Detection of secreted and intracellular annexin II by a radioimmunoassay

Davis, Randall G.; Vishwanatha, Jamboor K.

doi:10.1016/0022-1759(95)00207-3

Cited by 10 publications

(7 citation statements)

References 11 publications

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“…It is involved in DNA replication [29], and invasion and metastasis [23], [26]–[28], [30], [31]. It binds with gastrin [32], tissue plasminogen activator [27], [28], actin [33], and tenacin C [23] and has been investigated as a serum [34] and urine [35] biomarker of pancreatic cancer. Expression levels of annexin A2 are related to resistance to gemcitabine [36], which is mediated by the interaction of an alternatively spliced segment of tenascin-C with annexin A2 under the control of the PI3K/Akt and NF-kB pathways [37].…”

Section: Discussionmentioning

confidence: 99%

A Functional Proteomic Method for Biomarker Discovery

et al. 2011

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The sequencing of the human genome holds out the hope for personalized medicine, but it is clear that analysis of DNA or RNA content alone is not sufficient to understand most disease processes. Proteomic strategies that allow unbiased identification of proteins and their post-transcriptional and -translation modifications are an essential complement to genomic strategies. However, the enormity of the proteome and limitations in proteomic methods make it difficult to determine the targets that are particularly relevant to human disease. Methods are therefore needed that allow rational identification of targets based on function and relevance to disease. Screening methodologies such as phage display, SELEX, and small-molecule combinatorial chemistry have been widely used to discover specific ligands for cells or tissues of interest, such as tumors. Those ligands can be used in turn as affinity probes to identify their cognate molecular targets when they are not known in advance. Here we report an easy, robust and generally applicable approach in which phage particles bearing cell- or tissue-specific peptides serve directly as the affinity probes for their molecular targets. For proof of principle, the method successfully identified molecular binding partners, three of them novel, for 15 peptides specific for pancreatic cancer.

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Section: Discussionmentioning

confidence: 99%

A Functional Proteomic Method for Biomarker Discovery

et al. 2011

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“…Annexins are released extracellularly by endothelial cells (99), lactating mammary epithelium (282) chondrocytes and fibroblasts (262,183,205), and is present in sera of patients with myocardial infarction (287), prostate secretion (135), amniotic fluid (99), and pulmonary surfactant (314). Annexin I1 is also released by syncytiotrophoblasts (379, keratinocytes (212), fibroblasts (205), osteoclasts (329), pancreatic adenocarcinoma (79, and present in sera of patients with rheumatoid arthritis and SLE (339), in retroplacental sera (374), and bronchoalveolar lavage (75).…”

Section: Distributionmentioning

confidence: 99%

Human placental Fcγ‐binding proteins in the maternofetal transfer of IgG

Kristoffersen

1996

APMIS

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“…The presence of soluble A11 in normal human serum (23) strongly suggests physiological release of AII. As A11 is present in normal human kidney (1) and can be secreted or released by malignant cells ( 5 ) , we were interested in investigating whether A11 is secreted from kidneys with a malignant tumour. Renal cell carcinomas are clinically unpredictable.…”

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confidence: 99%

Inhibition of phytohaemagglutinin‐induced lymphoproliferation by soluble annexin II in sera from patients with renal cell carcinoma

Aarli

Jensen

Kristoffersen

et al. 1997

APMIS

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Annexin II (AII) is a member of a family of glycoproteins which bind negatively charged phospholipids in a calcium‐dependent manner. Annexins are membrane‐associated proteins, expressed both in normal and malignant cells, but have also been detected as soluble molecules in serum and other body fluids. Because of their adhesive properties, it has been suggested that annexins play a role in the metastatic process. An ELISA was established for quantification of soluble AII. Within‐run variation was 5.2–10.4% and run‐to‐run variation 12.4–15.6%. Soluble AII was detected in all sera studied. A strongly positive serum was arbitrarily given the value 100 AII units and used as reference serum. The mean level in sera from 20 normal blood donors was 49 (SE 5.6) AII units. Sera from peripheral blood of five patients with renal cell carcinoma and sera from blood obtained from the renal vein of the same patients contained 47 (SE 20) and 83 (SE 28) AII units, respectively. In two patients, AII levels were increased in renal vein serum as compared with peripheral blood serum. Interestingly, in both cases, and in none of the three remaining cases, phytohaemagglutinin‐stimulated lymphoproliferation was suppressed by renal vein serum as compared with peripheral blood serum. Affinity absorption of AII from the renal vein sera with increased AII levels strongly reduced their immunosuppressive activity. Addition of affinity‐purified AII to cell cultures suppressed lymphoproliferation. These data show that the level of AII is markedly increased in renal vein sera from some patients with renal cell carcinoma, suggesting that AII may be locally released in vivo. The study also demonstrates an immunosuppressive effect of soluble AII in vitro. We speculate that soluble AII released by the tumour has immunosuppressive properties. This study identifies soluble AII as a novel immunosuppressive factor in sera from patients with renal cell carcinoma. A further study including a larger number of patients is currently in progress, in order to investigate the pathological significance of this finding.

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Detection of secreted and intracellular annexin II by a radioimmunoassay

Cited by 10 publications

References 11 publications

A Functional Proteomic Method for Biomarker Discovery

A Functional Proteomic Method for Biomarker Discovery

Human placental Fcγ‐binding proteins in the maternofetal transfer of IgG

Inhibition of phytohaemagglutinin‐induced lymphoproliferation by soluble annexin II in sera from patients with renal cell carcinoma

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