Cellular and paracellular calcium transport in rat ileum: effects of dietary calcium.

1978 ◽  
Vol 235 (6) ◽  
pp. E726 ◽  
Author(s):  
H N Nellans ◽  
D V Kimberg
Keyword(s):  
Brush Border ◽  
Calcium Transport ◽  
Voltage Dependence ◽  
Electrochemical Gradient ◽  
Rat Ileum ◽  
Low Calcium Diet ◽  
Absolute Effect ◽  
Paracellular Pathways ◽  
Cellular Ca

The mechanism of calcium transport and its modulation by dietary Ca restriction in rat ileum have been investigated employing an in vitro voltage-clamp technique. Ca fluxes directed from mucosa-to-serosa (J(Ca)ms) and serosa-to-mucosa (J(Ca)sm) exhibit components consistent with both cellular and paracellular pathways. The cellular Ca fluxes are both dependent on medium Na and are abolished at 10 degrees C. In addition, a cellular component of J(Ca)ms displays voltage dependence. A low-calcium diet, which induces the formation of 1,25-dihydroxycholecalciferol, causes a marked increase in both cellular J(Ca)ms and Ca influx from media to cells with little absolute effect on the paracellular pathway. This evidence is consistent with the existence of electrogenic Na-Ca exchange pumps at both brush-border and basolateral membranes, driven in part by the Na electrochemical gradient. Dietary Ca conditioning may control the direction of net Ca transport by modulation of the saturable influx process at the brush border.

Calcium transport in the ileum of uremic rats

1982 ◽  
Vol 242 (2) ◽  
pp. G128-G134
Author(s):  
M. Koller ◽  
U. Binswanger
Keyword(s):  
Renal Failure ◽  
Calcium Transport ◽  
Dihydroxyvitamin D3 ◽  
Calcium Diet ◽  
Low Calcium Diet ◽  
Low Calcium ◽  
Unidirectional Fluxes ◽  
Small Intestinal ◽  
Normal Calcium

Duodenal and ileal calcium transport was studied by 45Ca uptake and estimation of unidirectional fluxes in vitro in kidney-intact and 5/6-nephrectomized rats. After normal-calcium diet, calcium transport was impaired by uremia in the duodenum but not in the ileum. However, 5/6-nephrectomized rats on low-calcium diet showed, in concert with impaired growth, a reduced calcium transport both in duodenum and ileum. Comparing data after normal- and low-calcium diets, the ileal adaptation to low-calcium diet was intact in mild renal failure but abolished in severe uremia (urea less than 100 mg/dl). These results suggest that ileal calcium transport after normal-calcium diet is mainly passive. Taking into account reduced food intake as an additional factor, the active ileal calcium transport after low-calcium diet declines with progressive renal failure according to decreasing levels of 1,25-dihydroxyvitamin D3. A suspected enhancement of the distal small intestinal calcium transport by parathyroid hormone in uremic rats as compensation for proximally impaired absorption could not be demonstrated.

scholarly journals Myosin 1a Regulates Osteoblast Differentiation Independent of Intestinal Calcium Transport

2019 ◽  
Vol 3 (11) ◽  
pp. 1993-2011
Author(s):  
Scott Munson ◽  
Yongmei Wang ◽  
Wenhan Chang ◽  
Daniel D Bikle
Keyword(s):  
Intestinal Epithelium ◽  
Brush Border ◽  
Calcium Transport ◽  
Osteoblast Differentiation ◽  
Epithelial Cell Line ◽  
Null Mouse ◽  
Normal Numbers ◽  
Calmodulin Binding ◽  
Intestinal Calcium Transport

Abstract Myosin 1A (Myo1a) is a mechanoenzyme previously thought to be located exclusively in the intestinal epithelium. It is the principle calmodulin-binding protein of the brush border. Based on earlier studies in chickens, we hypothesized that Myo1a facilitates calcium transport across the brush border membrane of the intestinal epithelium, perhaps in association with the calcium channel Trpv6. Working with C2Bbe1 cells, a human intestinal epithelial cell line, we observed that overexpression of Myo1a increased, whereas the antisense construct blocked calcium transport. To further test this hypothesis, we examined mice in which either or both Myo1a and Trpv6 had been deleted. Although the Trpv6-null mice had decreased intestinal calcium transport, the Myo1a-null mouse did not, disproving our original hypothesis, at least in mice. Expecting that a reduction in intestinal calcium transport would result in decreased bone, we examined the skeletons of these mice. To our surprise, we found no decrease in bone in the Trpv6-null mouse, but a substantial decrease in the Myo1a-null mouse. Double deletions were comparable to the Myo1a null. Moreover, Myo1a but not Trpv6 was expressed in osteoblasts. In vitro, the bone marrow stromal cells from the Myo1a-null mice showed normal numbers of colony-forming units but marked decrements in the formation of alkaline phosphatase–positive colonies and mineralized nodules. We conclude that Myo1a regulates osteoblast differentiation independent of its role, if any, in intestinal calcium transport, whereas Trpv6 functions primarily to promote intestinal calcium transport with little influence in osteoblast function.

Evidence for Active Transport of Tripeptides by Hamster Jejunum in Vitro

1975 ◽  
Vol 49 (4) ◽  
pp. 305-312 ◽  
Author(s):  
Jill M. Addison ◽  
D. Burston ◽  
J. W. Payne ◽  
S. Wilkinson ◽  
D. M. Matthews
Keyword(s):  
Active Transport ◽  
Intestinal Mucosa ◽  
Brush Border ◽  
Structural Features ◽  
Intestinal Wall ◽  
Metabolic Inhibitors ◽  
Electrochemical Gradient ◽  
Intracellular Compartment ◽  
Active Mechanism

1. This paper describes the uptake by rings of everted hamster jejunum in vitro of three peptides with structural features making them resistant to hydrolysis, glycylsarcosylsarcosine, glycylsarcosylsarcosylsarcosine and β-alanylglycylglycine. 2. Glycylsarcosylsarcosine was taken up by a saturable mechanism and accumulated intact in the intracellular compartment of the intestinal wall, apparently against an electrochemical gradient. Its uptake was reduced by Na+-replacement, anoxia and metabolic inhibitors. It was concluded that uptake of this peptide was the result of Na+-dependent active transport. 3. Glycylsarcosylsarcosylsarcosine was very poorly taken up and its uptake did not appear to be the result of active transport. 4. β-Alanylglycylglycine appeared intact in the intracellular compartment of the intestinal wall on a substantial scale though it was not concentrated. No satisfactory evidence of uptake by a saturable mechanism was obtained. Uptake was, however, inhibited by anoxia, 2,4-dinitrophenol and Na+-replacement. Reasons are given for supposing that uptake of this peptide may be the result of Na+-dependent active transport by the same carrier as that utilized by glycylsarcosylsarcosine. 5. The results suggest that provided that they escape brush-border hydrolysis, tripeptides, like dipeptides, are actively transported into the absorptive cells of the intestinal mucosa, but that the ability of these cells to take up peptides by an active mechanism is unlikely to extend to tetrapeptides.

Transepithelial calcium transport by rat cecum: high-efficiency absorptive site

1981 ◽  
Vol 240 (6) ◽  
pp. G424-G431 ◽  
Author(s):  
H. N. Nellans ◽  
R. S. Goldsmith
Keyword(s):  
Calcium Transport ◽  
High Efficiency ◽  
Calcium Absorption ◽  
Short Circuit ◽  
Calcium Fluxes ◽  
Calcium Diet ◽  
Low Calcium Diet ◽  
High Calcium ◽  
Rat Cecum

Transepithelial calcium transport has been investigated in rat cecum under in vitro voltage-clamp conditions. Under short-circuit conditions, the cecum behaves as a relatively tight epithelium for calcium fluxes, where mucosal-to-serosal (JCam leads to s) flux exceeds the reverse flux by at least 15-fold. JCanet is abolished in the presence of 1 mM N-ethylmaleimide, is inhibited by 40% with 1 mM ouabain, and is decreased by at least 60% when medium sodium is replaced by choline. Voltage-clamping experiments suggest that both electroneutral- and electrogenic-mediated calcium fluxes traverse the cell in the mucosal-to-serosal direction. Serosal-to-mucosal flux is purely diffusional and probably constrained to the paracellular pathway. In rats weighing less than 175 g, a low-calcium diet has no significant stimulatory effect on JCam leads to s, but a high-calcium diet markedly reduces this flux. These results suggest that the cecum possesses the highest density of calcium transport sites in the rat intestine and is ideally suited for bulk calcium absorption, which may be “down regulated” in response to an increased calcium load in growing animals.

scholarly journals ApoE4 (Δ272–299) induces mitochondrial‐associated membrane formation and mitochondrial impairment by enhancing GRP75-modulated mitochondrial calcium overload in neuron

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tao Liang ◽  
Weijian Hang ◽  
Jiehui Chen ◽  
Yue Wu ◽  
Bin Wen ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Er Stress ◽  
Mitochondrial Dysfunction ◽  
Mitochondrial Function ◽  
Calcium Transport ◽  
Calcium Overload ◽  
Mitochondrial Calcium ◽  
Mitochondrial Impairment

Abstract Background Apolipoprotein E4 (apoE4) is a major genetic risk factor of Alzheimer’s disease. Its C-terminal-truncated apoE4 (Δ272–299) has neurotoxicity by affecting mitochondrial respiratory function. However, the molecular mechanism(s) underlying the action of apoE4 (Δ272–299) in mitochondrial function remain poorly understood. Methods The impact of neuronal apoE4 (Δ272–299) expression on ER stress, mitochondrial-associated membrane (MAM) formation, GRP75, calcium transport and mitochondrial impairment was determined in vivo and in vitro. Furthermore, the importance of ER stress or GRP75 activity in the apoE4 (Δ272–299)-promoted mitochondrial dysfunction in neuron was investigated. Results Neuronal apoE4 (Δ272–299) expression induced mitochondrial impairment by inducing ER stress and mitochondrial-associated membrane (MAM) formation in vivo and in vitro. Furthermore, apoE4 (Δ272–299) expression promoted GRP75 expression, mitochondrial dysfunction and calcium transport into the mitochondria in neuron, which were significantly mitigated by treatment with PBA (an inhibitor of ER stress), MKT077 (a specific GRP75 inhibitor) or GRP75 silencing. Conclusions ApoE4 (Δ272–299) significantly impaired neuron mitochondrial function by triggering ER stress, up-regulating GRP75 expression to increase MAM formation, and mitochondrial calcium overload. Our findings may provide new insights into the neurotoxicity of apoE4 (Δ272–299) against mitochondrial function and uncover new therapeutic targets for the intervention of Alzheimer’s disease.

scholarly journals New inhibitors of glucosylceramide synthase and their effect on cell fate

2014 ◽  
Vol 7 (2) ◽  
pp. 99-104 ◽  
Author(s):  
Katarína Turáková ◽  
Boris Lakatoš ◽  
Andrej Ďuriš ◽  
Daniela Moravčíková ◽  
Dušan Berkeš
Keyword(s):  
Cell Viability ◽  
Cell Fate ◽  
Calcium Transport ◽  
Large Scale ◽  
Process Development ◽  
Pharmaceutical Research ◽  
Pathological Process ◽  
Uridine Diphosphate ◽  
Induction Of Apoptosis

Abstract Glucosylceramide (GlcCer) is an essential glycosylated lipid found in organisms ranging from fungi to mammals. It is composed of a hydrophilic β-linked glucose and a hydrophobic ceramide, with a predominant content of sphingosine in mammals (d18:1). GlcCer is the precursor of a large scale of different glycosphingolipids. This cerebrozide is synthesized from uridine diphosphate-glucose and ceramide by a GlcCer synthase (UDP-glucose:ceramide glucosyltransferase; UGCG, EC 2.4.1.80). GlcCer-based sphingolipids have been identified as important mediators of a variety of cellular functions and their disequilibrium leads to pathological process development and may induce several diseases progression. Therefore, design of UGCG inhibitor represents an important topic for pharmaceutical research. In this paper, we aimed to study effects of newly synthesized derivatives of (±)-threo-1-phenyl-2-palmitoylamino-3-morpholino-1-propanol (PPMP, known UGCG inhibitor) on: i) activity of UGCG in vitro; ii) thymocytes viability; iii) calcium transport through plasma membrane of thymocytes; iv) induction of apoptosis and autophagy in thymocytes. Thymocytes were isolated from thymus of three to seven weeks old mice (ICR strain). The key factors influencing the effect of PPMP analogues were their concentration, chemical structure and incubation time. Derivatives were able to change Ca2+ transport already after 15 min of cultivation, but their effects on cell viability were manifested at least after 12 h of cultivation. Four from fifteen studied compounds affected UGCG activity after four hour lasting cultivation, - but without correlation with data relating to effects on calcium transport and/or cell viability. Most potent UGCG inhibitor was chosen and applied for induction of apoptosis and autophagy in thymocytes. This inhibitor induced typical DNA fragmentation and upregulation of LC3B protein as autophagy marker, after 2 h and 4 h cultivation, respectively.

Brush border myosin-I microinjected into cultured cells is targeted to actin-containing surface structures

1994 ◽  
Vol 107 (6) ◽  
pp. 1623-1631 ◽  
Author(s):  
M. Footer ◽  
A. Bretscher
Keyword(s):  
Plasma Membrane ◽  
Brush Border ◽  
Actin Filaments ◽  
Cultured Cells ◽  
Surface Structures ◽  
Specific Expression ◽  
Cultured Fibroblasts ◽  
Myosin I ◽  
Section Electron

The isolated intestinal microvillus cytoskeleton (core) consists of four major proteins: actin, villin, fimbrin and brush border myosin-I. These proteins can assemble in vitro into structures resembling native microvillus cores. Of these components, villin and brush border myosin-I show tissue-specific expression, so they may be involved in the morphogenesis of intestinal microvilli. When introduced into cultured cells that normally lack the protein, villin induces a reorganization of the actin filaments to generate large surface microvilli. Here we examine the consequences of microinjecting brush border myosin-I either alone or together with villin into cultured fibroblasts. Injection of brush border myosin-I has no discernible effect on the overall morphology of the cells, but does become localized to either normal or villin-induced microvilli and other surface structures containing an actin cytoskeleton. Since some endogenous myosin-Is have been found associated with cytoplasmic vesicles, these results show that brush border myosin-I has a domain that specifically targets it to the plasma membrane in both intestinal and cultured cell systems. Ultrastructural examination of microvilli on control cultured cells revealed that they contain a far more highly ordered bundle of microfilaments than had been previously appreciated. The actin filaments in microvilli of villin-injected cells appeared to be more tightly cross-linked when examined by thin-section electron microscopy. In intestinal microvilli, the core bundle is separated from the plasma membrane by about 30 nm due to the presence of brush border myosin-I.(ABSTRACT TRUNCATED AT 250 WORDS)

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