Transepithelial Calcium Transport in Gut and Kidney

1990 ◽  
pp. 199-223 ◽  
Author(s):  
Felix Bronner
Keyword(s):  
Calcium Transport

Ca++-ATPase activity in the hepatopancreas cells of Oniscus asellus

1992 ◽  
Vol 50 (1) ◽  
pp. 820-821
Author(s):  
G.M. Vernon ◽  
A. Surace ◽  
R. Witkus
Keyword(s):  
B Cells ◽  
Epithelial Cell ◽  
Atpase Activity ◽  
Calcium Transport ◽  
Carcinus Maenas ◽  
Cell Types ◽  
Molt Cycle ◽  
Copper And Zinc

The hepatopancreas consists of a pair of bilobed tubules comprised of two epithelial cell types. S cells are absorptive and accumulate metals such as copper and zinc. Ca++ concentrations vary between the S and B cells and during the molt cycle. Roer and Dillaman implicated Ca++-ATPase in calcium transport during molting in Carcinus maenas. This study was undertaken to compare the localization of Ca++-ATPase activity in the S and B cells during intermolt.

Immunogold localization of calmodulin in root caps of the maize Cultivar Merit

1990 ◽  
Vol 48 (3) ◽  
pp. 674-675
Author(s):  
P.T. Nguyen ◽  
C. Uphoff ◽  
C.L. Stinemetz
Keyword(s):  
Calcium Binding ◽  
Calcium Transport ◽  
Primary Role ◽  
Immunogold Localization ◽  
Root Tips ◽  
Electrical Currents ◽  
Considerable Evidence ◽  
Maize Cultivar ◽  
Gravity Response ◽  
Induced Changes

Considerable evidence suggest that the calcium-binding protein calmodulin (CaM) may mediate calcium action and/or transport important in the gravity response of plants. Calmodulin is present in both shoots and roots and is capable of regulating calcium transport in plant vesicles. In roots calmodulin is concentrated in the tip, the gravisensing region of the root; and is reported to be closely associated with amyloplasts, organelles suggested to play a primary role in gravi-perception. Inhibitors of CaM such as chlorpromazine, calmidazolium, and compound 48/80 interfere with the gravitropic response of both snoots and roots. The magnitude of the inhibition corresponded well with the extent to which the drug binds to endogenous CaM. Compound 48/80 and calmidazolium block gravi-induced changes in electrical currents across root tips, a phenomenon thought to be associated with the sensing of the gravity stimulus.In this study, we have investigated the subcellular distribution of CaM in graviresponsive and non-graviresponsive root caps of the maize cultivar Merit.

Effectiveness of insulin therapy on altered renal calcium transport in diabetic rats

Diabetes ◽  
1979 ◽  
Vol 28 (12) ◽  
pp. 1088-1094 ◽  
Author(s):  
B. Hoskins ◽  
R. Y. Feibelman ◽  
A. M. Koury ◽  
R. Taylor
Keyword(s):  
Insulin Therapy ◽  
Calcium Transport ◽  
Diabetic Rats ◽  
Renal Calcium Transport

Calcium transport in turtle bladder

1987 ◽  
Vol 253 (6) ◽  
pp. R917-R921
Author(s):  
S. Sabatini ◽  
N. A. Kurtzman
Keyword(s):  
Calcium Transport ◽  
Calcium Absorption ◽  
Short Circuit ◽  
Open Circuit ◽  
Calcium Flux ◽  
Bladder Epithelium ◽  
Control Value ◽  
Sodium Calcium ◽  
Turtle Bladder ◽  
Absorptive Flux

Unidirectional 45Ca fluxes were measured in the turtle bladder under open-circuit and short-circuit conditions. In the open-circuited state net calcium flux (JnetCa) was secretory (serosa to mucosa) and was 388.3 +/- 84.5 pmol.mg-1.h-1 (n = 20, P less than 0.001). Ouabain (5 X 10(-4) M) reversed JnetCa to an absorptive flux (serosal minus mucosal flux = -195.8 +/- 41.3 pmol.mg-1.h-1; n = 20, P less than 0.001). Amiloride (1 X 10(-5) M) reduced both fluxes such that JnetCa was not significantly different from zero. Removal of mucosal sodium caused net calcium absorption; removal of serosal sodium caused calcium secretion. When bladders were short circuited, JnetCa decreased to approximately one-third of control value but remained secretory (138.4 +/- 54.3 pmol.mg-1.h-1; n = 9, P less than 0.025). When ouabain was added under short-circuit conditions, JnetCa was similar in magnitude and direction to ouabain under open-circuited conditions (i.e., absorptive). Tissue 45Ca content was approximately equal to 30-fold lower when the isotope was placed in the mucosal bath, suggesting that the apical membrane is the resistance barrier to calcium transport. The results obtained in this study are best explained by postulating a Ca2+-ATPase on the serosa of the turtle bladder epithelium and a sodium-calcium antiporter on the mucosa. In this model, the energy for calcium movement would be supplied, in large part, by the Na+-K+-ATPase. By increasing cell sodium, ouabain would decrease the activity of the mucosal sodium-calcium exchanger (or reverse it), uncovering active calcium transport across the serosa.

scholarly journals ATP-linked calcium transport in cells and membrane vesicles of Streptococcus faecalis.

1978 ◽  
Vol 253 (7) ◽  
pp. 2085-2092 ◽  
Author(s):  
H. Kobayashi ◽  
J. Van Brunt ◽  
F.M. Harold
Keyword(s):  
Calcium Transport ◽  
Membrane Vesicles ◽  
Streptococcus Faecalis ◽  
In Cells
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