Spectrin: Present status of a putative cyto-skeletal protein of the red cell membrane

Marchesi, V.

doi:10.1007/bf01869164

Cited by 96 publications

(22 citation statements)

References 71 publications

(67 reference statements)

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“…The proteins that make up the membrane skeleton of the human erythrocyte have been studied in some detail (3)(4)(5)(6). The principal components are spectrin and an erythrocyte form of actin (7).…”

Section: Introductionmentioning

confidence: 99%

Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis.

Knowles¹,

Morrow²,

Speicher³

et al. 1983

J. Clin. Invest.

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A B S T R A C T The structural and functional properties of spectrin from normal and hereditary pyropoikilocytosis (HPP) donors from the two unrelated families were studied. The structural domains of the spectrin molecule were generated by mild tryptic digestion and analyzed by two-dimensional electrophoresis (isoelectric focusing; sodium dodecyl sulfate-polyacrylamide gel electrophoresis). The aI-T80 peptide (Mr 80,000) is not detectable in two related HPP donors; instead, two new peptides (Mr 50,000 and 21,000) are generated and have been identified as fragments of the normal aI-T80. A third sibling has reduced levels of both the normal aI-T80 and the two new peptides.A similar analysis of spectrin from another HPP family indicates that their spectrins contain reduced amounts of the aI-T80 and the 50,000 and 21,000 fragments of the aI domain. The HPP donor also has other structural variations in the al, aIl, and alII domains.The aI-T80 domain of normal spectrin has been shown to be an important site for spectrin oligomerization (J. Morrow and V. T. Marchesi. 1981. J. Cell Biol. 88: 463-468), and in vitro assays indicate that HPP spectrin has an impaired ability to oligomerize. Ghost membranes from HPP donors are also more fragile than membranes from normal erythrocytes when measured by ektacytometry. In both the oligomerization and fragility assays, the degree of impairment is correlated with the amount of normal aI-T80 present in the spectrin molecule.A preliminary report of this work was presented at an ICN/UCLA Symposium, Keystone, CO, 18 February 1981.

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Section: Introductionmentioning

confidence: 99%

Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis.

Knowles¹,

Morrow²,

Speicher³

et al. 1983

J. Clin. Invest.

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“…In mammalian erythrocytes, actin is attached to the plasma membrane through a high molecular weight protein, spectrin, which is found on the inner surface of the plasma membrane: it is composed of two nonidentical subunit polypeptides herein termed "a-spectrin" (Mr 240,000) and "/-spectrin" (Mr 220,000) (for reviews, see refs. [5][6][7]. Spectrin forms a crosslinked network with actin filaments (8,9) and is linked to the membrane through the association of the 8 subunit with ankyrin (10,11).…”

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confidence: 99%

Expression of the beta subunit of spectrin in nonerythroid cells.

Nelson¹,

Lazarides²

1983

Proc. Natl. Acad. Sci. U.S.A.

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Antibodies raised against electrophoretically purified chicken erythrocyte fi subunit of spectrin, called "1-spectrin," have been used to demonstrate the presence of an immunoreactive form of this polypeptide in nonerythroid tissues. Immunoautoradiography shows that, in chicken erythrocytes, this antiserum reacts with P-spectrin (Mr 220,000) and another polypeptide (Mr 230,000) that, by two-dimensional tryptic peptide analysis, shows extensive homology with P-spectrin but not with the a subunit of spectrin, called "e-spectrin." Immunoautoradiography and immunoprecipitation of various chicken tissues with this antiserum shows that either one variant or both variants of f-spectrin are expressed. Indirect immunofluorescence reveals that the antiserum reacts with a plasma membrane-associated component of erythroid and some nonerythroid cells. Particularly strong fluorescence is observed in skeletal and cardiac muscle cells where (3-spectrin appears to form a grid-like network along the inner surface ofthe sarcolemma. The noncoordinated distribution of a-and (-spectrin variants indicates that their expression may be tailored to the functional requirements of the plasma membrane in different cells.The fluid mosaic model for membranes, which was developed from early studies on the erythrocyte membrane (1, 2), has been extended to include the notion that the lateral mobility of proteins in the plane ofthe membrane is restricted by interactions between these proteins and the cytoskeleton (3, 4). The nature of these interactions remains, to a great extent, an unresolved problem despite the fact that several membrane-associated proteins have been implicated in this process. In mammalian erythrocytes, actin is attached to the plasma membrane through a high molecular weight protein, spectrin, which is found on the inner surface of the plasma membrane: it is composed of two nonidentical subunit polypeptides herein termed "a-spectrin" (Mr 240,000) and "/-spectrin" (Mr 220,000) (for reviews, see refs. 5-7). Spectrin forms a crosslinked network with actin filaments (8,9) and is linked to the membrane through the association of the 8 subunit with ankyrin (10, 11). Ankyrin associates with the membrane by binding to a subset of the transmembrane anion transporters (5, 7). Thus, in the erythrocyte, spectrin appears to play a pivotal role in linking the plasma membrane to the cytoskeleton and in restricting the mobility of certain transmembrane polypeptides. In the past, the failure to detect immunoreactive forms of spectrin in nonerythroid tissues (12, 13) has limited generalizations regarding the role of spectrin in the highly specialized erythrocyte. Recently, however, several laboratories have identified a spectrinlike protein in nonerythroid cells (14)(15)(16)(17)(18)(19)(20); the protein shows several biochemical properties common with a-spectrin from erythrocytes (18)(19)(20) (24), and their proteins were separated by NaDodSO4/10% or 12.5% polyacrylamide gel electrophoresis based on the system of Laemmli (25) as modi...

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“…It is reasonably proposed that the erythrocyte cytoskeleton may play an important role in regulating the topography of intramembranous proteins (11,12,29,31,38) and in determining erythrocyte shape and deformity (4,16,27,35). In search of the supramolecular organization of the cytoskeleton, extensive studies have recently been directed to the structure (18,33,39) and chemical nature of spectrin (15,24,25,41), including its binding with other proteins, such as erythrocyte actin, band 2 .1, and band 4 .1 (2,14,22,45,47,49) . Although the erythrocyte actin accompanied spectrin during extraction with low-salt EDTA, 70 SACHIKO TSUKITA, SHOICHIRO TSUKITA, HARUNORI ISHIKAWA, SHINGO SATO, and MAKOTO NAKAO…”

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confidence: 99%

Electron microscope study of reassociation of spectrin and actin with the human erythrocyte membrane

Tsukita¹,

Ishikawa²,

Sato³

et al. 1981

The Journal of Cell Biology

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Reassociation of spectrin and actin with human erythrocyte membranes was studied by stereoscopic electron microscopy of thin sections combined with tannic acid-glutaraldehyde fixation . Treatment of the erythrocyte membrane with 0.1 mM EDTA (pH 8.0) extracted >90% of the spectrin and actin and concomitantly removed filamentous meshworks underlying the membranes, followed by fragmentation into small inside-out vesicles . When such spectrindepleted vesicles were incubated with the EDTA extract (crude spectrin), a filamentous meshwork, similar to those of the original membranes, was reformed on the cytoplasmic surface of the vesicles . The filamentous components, with a uniform thickness of 9 nm, took a tortuous course and joined one another often in an end-to-end fashion to form an irregular but continuous meshwork parallel to the membrane . Purified spectrin was also reassociated with the vesicles in a population density of filamentous components almost comparable to that of the crude spectrin-reassociated vesicles . However, the meshwork formation was much smaller in extent, showing many independent filamentous components closely applied to the vesicle surface. When muscle G-actin was added to the crude spectrin-or purified spectrinreassociated vesicles under conditions which favor actin polymerization, actin filaments were seen to attach to the vesicles through the filamentous components . Two modes of association of actin filaments with the membrane were seen : end-to-membrane and side-to-membrane associations . In the end-to-membrane association, each actin filament was bound with several filamentous components exhibiting a spiderlike configuration, which was considered to be the unit of the filamentous meshwork of the original erythrocyte membrane .The existence of the cytoskeletal network underlying the erythrocyte membrane is now well documented (for reviews, see references 23, 25, 42). Evidence has accumulated that the erythrocyte cytoskeleton is mainly constituted of spectrin, the major peripheral membrane protein (28,47,48) . It is reasonably proposed that the erythrocyte cytoskeleton may play an important role in regulating the topography of intramembranous proteins (11,12,29,31,38) and in determining erythrocyte shape and deformity (4,16,27,35). In search of the supramolecular organization of the cytoskeleton, extensive studies have recently been directed to the structure (18,33,39) and chemical nature of spectrin (15,24,25,41), including its binding with other proteins, such as erythrocyte actin, band 2 .1, and band 4 .1 (2,14,22,45,47,49) . Although the erythrocyte actin accompanied spectrin during extraction with low-salt EDTA, 70 SACHIKO TSUKITA, SHOICHIRO TSUKITA, HARUNORI ISHIKAWA, SHINGO SATO, and MAKOTO NAKAO

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Spectrin: Present status of a putative cyto-skeletal protein of the red cell membrane

Cited by 96 publications

References 71 publications

Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis.

Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis.

Expression of the beta subunit of spectrin in nonerythroid cells.

Electron microscope study of reassociation of spectrin and actin with the human erythrocyte membrane

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