The fodrin-ankyrin cytoskeleton of choroid plexus preferentially colocalizes with apical Na+K(+)-ATPase rather than with basolateral anion exchanger AE2.

Alper, Seth L.; Stuart-Tilley, Alan K.; Simmons, Charles F.; Brown, Dennis; Drenckhahn, Detlev

doi:10.1172/jci117120

Cited by 111 publications

(78 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The tendency of ProSAP1 to accumulate in apical domains of epithelium-type cells is further underlined by its distribution pattern in the choroid plexus epithelium. Thus, ProSAP1 is preferentially localized beneath the apical cell surface of this epithelium where the actin/spectrin-based cytoskeleton is known to be concentrated (Alper et al 1994).…”

Section: Discussionmentioning

confidence: 91%

The Cortactin-binding Postsynaptic Density Protein ProSAP1 in Non-neuronal Cells

Redecker

Gundelfinger²,

Boeckers³

2001

J Histochem Cytochem.

View full text Add to dashboard Cite

(TMB) S U M M A R Y Proline-rich synapse-associated protein-1 (ProSAP1) is a neuronal PDZ domain-containing protein that has recently been identified as an essential element of the postsynaptic density. Via its interaction with the actin-binding protein cortactin and its integrative function in the organization of neurotransmitter receptors, ProSAP1 is believed to be involved in the linkage of the postsynaptic signaling machinery to the actin-based cytoskeleton, and may play a role in the cytoskeletal rearrangements that underlie synaptic plasticity. As a result of our ongoing studies on the distribution and function of this novel PDZ domain protein, we now report that the expression of ProSAP1 is restricted neither to neurons and interneuronal junctions nor to the nervous system. Using immunohistochemical techniques in conjunction with specific antibodies, we found that, in the CNS, ProSAP1 can be detected in certain glial cells, such as ependymal cells, tanycytes, subpial/radial astrocytes, and in the choroid plexus epithelium. Moreover, our immunohistochemical analyses revealed the presence of ProSAP1 in endocrine cells of the adenohypophysis and of the pancreas, as well as in non-neuronal cell types of other organs. In the pancreas, ProSAP1 immunoreactivity was also localized in the duct system of the exocrine parenchyma. Our findings demonstrate that, in addition to neurons, ProSAP1 is present in various non-neuronal cells, in which it may play a crucial role in the dynamics of the actin-based cytoskeleton.

show abstract

Section: Discussionmentioning

confidence: 91%

The Cortactin-binding Postsynaptic Density Protein ProSAP1 in Non-neuronal Cells

Redecker

Gundelfinger²,

Boeckers³

2001

J Histochem Cytochem.

View full text Add to dashboard Cite

show abstract

“…mAE2 is acutely and independently regulated by pH i and extracellular pH (52), NH 4 ϩ , and hypertonicity (16). We therefore examined zebrafish Ae2 for similar types of acute regulation.…”

Section: Resultsmentioning

confidence: 99%

“…After being washed, sections were incubated for 45 min with secondary fluorophor-coupled anti-Ig. Mouse monoclonal antibody to chicken Na ϩ -K ϩ -ATPase was previously described (4). FITC-coupled wheat germ agglutinin was from Vector Laboratories (Burlingame, CA).…”

Section: Measurement Of CLmentioning

confidence: 99%

Zebrafishslc4a2/ae2anion exchanger: cDNA cloning, mapping, functional characterization, and localization

Shmukler

Kurschat

Ackermann

et al. 2005

American Journal of Physiology-Renal Physiology

View full text Add to dashboard Cite

Although the zebrafish has been used increasingly for the study of pronephric kidney development, studies of renal ion transporters and channels of the zebrafish remain few. We report the cDNA cloning and characterization of the AE2 anion exchanger ortholog from zebrafish kidney, slc4a2/ae2. The ae2 gene in linkage group 2 encodes a polypeptide of 1,228 aa exhibiting 64% aa identity with mouse AE2a. The exonintron boundaries of the zebrafish ae2 gene are nearly identical to those of the rodent and human genes. Whole-mount in situ hybridization detects ae2 mRNA in prospective midbrain as early as the five-somite stage, then later in the pronephric primordia and the forming pronephric duct, where it persists through 72 h postfertilization (hpf). Zebrafish Ae2 expressed in Xenopus laevis oocytes mediates Na ϩ -independent, electroneutral 36 Cl Ϫ /Cl Ϫ exchange moderately sensitive to inhibition by DIDS, is inhibited by acidic intracellular pH and by acidic extracellular pH, but activated by (acidifying) ammonium and by hypertonicity. Zebrafish Ae2 also mediates Cl Ϫ /HCO 3 Ϫ exchange in X. laevis oocytes and accumulates in or near the plasma membrane in transfected HEK-293 cells. In 24 -48 hpf zebrafish embryos, the predominant but not exclusive localization of Ae2 polypeptide is the apical membrane of pronephric duct epithelial cells. Thus Ae2 resembles its mammalian orthologs in function, mechanism, and acute regulation but differs in its preferentially apical expression in kidney. These results will inform tests of the role of Ae2 in zebrafish kidney development and function.AE2; chloride/bicarbonate exchanger CHLORIDE/BICARBONATE EXCHANGERS of the SLC4 and SLC26 gene superfamilies control intracellular pH (pH i ), cell volume, and intracellular Cl Ϫ concentration ([Cl Ϫ ]) in most body tissues (1, 37, 45). As pH regulators, they serve in basolateral HCO 3 Ϫ extrusion, contributing to epithelial acid secretion, or in apical HCO 3 Ϫ extrusion, contributing to epithelial HCO 3 Ϫ secretion. As volume regulators, they serve in basolateral Cl

show abstract

“…However, the fulllength AE1 protein in mammals is normally restricted to erythroid cells, and the truncated form lacking the N-terminal 69 residues is found in the kidney (kAE1). The N-terminus of eAE1 interacts with many proteins, including ankyrin, protein 4.1 and glycolytic enzymes (Alper et al, 1994), whereas the N-terminus of kAE1 does not bind to these proteins (Wang et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Induction of anion exchanger-1 translation and its opposite roles in the carcinogenesis of gastric cancer cells and differentiation of K562 cells

Zhang

et al. 2010

Oncogene

View full text Add to dashboard Cite

Anion exchanger-1 (AE1), an erythroid-specific membrane protein, mediates the Cl À /HCO À 3 exchange across the plasma membrane and regulates intracellular pH. We have found that AE1 was unexpectedly expressed in gastric cancer cells and participated in the tumorigenesis of the cancer. Here, we focus on the induction of AE1 expression and its role in gastric carcinogenesis as well as in the differentiation of K562 cells. The results show that expression of AE1 is not related to genetic mutation or the mRNA level, but rather, that it is modulated by miR-24. miR-24 decreases the expression of AE1 through binding to the 3 0 UTR of AE1 mRNA. Transfection of an miR-24 into gastric cancer cells reduced the elevation of the AE1 protein, which resulted in return of AE1-sequestrated p16 to the nucleus, thereby inhibiting proliferation of the cells. Furthermore, the miR-24 inhibitor cooperated with hemin to induce the expression of AE1 in K562 cells and differentiation of the cells, which is consistent with results obtained from the cells cultured at pH 7.6 or from forced stable expression of AE1. These findings establish a novel regulation of miR-24-related AE1 expression in gastric carcinogenesis and erythropoiesis.

show abstract

The fodrin-ankyrin cytoskeleton of choroid plexus preferentially colocalizes with apical Na+K(+)-ATPase rather than with basolateral anion exchanger AE2.

Cited by 111 publications

References 46 publications

The Cortactin-binding Postsynaptic Density Protein ProSAP1 in Non-neuronal Cells

The Cortactin-binding Postsynaptic Density Protein ProSAP1 in Non-neuronal Cells

Zebrafishslc4a2/ae2anion exchanger: cDNA cloning, mapping, functional characterization, and localization

Induction of anion exchanger-1 translation and its opposite roles in the carcinogenesis of gastric cancer cells and differentiation of K562 cells

Contact Info

Product

Resources

About