Actin and Actin-Binding Proteins. A Critical Evaluation of Mechanisms and Functions

Pollard, Thomas D.; Cooper, John A.

doi:10.1146/annurev.bi.55.070186.005011

Cited by 1,434 publications

(551 citation statements)

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“…Deletion of one of the 37-amino acid motifs was recently identified in a patient with SLE and was associated with increased apoptosis in WEHI-231 B lymphoma cells transfected with the mutant HS1 and in the patient's peripheral B lymphocytes (24). Because the 37-amino acid repeats are considered to be important in HS1 binding to F-actin (a cytoplasmic protein) in NIH313 cells (39), this mutant HS1 may display reduced binding to F-actin and thereby more easily translocate from cytoplasm to nucleus after BCR stimulation, accelerating signal transduction (40). The function of the EP repeat motif from codons 363 to 374 has not been clarified.…”

Section: Discussionmentioning

confidence: 99%

Association of a four–amino acid residue insertion polymorphism of the HS1 gene with systemic lupus erythematosus: Molecular and functional analysis

Otsuka

Horiuchi

Yoshizawa

et al. 2004

Arthritis & Rheumatism

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Objective. To investigate whether polymorphism(s) or mutation(s) in the hematopoietic cellspecific Lyn substrate 1 (HS1) gene are involved in the pathogenesis of systemic lupus erythematosus (SLE).Methods. The entire coding region of the HS1 gene was analyzed by reverse transcriptase-polymerase chain reaction/single-strand conformational polymorphism analysis. HS1-transfected WEHI-231 cells or B lymphocytes from patients with SLE were studied for apoptosis, activation, and proliferation by flow cytometric analysis and MTT assay.Results. We identified a glutamic acid-prolineglutamic acid-proline insertion between codons 366 and 367 (EPEP366-367ins) and 2 amino acid substitutions (A235T and E361K). The genotype frequency among individuals homozygous for the EPEP؉ allele was 0.184 in 201 patients with SLE but only 0.098 in 184 healthy individuals (P ‫؍‬ 0.016). The allele frequency of EPEP366-367ins was 0.408 in patients with SLE; this frequency was significantly higher than that in healthy controls (0.312) (P ‫؍‬ 0.006). WEHI-231 cells transfected with EPEP؉ HS1 were 100-fold more sensitive to B cell receptor (BCR)-mediated apoptosis than were those transfected with HS1 without EPEP. B lymphocytes from SLE patients with the EPEP؉ allele were significantly more apoptotic without BCR stimulation and less activated after BCR stimulation than were those from SLE patients without the EPEP allele. Conclusion. These results suggest that HS1 with the EPEP insertion polymorphism transmits accelerated signals from BCR and is involved in the pathogenesis of SLE.Systemic lupus erythematosus (SLE) is a prototypic systemic autoimmune disease characterized by the presence of a variety of autoantibodies. Various genetic and environmental factors, including B cell hyperactivity, T cell dysfunction, and cytokine dysregulation, initiate immune activation in SLE that culminates in organ inflammation and damage (1-9). It has been considered that B cells are innocent bystanders that are activated secondarily by autoreactive T lymphocytes. However, recent evidence from the study of human SLE and its murine models suggests that B lymphocytes are intrinsically defective and are primarily essential for the maintenance of activated/memory T cells by presenting antigens to T cells.B cells from mice deficient in Lyn (10-12), CD22 (13-16), SHP-1 (17,18) exhibit a hyperreactive phenotype and produce autoantibodies. Indeed, Lyn-deficient mice demonstrate activation of autoreactive B cells and subsequent SLE-like symptoms, such as the production of anti-double-stranded DNA (anti-dsDNA)

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Section: Discussionmentioning

confidence: 99%

Association of a four–amino acid residue insertion polymorphism of the HS1 gene with systemic lupus erythematosus: Molecular and functional analysis

Otsuka

Horiuchi

Yoshizawa

et al. 2004

Arthritis & Rheumatism

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“…These constantly occurring deand repolymerization processes necessitate the activity of a large number of actin binding proteins (AbPs), which modify its supramolecular organization according to cellular needs. Many of these proteins are regulated in their activity by external signals, phosphorylation, changes in the intracellular free calcium-ion concentration, or by interaction with particular membrane lipids [for reviews see Pollard and Cooper, 1986;Pollard and Borisy, 2003].…”

Section: Introductionmentioning

confidence: 99%

The β‐thymosins: Intracellular and extracellular activities of a versatile actin binding protein family

Mannherz

Hannappel

2009

Cell Motil. Cytoskeleton

109

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The b-thymosins are N-terminally acetylated peptides of about 5 kDa molecular mass and composed of about 40-44 amino acid residues. The first member of the family, thymosin b4, was initially isolated from thymosin fraction 5, prepared in five steps from calf thymus. Thymosin b4 was supposed to be specifically produced and released by the thymic gland and to possess hormonal activities modulating the immune response. Various paracrine effects have indeed been reported for these peptides such as cardiac protection, angiogenesis, stimulation of wound healing, and hair growth. Besides these paracrine effects, it was noted that b-thymosins occur in high concentration in the cytoplasm of many eukaryotic cells and bind to the cytoskeletal component actin. Subsequently it became apparent from in vitro experiments that they preferentially bind to monomeric (G-)actin and stabilize it in its monomeric form. Due to this ability the b-thymosins are the main intracellular actin sequestering factor, i.e., they posses the ability to remove monomeric actin from the dynamic assembly and disassembly processes of the actin cytoskeleton that constantly occur in activated cells. In this review we will concentrate on the intracellular activity and localization of the b-thymosins, i.e., their modulating effect on the actin cytoskeleton. Cell Motil. Cytoskeleton 66: 839-851, 2009. '

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“…Sequence analysis revealed that Wcor719 encodes a protein with significant homology with ABP. This group of proteins is involved in the regulation of different cellular processes such as cytokinesis, cell locomotion, cytoplasmic streaming and actin assembly in the membrane cytoskeleton, and recently in signal transduction events [3][4][5][6][7]. The high expression of a gene with these characteristics suggests a possible function in regulating the structure of actin filaments during cold acclimation.…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of a low temperature regulated gene encoding an actin‐binding protein from wheat

1996

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Actin and Actin-Binding Proteins. A Critical Evaluation of Mechanisms and Functions

Cited by 1,434 publications

References 1 publication

Association of a four–amino acid residue insertion polymorphism of the HS1 gene with systemic lupus erythematosus: Molecular and functional analysis

Association of a four–amino acid residue insertion polymorphism of the HS1 gene with systemic lupus erythematosus: Molecular and functional analysis

The β‐thymosins: Intracellular and extracellular activities of a versatile actin binding protein family

Identification and characterization of a low temperature regulated gene encoding an actin‐binding protein from wheat

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