Expression of PTHrP and the PTH/PTHrP Receptor in Purified Alveolar Epithelial Cells, Myoepithelial Cells, and Stromal Fibroblasts Derived from the Lactating Rat Mammary Gland

1999 ◽  
Vol 248 (2) ◽  
pp. 415-422 ◽  
Author(s):  
S.F. Wojcik ◽  
C.C. Capen ◽  
T.J. Rosol
1996 ◽  
Vol 270 (3) ◽  
pp. L353-L361 ◽  
Author(s):  
R. H. Hastings ◽  
D. Summers-Torres ◽  
T. C. Cheung ◽  
L. S. Ditmer ◽  
E. M. Petrin ◽  
...  

Alveolar epithelial cells in vivo, primary cultures of adult rat type II cells, and human A549 alveolar carcinoma cells express parathyroid hormone-related protein (PTHrP). Here we demonstrated that type II cells and A549 cells also express the PTHrP receptor and that they exhibit differentiation-related responses to the amino-terminal PTHrP fragment, PTHrP-(1-34). PTHrP receptor expression in A549 cells was shown by detection of a 0.3-kb reverse transcriptase polymerase chain reaction product formed by primers specific for PTHrP receptor. In situ hybridization studies localized the site of production of PTHrP and PTHrP receptor mRNA in rat lung cells with morphology and location typical of type II cells. Primary cultures of such type II cells also expressed PTHrP receptor mRNA. Incubation with PTHrP-(1-34) stimulated disaturated phosphatidylcholine (DSPC) synthesis in A549 cells and increased the release of newly synthesized DSPC by cultured type II cells and A549 cells. In addition, PTHrP-(1-34) increased the number of lamellar bodies per type II cell and increased their expression of alkaline phosphatase in a dose-dependent manner. Thus PTHrP-(1-34) promoted a differentiated type II cell phenotype. Since cultured type II cells, alveolar epithelial cells in vivo, and A549 cells express PTHrP and the PTHrP receptor, PTHrP-(1-34) may be an autocrine regulatory factor in type II cells and lung cancer cells.


1989 ◽  
Vol 94 (3) ◽  
pp. 545-552
Author(s):  
R.S. Mahendran ◽  
M.J. O'Hare ◽  
M.G. Ormerod ◽  
P.A. Edwards ◽  
R.A. McIlhinney ◽  
...  

A monoclonal antibody (25.5) has been produced that recognises luminal epithelial cells of the rat mammary gland. This antibody together with monoclonal anti-CALLA antibodies, which react with mammary myoepithelial cells, has been used in biochemical, immunocytochemical and flow cytometric studies. Antibody 25.5 bound to proteins of molecular weight 70K and 25K (K = 10(3) Mr) in both the rat milk fat globule membrane and in single cell suspensions prepared from the virgin adult rat mammary gland. Anti-CALLA antibody (J5), recognised a 93–100K protein in the gland extracts, which co-electrophoresed with the CALLA/CD-10 antigen from NALM-6 acute lymphoblastic leukaemia cell line. Antibody 25.5 bound to the luminal surface of rat mammary epithelial cells at all stages of development from neonatal through to pregnancy, lactation and involution. CALLA immunoreactive staining has previously been shown on basally located presumptive myoepithelial cells at all stages of development. Flow cytometric analyses demonstrated that 25.5 and anti-CALLA antibodies stained independent cell populations in suspensions of single cells prepared from purified epithelial elements from the mammary gland of adult virgin rat.


1971 ◽  
Vol 51 (1) ◽  
pp. 127-135 ◽  
Author(s):  
R. C. RICHARDS ◽  
G. K. BENSON

SUMMARY Adult female rats undergoing their first lactation were experimentally weaned by removing their pups on day 4 of lactation. The initial phase of mammary gland involution began with the removal of protein granules from the milk by digestion in large stasis vacuoles in the alveolar epithelial cells. Later stages involved a progressive necrosis of the epithelial cells by auto-phagocytosis. Removal of fat droplets and cellular debris occurred at this time and was accomplished by macrophage-like cells. Finally, epithelial cells were detached from the basement membrane and were found, in varying stages of degeneration, lying free in the lumina of the alveoli.


1982 ◽  
Vol 30 (7) ◽  
pp. 667-676 ◽  
Author(s):  
M J Warburton ◽  
D Mitchell ◽  
E J Ormerod ◽  
P Rudland

Using antisera to specific proteins, the localization of the rat mammary parenchymal cells (both epithelial and myoepithelial), the basement membrane, and connective tissue components has been studied during the four physiological stages of the adult rat mammary gland, viz. resting, pregnant, lactating, and involuting glands. Antisera to myosin and prekeratin were used to localize myoepithelial cells, antisera to rat milk fat globule membrane for epithelial cells, antisera to laminin and type IV collagen to delineate the basement membrane and antisera to type I collagen and fibronectin as markers for connective tissue. In the resting, virgin mammary gland, myoepithelial cells appear to form a continuous layer around the epithelial cells and are in turn surrounded by a continuous basement membrane. Antiserum to fibronectin does not delineate the basement membrane in the resting gland. The ductal system is surrounded by connective tissue. Only the basal or myoepithelial cells in the terminal end buds of neonatal animals demonstrate cytoplasmic staining for basement membrane proteins, indicating active synthesis of these proteins during this period. In the secretory alveoli of the lactating rat, the myoepithelial cells no longer appear to form a continuous layer beneath the epithelial cells and in many areas the epithelial cells appear to be in contact with the basement membrane. The basement membrane in the lactating gland is still continuous around the ducts and alveoli. In the lactating gland, fibronectin appears to be located in the basement membrane region in addition to being a component of the stroma. During involution, the alveoli collapse, and appear to be in a state of dissolution. The basement membrane is thicker and is occasionally incomplete, as also are the basket-like myoepithelial structures. Basement membrane components can also be demonstrated throughout the collapsed alveoli.


Pneumologie ◽  
2014 ◽  
Vol 68 (06) ◽  
Author(s):  
S Seehase ◽  
B Baron-Luehr ◽  
C Kugler ◽  
E Vollmer ◽  
T Goldmann

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