Spectrin and Related Molecule

Goodman, Steven R.; Krebs, Keith E.; Whitfield, Carol F.; Riederer, Beat M.; Zagon, Ian S.

doi:10.3109/10409238809088319

Cited by 149 publications

(83 citation statements)

References 341 publications

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“…Yet the structural and functional domains of erythroid and nonerythroid spectrins are highly conserved between mouse and human: a long repeat domain, an actin-binding domain (N-terminal domain), and a C-terminal regulatory domain. This may account for the observed di erence in spectrin tetramer formation and stability between erythroid and nonerythroid subunits (Goodman et al, 1988). The highly conserved molecular structure of known nonerythroid b-spectrins across species indicates that elf may have evolved from a common ancestral gene and has similar biological functions.…”

Section: Discussionmentioning

confidence: 99%

Elf3 encodes a novel 200-kD β-spectrin: role in liver development

et al. 1999

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b-spectrins are crucial for the maintenance of cell shape, the establishment of cell polarity, and the formation of distinct membrane domains. Our strategy for identifying genes important for hepatocyte polarity has been to utilize subtractive hybridization of early embryonic mouse cDNA liver libraries. As a result, we have cloned three isoforms of a novel b-spectrin elf (embryonic liver b-fodrin), and here we report the analysis of elf3, the longest isoform (8172 nt). ELF3 comprises 2154 residues with an overall similarity of 89.0% and 95.3% to mouse b-spectrin (bSpIIS1) at the nucleotide and amino acid level, respectively. ELF3 is characterized by an actinbinding domain, a long repeat domain, and a short regulatory domain remarkable for the absence of a PH domain. Linkage analysis reveals that elf3 maps to mouse chromosome 11 between D11Bir6 and D11Xrf477, a di erent chromosomal locus from that of the other four spectrin genes. Northern blot analysis utilizing an elf3 3'-UTR probe demonstrates an abundant 9.0-kb transcript in brain, liver, and heart tissues. Western blot with a polyclonal antibody against ELF identi®es a 200 kD protein in mouse liver, brain, kidney, and heart tissues. Immunohistochemical studies demonstrate ELF labeling of the basolateral or sinusoidal membranes surface as well as a granular cytoplasmic pattern in hepatocytes. Antisense studies utilizing cultured liver explants show a vital role of elf3 in hepatocyte di erentiation and intrahepatic bile duct formation. The di erential expression, tissue localization, and functional studies demonstrate the importance of elf3 in modulating interactions between various components of the cytoskeleton proteins controlling liver and bile duct development.

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Section: Discussionmentioning

confidence: 99%

Elf3 encodes a novel 200-kD β-spectrin: role in liver development

et al. 1999

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“…The membrane-associated cytoskeleton is a twodimensional network located on the cytoplasmic surface of the plasma membrane [21][22][23][24][25][26][27][28][29]. It consists mainly of flexible rod-shaped tetramers of spectrin that are joined by actin protofilaments to form five-or sixsided polygons.…”

Section: Introductionmentioning

confidence: 99%

Spectrin's E2/E3 ubiquitin conjugating/ligating activity is diminished in sickle cells

2005

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Erythrocyte spectrin contains E2/E3 ubiquitin conjugating/ligating activity in its a subunit. Ankyrin is a target of spectrin's E2/E3 ubiquitin conjugating/ligating activity in vitro and in vivo. We compare the ubiquitination levels of ankyrin mediated by control and sickle cell spectrin using a biotinylated ubiquitin cell-free assay. Sickle cell spectrin has diminished ability to transfer ubiquitin from an intermediate spectrin-ubiquitin thioester adduct (a 0 spectrin) to ankyrin, which may be due to glutathiolation of spectrin's E2 and/ or E3 active site cysteines. There is also a diminished ability of the sickle cell ankyrin to serve as target of spectrin's E2/E3 activity, probably due to oxidative damage to ankyrin. A direct correlation exists between the a 0 /a spectrin ratio and spectrin's ability to ubiquitinate ankyrin. There is also an inverse correlation between severity of the disease and the a 0 /a spectrin ratio in SS erythrocytes. These results suggest that reduced spectrin E2/ E3 activity is an important determinant of sickle cell severity. Am. J. Hematol. 79:89-96, 2005.

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“…A human red blood cell (RBC) 1 is in residence in the human circulatory system for 120 days carrying oxygen from the lungs to all tissues within the body and carbon dioxide from the tissues back to the lungs. An RBC is an 8-m biconcave disk bounded by a plasma membrane.…”

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The Human Erythrocyte Proteome

Kakhniashvili

Bulla

Goodman

2004

Molecular & Cellular Proteomics

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This report describes an analysis of the red blood cell proteome by ion trap tandem mass spectrometry in line with liquid chromatography. Mature red blood cells lack all internal cell structures and consist of cytoplasm within a plasma membrane envelope. To maximize outcome, total red blood cell protein was divided into two fractions of membrane-associated proteins and cytoplasmic proteins. Both fractions were divided into subfractions, and proteins were identified in each fraction separately through tryptic digestion. Membrane protein digests were collected from externally exposed proteins, internally exposed proteins, "spectrin extract" mainly consisting of membrane skeleton proteins, and membrane proteins minus spectrin extract. Cytoplasmic proteins were divided into 21 fractions based on molecular mass by size exclusion chromatography. The tryptic peptides were separated by reverse-phase high-performance liquid chromatography and identified by ion trap tandem mass spectrometry. A total of 181 unique protein sequences were identified: 91 in the membrane fractions and 91 in the cytoplasmic fractions. Glyceraldehyde-3-phosphate dehydrogenase was identified with high sequence coverage in both membrane and cytoplasmic fractions. Identified proteins include membrane skeletal proteins, metabolic enzymes, transporters and channel proteins, adhesion proteins, hemoglobins, cellular defense proteins, proteins of the ubiquitin-proteasome system, G-proteins of the Ras family, kinases, chaperone proteins, proteases, translation initiation factors, and others. In addition to the known proteins, there were 43 proteins whose identification was not determined. Molecular & Cellular Proteomics 3:501-509, 2004.A human red blood cell (RBC) 1 is in residence in the human circulatory system for 120 days carrying oxygen from the lungs to all tissues within the body and carbon dioxide from the tissues back to the lungs. An RBC is an 8-m biconcave disk bounded by a plasma membrane. The major cytoplasmic constituent is hemoglobin, which is responsible for binding and releasing oxygen and carbon dioxide. On the cytoplasmic surface of the plasma membrane is a two-dimensional meshwork of proteins referred to as spectrin membrane skeleton. The spectrin membrane skeleton renders elasticity and flexibility to an RBC, allowing it to pass through vessels and capillaries that narrow to 1 m in diameter (1).Because of the ease in obtaining RBCs and because they lack internal organelles, the plasma membrane of this cell type has been studied extensively. The functions of hemoglobin are also well documented. Based on four decades of study, the identity, function, and topology of many RBC membrane proteins have been determined (1-3). With the advent of modern mass spectrometry (MS) and associated proteomic techniques, determination of the RBC proteome is now plausible. This kind of approach is a necessary first step in understanding how the RBC proteome becomes altered in various hematologic disorders. With this goal in mind, we utilized ion trap ...

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Spectrin and Related Molecule

Cited by 149 publications

References 341 publications

Elf3 encodes a novel 200-kD β-spectrin: role in liver development

Elf3 encodes a novel 200-kD β-spectrin: role in liver development

Spectrin's E2/E3 ubiquitin conjugating/ligating activity is diminished in sickle cells

The Human Erythrocyte Proteome

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