Cloning from the thyroid of a protein related to actin binding protein that is recognized by Graves disease immunoglobulins.

Leedman, Peter J.; Faulkner-Jones, Beverley; Cram, David S.; Harrison, Paul J.; West, Jeanette; O'Brien, Elizabeth; Simpson, Richard J.; Coppel, Ross L.; Harrison, Leonard C.

doi:10.1073/pnas.90.13.5994

Cited by 24 publications

(11 citation statements)

References 23 publications

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“…Two partial cDNA fragments of one species, termed actin-binding protein-like protein (ABPL), were cloned by PCR and mapped to chromosome 7; full-length cDNA has not been reported. A second species, termed truncated actin-binding protein (TABP) in one publication (9) and filamin homolog-1 in another (10), has been reported. The TABP open reading frame predicts a protein of only 195 residues, whereas only a 291-amino acid sequence has been reported for filamin homolog-1.…”

mentioning

confidence: 99%

Human β-Filamin Is a New Protein That Interacts with the Cytoplasmic Tail of Glycoprotein Ibα

Takafuta¹,

Wu²,

Murphy³

et al. 1998

Journal of Biological Chemistry

106

101

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mentioning

confidence: 99%

Human β-Filamin Is a New Protein That Interacts with the Cytoplasmic Tail of Glycoprotein Ibα

Takafuta¹,

Wu²,

Murphy³

et al. 1998

Journal of Biological Chemistry

106

101

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“…Additionally, a 21 kD truncated ABP with 70% homology to ABP-280 lacks the N-terminal actin binding domain and 22 of the 24 P-sheet repeats. Thus it neither binds nor cross-links actin filaments [53].…”

Section: Discussionmentioning

confidence: 94%

Expression and subcellular distribution of filamin isotypes in endothelial cells and pericytes

et al. 1998

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Two principal forms of the actin binding protein, filamin, are expressed in mammalian cells: nonmuscle and muscle isotypes (FLN-1 and FLN-2). A protein that copurifies with an alpha-naphthyl acetate hydrolyzing esterase from human omentum microvessel endothelial cells (EC) is isolated by nondenaturing electrophoresis, sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and electroblotting. The purified protein is subjected to in situ trypsin cleavage, reversed-phase high performance liquid chromatography (HPLC) and automated Edman degradation. Six peptide fragments from the protein are identified to have 60-66% identity with nonmuscle filamin (ABP-280). Two of these peptides are 100% identical to a previously sequenced human muscle filamin fragment. Polyclonal antibody is produced using a 16-residue synthetic peptide corresponding to a structural beta-sheet region of muscle filamin. Compared with a variety of vascular cells evaluated, retinal pericytes express an abundance of both muscle and non-muscle filamin isotypes. Pericytes contain at least 10 times more muscle filamin than human umbilical vein EC and at least three times the amount expressed in human omentum microvessel and bovine pulmonary artery EC. Differential detergent fractionation indicates that both filamin isotypes are primarily localized in the cytosol and membrane/organelle fractions of pericytes. Another actin crosslinking protein, alpha-actinin, is primarily found in the cytosol and cytoskeletal fractions. The dynamic regulation of actin microfilament organization in pericytes may be controlled in part by the two filamin isotypes, which in turn may contribute to pericyte contractility.

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“…Other receptors that can interact with ABP-280 include the acetylcholine receptors in chicken myoblasts, the immunoglobulin receptor Fc~'IR and the CDI8 subunit of the 132 integrin in leukocytes [27,34,35]. A truncated form of ABP-276/278, encompassing a part of repeat 23, hinge II and the entire repeat 24, interacted with the thyroid-stimulating hormone receptor in endocrine cells [17]. Through ABP interaction, membrane receptors mediate important cellular functions such as shape changes, focal adhesion, motility, signaling, and receptor clustering in response to external ligand binding.…”

Section: Discussionmentioning

confidence: 99%

Hepatitis B virus core protein interacts with the C-terminal region of actin-binding protein

2000

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Hepatitis B viral core protein is present in the nucleus and cytoplasm of infected hepatocytes. There is a strong correlation between the intrahepatic distribution of core protein and the viral replication state and disease activity in patients with chronic hepatitis. To understand the role of core protein in the pathogenesis of HBV, we used a yeast two-hybrid system to search for cellular proteins interacting with the carboxyl terminus of core protein, as this region is involved in a number of important functions in the viral replication cycle including RNA packaging and DNA synthesis. A cDNA encoding the extreme C-terminal region of human actin-binding protein, ABP-276/278, was identified. This interaction was further confirmed both in vitro and in vivo. In addition, the extreme C-terminal region of ABP-276/278 interacted with the nearly full-length HBV core protein. Since this region is present in both the core and the precore proteins, it is likely that both core and precore proteins of HBV can interact with the C-terminal region of ABP-276/278. The minimal region of ABP-276/278 which interacted with the HBV core protein was the C-terminal 199 amino acid residues which correspond to part of the 23rd repeat, the entire 24th repeat and the intervening hinge II region in ABPs. The potential functional outcome of ABP interaction in HBV replication and its contribution to the pathological changes seen in patients with chronic HBV infection are discussed.

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Cloning from the thyroid of a protein related to actin binding protein that is recognized by Graves disease immunoglobulins.

Abstract: Human actin binding protein (ABP) links specific membrane glycoproteins to cytoskeletal actin microfilaments. In human platelets and leukocytes, ABP directly links, respectively, the membrane glycoproteins GPlb and the high-affinity Fc receptor for IgG (FcIIR)

Cited by 24 publications

References 23 publications

Human β-Filamin Is a New Protein That Interacts with the Cytoplasmic Tail of Glycoprotein Ibα

Human β-Filamin Is a New Protein That Interacts with the Cytoplasmic Tail of Glycoprotein Ibα

Expression and subcellular distribution of filamin isotypes in endothelial cells and pericytes

Hepatitis B virus core protein interacts with the C-terminal region of actin-binding protein

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