of calcium binding proteins

Detection and localization of Cripto-1 b
✍ Caterina Bianco; Nicola Normanno; Antonella De Luca; Monica Rosaria Maiello; Chr 📂 Article 📅 2002 🏛 John Wiley and Sons 🌐 English ⚖ 630 KB

## Abstract Human Cripto‐1 (CR‐1), a member of the epidermal growth factor‐CFC (EGF‐CFC) family of peptides, is expressed in the developing mouse mammary gland and can modulate mammary epithelial cell migration, branching morphogenesis and milk protein expression in vitro. In order to screen for a

Expression and function of CCAAT/enhance
✍ L.R. Dearth; J. Hutt; A. Sattler; A. Gigliotti; J. DeWille 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 285 KB 👁 1 views

## Abstract CCAAT/Enhancer binding proteins (C/EBPs) play important roles in the regulation of cell growth and differentiation. This study investigated the expression and function of C/EBPβ isoforms in the mouse mammary gland, mammary tumors, and a nontransformed mouse mammary epithelial cell line