Mat-8, a Novel Phospholemman-like Protein Expressed in Human Breast Tumors, Induces a Chloride Conductance in Xenopus Oocytes

Morrison, Briggs W.; Moorman, J. Randall; Kowdley, Gopal C.; Kobayashi, Yvonne M.; Jones, Larry R.; Leder, Philip

doi:10.1074/jbc.270.5.2176

Cited by 140 publications

(124 citation statements)

References 26 publications

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“…Cloning and Sequencing-First strand cDNA synthesis was carried out in a total reaction volume of 20 l containing 5 g of total rectal gland RNA, 75 mM Tris-HCl, pH 8.3, 3 mM MgCl 2 , 10 mM DTT, 10 M oligo(dT) [12][13][14][15][16][17][18] , 1 mM each of deoxyribonucleotide triphosphates (dNTPs; dATP, dGTP, dCTP, and dTTP), and 200 units of Superscript II (Invitrogen, Paisley, UK). The reaction was incubated at 45°C for 2 h and then stored frozen at Ϫ20°C for use in PCR.…”

Section: Methodsmentioning

confidence: 99%

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Regulation of Na,K-ATPase by PLMS, the Phospholemman-like Protein from Shark

Mahmmoud

Cramb

Maunsbach

et al. 2003

Journal of Biological Chemistry

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In Na,K-ATPase membrane preparations from shark rectal glands, we have previously identified an FXYD domain-containing protein, phospholemman-like protein from shark, PLMS. This protein was shown to associate and modulate shark Na,K-ATPase activity in vitro. Here we describe the complete coding sequence, expression, and cellular localization of PLMS in the rectal gland of the shark Squalus acanthias. The mature protein contained 74 amino acids, including the N-terminal FXYD motif and a C-terminal protein kinase multisite phosphorylation motif. The sequence is preceded by a 20 amino acid candidate cleavable signal sequence. Immunogold labeling of the Na,K-ATPase ␣-subunit and PLMS showed the presence of ␣ and PLMS in the basolateral membranes of the rectal gland cells and suggested their partial colocalization. Furthermore, through controlled proteolysis, the C terminus of PLMS containing the protein kinase phosphorylation domain can be specifically cleaved. Removal of this domain resulted in stimulation of maximal Na,K-ATPase activity, as well as several partial reactions. Both the E 1 ϳP 3 E 2 -P reaction, which is partially rate-limiting in shark, and the K ؉ deocclusion reaction, E 2 (K) 3 E 1 , are accelerated. The latter may explain the finding that the apparent Na ؉ affinity was increased by the specific C-terminal PLMS truncation. Thus, these data are consistent with a model where interaction of the phosphorylation domain of PLMS with the Na,K-ATPase ␣-subunit is important for the modulation of shark Na,K-ATPase activity.

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Section: Methodsmentioning

confidence: 99%

“…This family includes phospholemman (PLM or FXYD1) (14), the ␥-subunit (FXYD2) (15), mammary tumor protein of 8-kDa molecular mass (MAT-8 or FXYD3) (16), channel-inducing factor (CHIF or FXYD4) (17), related to ion channel (RIC or FYXD5) (18), as well as FXYD6 and FXYD7.…”

mentioning

confidence: 99%

Regulation of Na,K-ATPase by PLMS, the Phospholemman-like Protein from Shark

Mahmmoud

Cramb

Maunsbach

et al. 2003

Journal of Biological Chemistry

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“…Injecting large amounts of cDNA, in contrast, yielded anion currents with an iodide > chloride conductivity sequence which activated slowly upon strong hyperpolarization (in excess of-100 mV) (data not shown). However, similar currents are endogenous to Xenopus oocytes [25] and can also be provoked by overexpression of phospholemman [26], Mat-8 [27], minK (also named IsK [28]) [29] and mutants of C1C-1 which are closed in that voltagerange [19]. Thus, it seems that these currents are just an artifact of overexpressing membrane proteins in Xenopus oocytes [30].…”

Section: Clc-6 Clc-7mentioning

confidence: 99%

ClC‐6 and ClC‐7 are two novel broadly expressed members of the CLC chloride channel family

1995

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We cloned two novel members of the CLC chloride channel family from rat and human brain. CIC-6 is a 97-kDa protein, and CIC-7 a 89-kDa protein roughly 45% identical with CIC-6. Together they define a new branch of this gene family. Both genes are very broadly expressed, e.g. in brain, testes, muscle and kidney. In mouse embryos, both genes are expressed as early as day 7. While the human gene for CIC-6 is located on human chromosome lp36 and shares this region with hCIC-Ka and hCIC-Kb, CIC-7 is on 16p13. CIC-6 has a highly conserved glycosylation site between transmembrane domains D8 and D9, while CIC-7 is the only known eukaryotic CIC protein which lacks this site. Hydropathy analysis indicates that domain D4 cannot serve as a transmembrane domain. Both CIC-6 and CIC-7 cannot be expressed as chloride channels in Xenopus oocytes, either singly or in combination.

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“…Mat-8 is an 8-kd transmembrane protein homologous to phospholemman (Morrison et al, 1995). It is differentially expressed in the MCF-7 breast cancer cell line and in a progressive variant of MCF-7 (Schiemann et al, 1998).…”

Section: Differential Expression In Two Lncapmentioning

confidence: 99%

Differentially Expressed Genes in Two LNCaP Prostate Cancer Cell Lines Reflecting Changes during Prostate Cancer Progression

Vaarala

Porvari

Kyllönen

et al. 2000

Laboratory Investigation

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SUMMARY:Prostate cancer tends to become transformed to androgen-independent disease over time when treated by androgen-deprivation therapy. We used two variants of the human prostate cancer cell line LNCaP to study gene expression differences during prostate cancer progression to androgen-independent disease. Production of prostate-specific antigen was regarded as a marker of androgen-dependence and loss of prostate-specific antigen was regarded as a marker of androgenindependence. mRNA from both cell lines was used for cDNA microarray screening. Differential expression of several genes was confirmed by Northern blotting. Monoamine oxidase A, an Expressed Sequence Tag (EST) similar to rat P044, and EST AA412049 were highly overexpressed in androgen-dependent LNCaP cells. Tissue-type plasminogen activator, interferon-inducible protein p78 (MxB), an EST similar to galectin-1, follistatin, fatty acid-binding protein 5, EST AA609749, annexin I, the interferon-inducible gene 1-8U, and phospholipase D1 were highly overexpressed in androgen-independent LNCaP cells. All studied genes had low or no expression in PC-3 cells. The EST similar to rat P044, the EST similar to galectin-1, follistatin, annexin I, and the interferon-inducible gene 1-8U were also expressed in benign prostatic hyperplasia tissue. The Y-linked ribosomal protein S4, Mat-8, and EST AA307912 were highly expressed in benign prostatic hyperplasia tissue. Additionally, both confirmation of differential expression in Northern blots and in situ hybridization were carried out for monoamine oxidase A, the EST similar to rat P044, the EST similar to galectin-1, fatty acid-binding protein 5, and the interferon-inducible gene 1-8U. We identified several potential prostate cancer markers, indicating that the method used is a useful tool for the screening of cancer markers, but other methods, such as in situ hybridization, are needed to further investigate the observations. (Lab Invest 2000, 80:1259-1268.

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Mat-8, a Novel Phospholemman-like Protein Expressed in Human Breast Tumors, Induces a Chloride Conductance in Xenopus Oocytes

Cited by 140 publications

References 26 publications

Regulation of Na,K-ATPase by PLMS, the Phospholemman-like Protein from Shark

Regulation of Na,K-ATPase by PLMS, the Phospholemman-like Protein from Shark

ClC‐6 and ClC‐7 are two novel broadly expressed members of the CLC chloride channel family

Differentially Expressed Genes in Two LNCaP Prostate Cancer Cell Lines Reflecting Changes during Prostate Cancer Progression

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