Immunochemical Demonstration of a Novel β-Subunit Isoform of X,K-ATPase in Human Skeletal Muscle

Pestov, Nikolay B.; Korneenko, Tatyana V.; Zhao, Hao; Adams, Gail; Shakhparonov, M. I.; Modyanov, Nikolaï N.

doi:10.1006/bbrc.2000.3692

Cited by 13 publications

(37 citation statements)

References 21 publications

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“…This allowed identification of two alternatively spliced forms of the mouse ␤ m transcript (GenBank accession nos. AF348324 and AF348325), one of them lacking 12 bp within the ORF, similar to that previously demonstrated in human, rat, and pig muscles (36,39,40). The first translation product (variant A) consists of 356 amino acid residues and has a molecular mass of 41.4 kDa (Fig.…”

Section: Resultssupporting

confidence: 78%

“…Immunization and affinity purification of rabbit polyclonal antibodies against human ␤m lacking transmembrane region were described previously (40). Similarly, this rabbit serum was subsequently used to isolate antibodies against mouse COOH-terminal ectodomain by affinity purification.…”

Section: Animals and Tissuesmentioning

confidence: 99%

“…This protein shares typical X,K-ATPase ␤-subunit features including the overall domain disposition and possesses all conserved sequence motifs. However, only ␤ m possesses a very acidic NH 2 terminus and short high-mannose or hybrid N-glycans (40), whereas mature forms of other ␤s always have complex-type glycans (4,20,44). This glycosylation pattern suggested the subcellular location of ␤ m in an intracellular compartment, and not the plasma membrane as is normally the case for various X,KATPases (4,20).…”

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confidence: 99%

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Accumulation of β_m, a structural member of X,K-ATPase β-subunit family, in nuclear envelopes of perinatal myocytes

Zhao

Pestov²,

Korneenko³

et al. 2004

American Journal of Physiology-Cell Physiology

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Zhao, Hao, Nikolay B. Pestov, Tatyana V. Korneenko, Mikhail I. Shakhparonov, and Nikolai N. Modyanov. Accumulation of ␤ m, a structural member of X,K-ATPase ␤-subunit family, in nuclear envelopes of perinatal myocytes. Am J Physiol Cell Physiol 286: C757-C767, 2004. First published December 3, 2003 10.1152/ ajpcell.00358.2003.-Recently discovered muscle-specific ␤ m protein is structurally closely related to the X,K-ATPase ␤-subunits. However, it has a number of unique properties such as predominant localization in intracellular stores and lack of association with known X,K-ATPase ␣-subunits on heterologous coexpression. In this study, the primary structure of mouse ␤ m was determined and developmental regulation of the gene (ATP1B4) was analyzed. The expression is first detected at day 14 of gestation, is sharply increased at day 16, and reaches its maximum at day 18. After birth, the expression quickly decreases and is hardly detectable in adult mice. A more detailed subcellular localization study was undertaken, and its results indicate that ␤ m not only is located in sarcoplasmic reticulum but is concentrated in nuclear envelopes of both prenatal and postnatal skeletal muscles. Immunohistochemical studies show that ␤ m is specific to myocytes and, at the subcellular level, many nuclear envelopes are intensively labeled in both fetal and newborn skeletal muscles. Accordingly, ␤ m is detected by immunoblotting in purified nuclei and nuclear membranes from neonatal skeletal muscles. On transfection of human rhabdomyosarcoma cell line RD, green fluorescent proteintagged ␤ m resides intracellularly with significant enrichment in nuclear envelopes, whereas ␤ m with transmembrane domain deleted localizes in both cytoplasm and nucleoplasm. Nuclear ␤ m apparently is not in association with Na,K-ATPase because we never detected its ␣-subunit in myonuclear membranes. These results indicate that ␤ m has a specialized function in mammalian perinatal myocytes, different from functions of other X,K-ATPase ␤-subunits. The unique temporospatial distribution of ␤ m protein expression suggests its important role in development of growing skeletal muscle.ATP1B4; sodium, potassium-adenosine 5Ј-triphosphatase; nuclear membrane; skeletal muscle development AMONG MORE THAN 200 P-ATPases identified in prokaryotes and eukaryotes (1), most enzymes have just a single catalytic subunit. However, the animal X,K-ATPases (Na,K-ATPase, gastric H,K-ATPase, and nongastric H,K-ATPase) contain, in addition to the catalytic ␣-subunit, an accessory ␤-subunit. Although major functions such as ATP binding, phosphorylation, and ion transport are performed by the ␣-subunit, the ␣-␤ interaction is required for maturation, stability, and translocation of the ATPases to plasma membrane (4, 44). Moreover, the ␤-subunit seems to be related to K transport, the unique feature of the X,K-ATPase family members (16, 45). The ␤-subunit is involved in K affinity and cardiac glycoside sensitivity (25, 45). Different ␣-and ␤-isoform combinations exhibit functiona...

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Section: Resultssupporting

confidence: 78%

Section: Animals and Tissuesmentioning

confidence: 99%

mentioning

confidence: 99%

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Accumulation of β_m, a structural member of X,K-ATPase β-subunit family, in nuclear envelopes of perinatal myocytes

Zhao

Pestov²,

Korneenko³

et al. 2004

American Journal of Physiology-Cell Physiology

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“…Despite the similarities with X-K-ATPase ␤-isoforms, ␤ m has also some atypical characteristics. First, it contains two long glutamate-rich regions in the cytoplasmic NH 2 terminus that are not present in X-K-ATPase ␤-subunits (357). Second, based on results of cell fractionation (356) and on its state of glycosylation (357), ␤ m appears to be concentrated in the sarcoplasmic reticulum; in contrast, X-K-ATPase ␤-subunits are predominantly found at the plasma membrane.…”

Section: ␤-Subunit Isoformsmentioning

confidence: 99%

“…First, it contains two long glutamate-rich regions in the cytoplasmic NH 2 terminus that are not present in X-K-ATPase ␤-subunits (357). Second, based on results of cell fractionation (356) and on its state of glycosylation (357), ␤ m appears to be concentrated in the sarcoplasmic reticulum; in contrast, X-K-ATPase ␤-subunits are predominantly found at the plasma membrane. Recent studies reveal that ␤ m is a resident of the endoplasmic reticulum, which does not act as a chaperone for the maturation of any of the known X-K-ATPase ␤-subunits, thus representing a protein functionally distinct from other members of the ␤-subunit family (108).…”

Section: ␤-Subunit Isoformsmentioning

confidence: 99%

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

Cereijido

Contreras

Shoshani

2004

Physiological Reviews

151

100

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Transporting epithelia posed formidable conundrums right from the moment that Du Bois Raymond discovered their asymmetric behavior, a century and a half ago. It took a century and a half to start unraveling the mechanisms of occluding junctions and polarity, but we now face another puzzle: lest its cells died in minutes, the first high metazoa (i.e., higher than a sponge) needed a transporting epithelium, but a transporting epithelium is an incredibly improbable combination of occluding junctions and cell polarity. How could these coincide in the same individual organism and within minutes? We review occluding junctions (tight and septate) as well as the polarized distribution of Na+-K+-ATPase both at the molecular and the cell level. Junctions and polarity depend on hosts of molecular species and cellular processes, which are briefly reviewed whenever they are suspected to have played a role in the dawn of epithelia and metazoan. We come to the conclusion that most of the molecules needed were already present in early protozoan and discuss a few plausible alternatives to solve the riddle described above.

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The βm Protein, a Member of the X,K-ATPase β-Subunits Family, Is Located Intracellularly in Pig Skeletal Muscle

Pestov

Korneenko

Zhao

et al. 2001

Archives of Biochemistry and Biophysics

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Immunochemical Demonstration of a Novel β-Subunit Isoform of X,K-ATPase in Human Skeletal Muscle

Cited by 13 publications

References 21 publications

Accumulation of β_m, a structural member of X,K-ATPase β-subunit family, in nuclear envelopes of perinatal myocytes

Accumulation of β_m, a structural member of X,K-ATPase β-subunit family, in nuclear envelopes of perinatal myocytes

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

The βm Protein, a Member of the X,K-ATPase β-Subunits Family, Is Located Intracellularly in Pig Skeletal Muscle

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Immunochemical Demonstration of a Novel β-Subunit Isoform of X,K-ATPase in Human Skeletal Muscle

Cited by 13 publications

References 21 publications

Accumulation of βm, a structural member of X,K-ATPase β-subunit family, in nuclear envelopes of perinatal myocytes

Accumulation of βm, a structural member of X,K-ATPase β-subunit family, in nuclear envelopes of perinatal myocytes

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

The βm Protein, a Member of the X,K-ATPase β-Subunits Family, Is Located Intracellularly in Pig Skeletal Muscle

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Accumulation of β_m, a structural member of X,K-ATPase β-subunit family, in nuclear envelopes of perinatal myocytes

Accumulation of β_m, a structural member of X,K-ATPase β-subunit family, in nuclear envelopes of perinatal myocytes