Electron microscopic cytochemical localization of a basolateral calcium adenosine triphosphatase in vitamin D replete chick enterocytes

A modified Wachstein-Meisel medium containing lead or cerium as capturing ions was used to localize Ca2+-Mg2+ adenosine triphosphatase (ATPase; EC 3.6.1.3) in rat incisor ameloblasts during enamel formation. Sections representing different developmental stages were processed for electron microscopic cytochemistry. Distribution and intensity of the observed reaction product, which was almost exclusively associated with cell membranes, varied according to the stage of enamel formation. During the secretory stage, intense reaction product was evident along the entire plasma membrane of ameloblasts and papillary cells. The early transitional ameloblasts showed reaction product on their proximal and lateral cell membranes, but not distally. In late transitional (pre-absorptive) ameloblasts, distal cell membranes exhibited intense reaction product. During enamel maturation, smooth-ended ameloblasts showed reaction product proximally and laterally, but not distally. Ruffle-ended maturative ameloblasts exhibited intense reaction product along their lateral and distal membranes. The intensity of the latter was decreased but not eliminated by levamisole. In the transition from smooth-ended to ruffle-ended cells, the reaction product became evident distally, concomitant with the appearance of cell membrane invaginations. These data are consistent with a possible role for Ca2+-Mg2+ ATPase in controlling calcium availability at the enamel mineralization front.

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Pregnancy and Lactation Increase Vitamin D-Dependent Intestinal Membrane Calcium Adenosine Triphosphatase and Calcium Binding Protein Messenger Ribonucleic Acid Expression1

Endocrinology ◽

10.1210/endo.139.8.6141 ◽

1998 ◽

Vol 139 (8) ◽

pp. 3520-3524 ◽

Cited By ~ 21

Author(s):

Yingting Zhu ◽

Jesse P. Goff ◽

Timothy A. Reinhardt ◽

Ronald L. Horst

Keyword(s):

Vitamin D ◽

Ribonucleic Acid ◽

Calcium Binding ◽

Adenosine Triphosphatase ◽

Binding Protein ◽

Calcium Binding Protein ◽

Messenger Ribonucleic Acid ◽

Intestinal Membrane ◽

Pregnancy And Lactation ◽

Calcium Adenosine Triphosphatase

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PROBLEMS ASSOCIATED WITH THE DEMONSTRATION BY LEAD METHODS OF ADENOSINE TRIPHOSPHATASE ACTIVITY IN RESIDENT PERITONEAL MACROPHAGES AND EXUDATE MONOCYTES OF THE GUINEA PIG

Journal of Histochemistry & Cytochemistry ◽

10.1177/21.5.488 ◽

1973 ◽

Vol 21 (5) ◽

pp. 488-498 ◽

Cited By ~ 16

Author(s):

R. E. POELMANN ◽

W. T. DAEMS ◽

E. J. VAN LOHUIZEN

Keyword(s):

Plasma Membrane ◽

Guinea Pig ◽

Microscopic Study ◽

Heterogeneous Nucleation ◽

Adenosine Triphosphatase ◽

Peritoneal Macrophages ◽

Electron Microscopic ◽

Adenosine Triphosphatase Activity ◽

Eosinophilic Granulocytes ◽

Membrane Bound

This cytochemical and electron microscopic study on peritoneal macrophages of the guinea pig has raised doubts concerning the validity of lead methods for the demonstration of plasma membrane-bound adenosine triphosphatase activity. The problems encountered are inherent in the use of lead ions as a capture reagent. The nonenzymatically formed precipitates reflect sites of heterogeneous nucleation specific for certain kinds of cells, e.g., resident peritoneal macrophages, eosinophilic granulocytes and, to a lesser degree, exudate monocytes. This type of precipitation is also catalyzed on the surface of nonbiologic matrices such as latex particles. Enzymatic processes may well occur, but they cannot be distinguished from nonenzymatic processes.

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The in vitro effects of vitamin D on oxidative phosphorylation and adenosine triphosphatase activity by rat liver mitochondria

Biochemical Pharmacology ◽

10.1016/0006-2952(75)90041-6 ◽

1975 ◽

Vol 24 (23) ◽

pp. 2127-2132 ◽

Cited By ~ 4

Author(s):

Prakorn Chudapongse ◽

Sirisiln Lowchareonkul

Keyword(s):

Vitamin D ◽

Oxidative Phosphorylation ◽

Rat Liver ◽

Adenosine Triphosphatase ◽

Liver Mitochondria ◽

Rat Liver Mitochondria ◽

Adenosine Triphosphatase Activity ◽

In Vitro Effects

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Cytochemical localization of calcium and Ca2+,Mg2(+)-adenosine triphosphatase in colchicine-altered rat incisor ameloblasts.

Journal of Histochemistry & Cytochemistry ◽

10.1177/38.10.2144864 ◽

1990 ◽

Vol 38 (10) ◽

pp. 1469-1478 ◽

Cited By ~ 9

Author(s):

D R Eisenmann ◽

A H Salama ◽

A M Zaki ◽

S H Ashrafi

Keyword(s):

Electron Microscopy ◽

Transmission Electron Microscopy ◽

Adenosine Triphosphatase ◽

Morphological Changes ◽

Rat Incisor ◽

Cytochemical Localization ◽

Early Maturation ◽

Transmission Electron ◽

Maturation Stages ◽

Secretory Transport

Colchicine is known to affect secretory, transport, and degradative functions of ameloblasts. The effects of colchicine on membrane-associated calcium and Ca2+,Mg2(+)-ATPase in secretory and maturation ameloblasts were investigated cytochemically. The pyroantimonate (PPA) method was used for localizing calcium and a modified Wachstein-Meisel medium was used to localize Ca2+,Mg2(+)-ATPase. Sections representing secretory and early maturation stages were examined by transmission electron microscopy. Morphological changes induced by colchicine included dislocated organelles and other well-established reactions to such anti-microtubule drugs. Calcium pyroantimonate (Ca-PA) deposits in most ameloblast types were markedly reduced, with the greater reduction occurring in those cells more severely altered morphologically. However, the cell membranes of both control and experimental smooth-ended maturation ameloblasts were essentially devoid of Ca-PA. The normal distribution and intensity of Ca2+,Mg2(+)-ATPase was not affected by colchicine. Because the observed reduction of membrane-associated calcium is apparently not mediated by Ca2+,Mg2(+)-ATPase in this case, other aspects of the calcium regulating system of ameloblasts are apparently targeted by colchicine.

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Preeclampsia and calcium adenosine triphosphatase activity of red blood cell ghosts

American Journal of Obstetrics and Gynecology ◽

10.1016/0002-9378(94)90161-9 ◽

1994 ◽

Vol 171 (5) ◽

pp. 1361-1365 ◽

Cited By ~ 20

Author(s):

Gianfranco Nardulli ◽

Fulgencio Proverbio ◽

Flor G. Limongi ◽

Reinaldo Marín ◽

Teresa Proverbio

Keyword(s):

Blood Cell ◽

Red Blood Cell ◽

Adenosine Triphosphatase ◽

Adenosine Triphosphatase Activity ◽

Calcium Adenosine Triphosphatase

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Studies in vitro on the effects of 1H,2H,4H(5H)-octafluorocyclohexane and 1H,4H(2H)-nonafluorocyclohexane on enzymes and organelles

Biochemical Journal ◽

10.1042/bj1140785 ◽

1969 ◽

Vol 114 (4) ◽

pp. 785-792 ◽

Cited By ~ 1

Author(s):

Jayasree Nath ◽

H G Bray

Keyword(s):

Adenosine Triphosphatase ◽

Marked Decrease ◽

Reductase Activity ◽

Electron Microscopic Examination ◽

Electron Microscopic ◽

Toxic Compound ◽

Marked Inhibition ◽

Liver Homogenates ◽

Nadh Cytochrome

A comparison has been made of the effect of 1H,2H,4H(5H)-octafluorocyclohexane, which is highly toxic (LD50 17mg./kg. in rats), and of 1H,4H(2H)-nonafluorocyclohexane, which is relatively non-toxic (LD50>440mg./kg. in rats), on the respiration of rat liver homogenates and mitochondria in vitro. 1H,2H,4H(5H)-Octafluorocyclohexane strongly inhibited the respiration of both homogenates and mitochondria, but neither compound had any significant effect on glycolysis or on glutamate dehydrogenase or NADH–cytochrome c reductase activity. 1H,2H,4H(5H)-Octafluorocyclohexane, however, caused a very marked inhibition of cytochrome oxidase activity, causing an almost complete lesion in this region of the respiratory chain. 1H,4H(2H)-Nonafluorocyclohexane was without effect in this respect. A marked decrease in turbidity of mitochondrial suspensions at 520nm. was caused by addition of both compounds, the effect being greater with 1H,2H,4H(5H)-octafluorocyclohexane. ATP, Mg2+ and bovine serum albumin did not reverse these changes. Mitochondrial adenosine triphosphatase activity was increased twofold by the toxic compound, but only slightly by the non-toxic compound. Electron-microscopic examination of mitochondria treated with 1H,2H,4H(5H)-octafluorocyclohexane revealed gross morphological damage, whereas the effect of 1H,4H(2H)-nonafluorocyclohexane appeared to be merely to cause swelling. The results obtained account, to some extent at any rate, for the toxic effects of 1H,2H,4H(5H)-octafluorocyclohexane.

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