Molecular characterization of human Ro/SS-A antigen. Amino terminal sequence of the protein moiety of human Ro/SS-A antigen and immunological activity of a corresponding synthetic peptide.

Lieu, Tsu-San; Newkirk, Marianna M.; Capra, J. Donald; Sontheimer, Richard D.

doi:10.1172/jci113607

Cited by 61 publications

(20 citation statements)

References 37 publications

(28 reference statements)

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“…The mechanism by which the calreticulin-peptide complex elicits immunity is unknown. A number of antigenic epitopes of calreticulin have been identified (20). The epitopes eliciting a humoral response in patients with autoimmune diseases have been reported to be located in the NH 2 -terminal part of the molecule.…”

Section: Discussionmentioning

confidence: 99%

An Autoantibody-Mediated Immune Response to Calreticulin Isoforms in Pancreatic Cancer

Hong¹,

Misek²,

Wang³

et al. 2004

Cancer Research

115

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The identification of circulating tumor antigens or their related autoantibodies provides a means for early cancer diagnosis as well as leads for therapy. We have used a proteomic approach to identify proteins that commonly induce a humoral response in pancreatic cancer. Aliquots of solubilized proteins from a pancreatic cancer cell line (Panc-1) were subjected to two-dimensional PAGE, followed by Western blot analysis in which sera of individual patients were tested for primary antibodies. Sera from 36 newly diagnosed patients with pancreatic cancer, 18 patients with chronic pancreatitis, 33 patients with other cancers, and 15 healthy subjects were analyzed. Autoantibodies were detected against either one or two calreticulin isoforms identified by mass spectrometry in sera from 21 of 36 patients with pancreatic cancer. One of 18 chronic pancreatitis patients and 1 of 15 healthy controls demonstrated autoantibodies to calreticulin isoform 1; none demonstrated autoantibodies to isoform 2. None of the sera from patients with colon cancer exhibited reactivity against either of these two proteins. One of 14 sera from lung adenocarcinoma patients demonstrated autoantibodies to calreticulin isoform 1; 2 of 14 demonstrated autoantibodies to isoform 2. Immunohistochemical analysis of calreticulin in pancreatic/ampullary tumor tissue arrays using an isoform nonspecific antibody revealed diffuse and consistent cytoplasmic staining in the neoplastic epithelial cells of the pancreatic and ampullary adenocarcinomas. The detection of autoantibodies to calreticulin isoforms may have utility for the early diagnosis of pancreatic cancer.

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Section: Discussionmentioning

confidence: 99%

An Autoantibody-Mediated Immune Response to Calreticulin Isoforms in Pancreatic Cancer

Hong¹,

Misek²,

Wang³

et al. 2004

Cancer Research

115

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“…Recently, another group has reported the determination of the amino-terminal 16 amino acids of the SS-A/Ro antigen purified by biochemical means from calf thymus (26) (21), detailed in Fig. 4 B.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of a cDNA clone encoding the 60-kD component of the human SS-A/Ro ribonucleoprotein autoantigen.

Ben-Chétrit

Gandy²,

Tan³

et al. 1989

J. Clin. Invest.

189

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“…Vinculin and ␣-actinin, but not the ␣ v ␤ 3 integrin, are selectively redistributed from the restructured focal adhesions in response to thrombospondin (5,8). A 19-amino acid sequence (amino acids [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35] in the N-terminal heparin-binding domains of both TSP-1 and TSP-2, referred to as the hep I peptide, has been determined to be sufficient for focal adhesion disassembly (9). The signaling events stimulated by thrombospondin/hep I interactions with cells are only partially understood.…”

Section: Thrombospondin (Tsp)mentioning

confidence: 99%

“…Has Sequence Homology to Calreticulin-The hep I peptide of thrombospondin (amino acids [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35] has been shown to cause loss of focal adhesions from spread BAE cells (9). To identify hep I-binding proteins that mediate focal adhesion disassembly, we used an affinity purification approach.…”

Section: A 60-kda Hep I-binding Protein Isolated From Bae Extractsmentioning

confidence: 99%

Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin

Goicoechea¹,

Orr²,

Pallero³

et al. 2000

Journal of Biological Chemistry

155

135

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Thrombospondin induces reorganization of the actin cytoskeleton and restructuring of focal adhesions. This activity is localized to amino acids 17-35 in the N-terminal heparin-binding domain of thrombospondin and can be replicated by a peptide (hep I) with this sequence. Thrombospondin/hep I stimulate focal adhesion disassembly through a mechanism involving phosphoinositide 3-kinase activation. However, the receptor for this thrombospondin sequence is unknown. We now report that calreticulin on the cell surface mediates focal adhesion disassembly by thrombospondin/hep I. A 60-kDa protein from endothelial cell detergent extracts has homology and immunoreactivity to calreticulin, binds a hep I affinity column, and neutralizes thrombospondin/ hep I-mediated focal adhesion disassembly. Calreticulin on the cell surface was confirmed by biotinylation, confocal microscopy, and by fluorescence-activated cell sorting analyses. Thrombospondin and calreticulin potentially bind through the hep I sequence, since thrombospondin-calreticulin complex formation can be blocked specifically by hep I peptide. Antibodies to calreticulin and preincubation of thrombospondin/hep I with glutathione S-transferase-calreticulin block thrombospondin/hep I-mediated focal adhesion disassembly and phosphoinositide 3-kinase activation, suggesting that calreticulin is a component of the thrombospondin-induced signaling cascade that regulates cytoskeletal organization. These data identify both a novel receptor for the N terminus of thrombospondin and a distinct role for cell surface calreticulin in cell adhesion.

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Molecular characterization of human Ro/SS-A antigen. Amino terminal sequence of the protein moiety of human Ro/SS-A antigen and immunological activity of a corresponding synthetic peptide.

Cited by 61 publications

References 37 publications

An Autoantibody-Mediated Immune Response to Calreticulin Isoforms in Pancreatic Cancer

An Autoantibody-Mediated Immune Response to Calreticulin Isoforms in Pancreatic Cancer

Isolation and characterization of a cDNA clone encoding the 60-kD component of the human SS-A/Ro ribonucleoprotein autoantigen.

Thrombospondin Mediates Focal Adhesion Disassembly through Interactions with Cell Surface Calreticulin

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