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  • 1
    Electronic Resource
    Electronic Resource
    Actin and tubulin binding domains of synapsins Ia and Ib (1991)
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 413-422 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00216a016
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  • 2
    Electronic Resource
    Electronic Resource
    Adhesion between epithelial cells and T lymphocytes mediated by E-cadherin and the α E β 7 integrin (1994)
    [s.l.] : Nature Publishing Group
    Nature 372 (1994), S. 190-193 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] To identify a specific adhesion molecule on epithelial cells (EpC) that might mediate adhesion to intraepithelial lympho-cytes (IEL), we immunized mice with a mucosal EpC line (16E6.A5) known to support divalent-cation-dependent IEL adhesion3 and screened the resultant hybridoma culture ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/372190a0
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  • 3
    Electronic Resource
    Electronic Resource
    Autoantibodies specific for villin found in patients with colon cancer and other colitides (1995)
    Springer
    Digestive diseases and sciences 40 (1995), S. 389-395 
    Details
    ISSN: 1573-2568
    Keywords: autoantibodies ; villin ; colon cancer ; colitis ; brush border
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We have sought evidence for blood-borne autoantigens from the apical regions of the intestinal epithelial cell that are associated with specific gastrointestinal diseases. While a wide range of brush border-specific proteins are antigenic in various disease states, significantly increased levels of autoantibody to villin, a 95-kDa protein microvillar actin-binding protein, were identified by western blot in colon cancer patients' sera. Examination of a population with a range of colonic diseases showed that anti-villin antibody is most prevalent in patients with colon cancer at significantly higher (P〈0.005) levels than normal controls. We conclude that cryptic antigens within the brush border, specifically including villin, incite an active autoimmune response. The pathological significance of these antibodies remains to be determined. These anti-villin antibodies also may provide a unique noninvasive approach for the detection of gastrointestinal pathology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02065426
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  • 4
    Electronic Resource
    Electronic Resource
    Functional diversity among spectrin isoforms (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 12 (1989), S. 225-247 
    Details
    ISSN: 0886-1544
    Keywords: spectrin ; ankyrin ; protein 4.1 ; membrane skeleton ; spectrin-filament interaction ; fodrin ; adducin ; calpactin I ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The purpose of this review on spectrin is to examine the functional properties of this ubiquitous family of membrane skeletal proteins. Major topics include spectrin-membrane linkages, spectrin-filament linkages, the subcellular localization of spectrins in various cell types and a discussion of major functional differences between erythroid and nonerythroid spectrins. This includes a summary of studies from our own laboratories on the functional and structural comparison of avian spectrin isoforms which are comprised of a common alpha subunit and a tissue-specific beta subunit. Consequently, the observed differences among these spectrins can be assigned to differences in the properties of the beta subunits.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970120405
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  • 5
    Electronic Resource
    Electronic Resource
    Contributions of the β-subunit to spectrin structure and function (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 12 (1989), S. 248-263 
    Details
    ISSN: 0886-1544
    Keywords: ankyrin ; adducin ; protein 4.1 ; correlation length ; flexural rigidity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The three avian spectrins that have been characterized consist of a common α-subunit (240 kD) paired with an isoform-specific β-subunit from either erythrocyte (220 or 230 kD), brain (235 kD), or intestinal brush border (260 kD). Analysis of avian spectrins, with their naturally occurring “subunit replacement” has proved useful in assessing the relative contribution of each subunit to spectrin function. In this study we have completed a survey of avian spectrin binding properties and present morphometric analysis of the relative flexibility and linearity of various avian and human spectrin isoforms. Evidence is presented that, like its mammalian counterpart, avian brain spectrin binds human erythroid ankyrin with low affinity. Cosedimentation analysis demonstrates that (1) avian erythroid protein 4.1 stimulates spectrin-actin binding of both mammalian and avian erythrocyte and brain spectrins, but not the TW 260/240 isoform, (2) calpactin I does not potentiate actin binding of either TW 260/240 or brain spectrin, and (3) erythrocyte adducin does not stimulate the interaction of TW 260/240 with actin.In addition, a morphometric analysis of rotary-shadow images of spectrin isoforms, individual subunits, and reconstituted complexes from isolated subunits was performed. This analysis revealed that the overall flexibility and linearity of a given spectrin heterodimer and tetramer is largely determined by the intrinsic rigidity and linearity of its β-spectrin subunit. No additional rigidity appears to be imparted by noncovalent associations between the subunits. The scaled flexural rigidity of the most rigid spectrin analyzed (human brain) is similar to that reported for F-actin.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970120406
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  • 6
    Electronic Resource
    Electronic Resource
    Spectrin oligomers: A structural feature of the erythrocyte cytoskeleton (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 17 (1981), S. 275-287 
    Details
    ISSN: 0275-3723
    Keywords: spectrin ; erythrocyte ; cytoskeleton ; oligomers ; tetramer ; associations ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Spectrin reversibly self-associates to high molecular weight oligomers through a concentration-driven process characterized by association constants of about 105 mol-1. This association is prominent under physiological conditions of pH, ionic strength, and temperature. It is disrupted by urea, but not Triton X-100. The process of spectrin association appears mathematically to resemble that for tropomyosin, although the mechanism is probably different. Spectrin association is weak compared to other prominent protein-protein associations in the red cell membrane skeleton. The linkage of these weak and strong associations suggests a process whereby the membrane skelton spontaneously assembles. Such affinity-modulated assembly involving weak associations is likely to be the focus of numerous membrane control mechanisms.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.380170308
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  • 7
    Electronic Resource
    Electronic Resource
    The Polymeric State of Actin in the Human Erythrocyte Cytoskeleton (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 18 (1982), S. 493-505 
    Details
    ISSN: 0730-2312
    Keywords: actin ; cytoskeleton ; red cell ; erythrocyte ; size distribution ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Reports on the polymeric state of actin in the red cell have been diverse. We have used phalloidin to stabilize the actin in erythrocyte ghosts prior to extraction in low ionic strength media. A mild proteolytic digestion and Sepharose 4B gel filtration enable an F-actin polymer to be isolated in pure form [1]. Detailed size analysis of this polymer in a range of experiments suggests that actin exists in the erythrocyte principally as a polymer of 100 nm length composed of 30 monomers in a double helical chain 15 monomers long with an estimated molecular weight of 1.3 × 106 daltons.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.1982.240180410
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  • 8
    Electronic Resource
    Electronic Resource
    Phosphorylation of ankyrin down-regulates its cooperative interaction with spectrin and protein 3 (1988)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 37 (1988), S. 301-315 
    Details
    ISSN: 0730-2312
    Keywords: protein phosphorylation ; cytoskeleton ; erythrocyte ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Ankyrin mediates the primary attachment between beta spectrin and protein 3. Ankyrin and spectrin interact in a positively cooperative fashion such that ankyrin binding increases the extent of spectrin tetramer and oligomer formation (Giorgi and Morrow: submitted, 1988). This cooperative interaction is enhanced by the cytoplasmic domain of protein 3, which is prepared as a 45-4l-kDa fragment generated by chymotryptic digestion of erythrocyte membranes. Using sensitive isotope-ratio methods and non-denaturing PAGE, we now demonstrate directly (1) the enhanced affinity of ankyrin for spectrin oligomers compared to spectrin dimers; (2) a selective stimulation of the affinity of ankyrin for spectrin oligomer by the 43-kDa cytoplasmic domain of protein 3; and (3) a selective reduction in the affinity of ankyrin for spectrin tetramer and oligomer after its phosphorylation by the erythrocyte cAMP-independent membrane kinase. The phosphorylation of ankyrin does not affect its binding to spectrin dimer. Ankyrin also enhances the rate of interconversion between dimer-tetramer-oligomer by 2-3-fold at 30°C, and in the presence of the 43-kDa fragment, ankyrin stimulates the rate of oligomer interconversions by nearly 40-fold at this temperature. These results demonstrate a long-range cooperative interaction between an integral membrane protein and the peripheral cytoskeleton and indicate that this linkage may be regulated by covalent protein phosphorylation. Such interactions may be of general importance in nonerythroid cells.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240370305
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  • 9
    Electronic Resource
    Electronic Resource
    Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin (1986)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 30 (1986), S. 51-69 
    Details
    ISSN: 0730-2312
    Keywords: cytoskeleton ; spectrin ; ankyrin ; calmodulin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A study of human erythrocyte and brain spectrin with particular emphasis on the beta subunits revealed a structural homology but functional dissimilarity between these two molecules. Six monoclonal antibodies raised to human erythrocyte beta spectrin identify three of the four proteolytically defined domains of erythrocyte beta spectrin. Five of these monoclonal antibodies cross-react with human brain spectrin. None of a previously identified set of alpha erythrocyte spectrin monoclonal antibodies [Yurchenco et al: J Biol Chem 257:9102, 1982] reacted with brain spectrin. A domain map generated by limited tryptic digestion shows that brain spectrin is composed of proteolytically resistant domains analogous to erythrocyte spectrin, but the brain protein is more basic. The binding of brain spectrin to erythrocyte ankyrin, both in solution and on erythrocyte IOVs, yielded an association constant approximately 100 times weaker than for erythrocyte spectrin. The binding of azido-calmodulin under native conditions was specific for the erythrocyte beta subunit but was not calcium dependent. In contrast, azido-calmodulin bound only to the alpha subunit of brain spectrin in a calcium-dependent manner. The similarity of structure but modified functional character-istics of the brain and erythrocyte beta spectrins suggest that these proteins serve different cellular roles.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240300107
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  • 10
    Electronic Resource
    Electronic Resource
    A domain of synapsin I involved with actin bundling shares immunologic cross-reactivity with villin (1988)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 36 (1988), S. 25-35 
    Details
    ISSN: 0730-2312
    Keywords: neuronal phosphoprotein ; brush border ; protein domains ; cytoskeleton ; synaptic vesicles ; actin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Synapsin I is a neuronal phosphoprotein that can bundle actin filaments in vitro. This activity is under phosphorylation control, and may be related to its putative in vivo role of regulating the clustering and release of small synaptic vesicles. We have compared human and bovine synapsin I by peptide mapping, and have used NTCB (2-nitro-5-thiocyano benzoic acid) cleavage to generate a series of peptide fragments from bovine synapsin I. After chymotryptic digestion, 88% of the tyrosine-containing fragments appear to be structurally identical in human and bovine synapsin I, as judged by their positions on high-resolution two-dimensional peptide maps. The alignment of the NTCB peptides within the parent protein have been determined by peptide mapping, and the ability of these fragments to precipitate with actin bundles has been measured. Only peptides that are derived from regions near the ends of the protein are active. One such 25-kDa peptide which sediments with actin also cross-reacts with antibodies to chicken villin, an actin binding and bundling protein derived from the intestinal microvillus. Since in other respects villin appears to be an unrelated protein, these results suggest the possibility that certain actin binding proteins may show immunologic cross-reactivity due to convergent evolution within the acting binding domain.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240360104
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