A cellular protein phosphorylated by the avian sarcoma virus transforming gene product is associated with ribonucleoprotein particles.

Arrigo, André Patrick; Darlix, Jean‐Luc; Spahr, Pierre-François

doi:10.1002/j.1460-2075.1983.tb01424.x

Cited by 29 publications

(36 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…69 One study reported that 15% of cellular ANXA2 was nuclear and was released from the nucleus by RNase A. 74,76,77 This is consistent with the report that ANXA2 binds to RNA 78 ; nevertheless, the role of nuclear ANXA2 still remains elusive.The tissue content of ANXA2 and S100A10 has been reported in both avian and mammalian tissues. These proteins are undetectable in heart, smooth muscle, skeletal muscle, and cartilage.…”

supporting

confidence: 70%

“…[50][51][52] ANXA2 is primarily localized in the cytoplasm and plasma membrane with a small population in the nucleus. 74 Many functions have been attributed to ANXA2. Extracellular ANXA2 was originally identified as a receptor for tenascin-C, 75 and The convex side faces the cellular membrane and contains the Ca 2ϩ and phospholipid binding sites, whereas the concave side faces away from the membrane and contains both the N-and C-terminal regions of ANXA2.…”

Section: The Aiit Structurementioning

confidence: 99%

See 1 more Smart Citation

The role of the annexin A2 heterotetramer in vascular fibrinolysis

Madureira¹,

Surette²,

Phipps³

et al. 2011

Blood

110

129

View full text Add to dashboard Cite

The vascular endothelial cells line the inner surface of blood vessels and function to maintain blood fluidity by producing the protease plasmin that removes blood clots from the vasculature, a process called fibrinolysis. Plasminogen receptors play a central role in the regulation of plasmin activity. The protein complex annexin A2 heterotetramer (AIIt) is an important plasminogen receptor at the surface of the endothelial cell. AIIt is composed of 2 molecules of annexin A2 (ANXA2) bound together by a dimer of the protein S100A10. Recent work performed by our laboratory allowed us to clarify the specific roles played by ANXA2 and S100A10 subunits within the AIIt complex, which has been the subject of debate for many years. The ANXA2 subunit of AIIt functions to stabilize and anchor S100A10 to the plasma membrane, whereas the S100A10 subunit initiates the fibrinolytic cascade by colocalizing with the urokinase type plasminogen activator and receptor complex and also providing a common binding site for both tissue-type plasminogen activator and plasminogen via its C-terminal lysine residue. The AIIt mediated colocalization of the plasminogen activators with plasminogen results in the rapid and localized generation of plasmin to the endothelial cell surface, thereby regulating fibrinolysis. (Blood. 2011;118(18):4789-4797) IntroductionThe vascular endothelium consists of a single cell layer lining all vessels that separates the blood from the tissues. It is estimated to be composed of ϳ 10 13 cells, representing a weight of 1.5 kg and an area of 4000 to 7000 m 2 . 1 Endothelial cells play a role in primary hemostasis, coagulation, fibrinolysis, and regulation of vasomotor tone. In addition to regulating the flow of nutrients, the vascular endothelium regulates many diverse biologically active molecules. These functions of the endothelium are achieved through the presence of membrane-bound receptors for various proteins, lipidtransporting complexes, hormones, and metabolites, as well as through specific extracellular proteins and receptors that regulate cell-cell and cell-matrix interactions. 2 Whereas exposure to inflammatory and/or septic stimuli rapidly leads to procoagulant behavior, unperturbed endothelial cells provide an anticoagulant environment. After vascular insult, endothelial cells express tissue factor and initiate the coagulation cascade that results in thrombin activation and fibrin clot deposition. At the same time, anticoagulant pathways and fibrinolysis are activated to avoid disseminated coagulation and to also limit fibrin accumulation. [3][4][5] Fibrinogen is a large glycoprotein that constitutes the main component of a fibrin clot. Each fibrinogen molecule is composed of 2 sets of A␣-, B␤-, and ␥-polypeptide chains that form a protein containing 2 distal D regions connected to a central E region by a coiled-coil segment. 6 Fibrin is produced on cleavage of the fibrinopeptides by thrombin, which results in the formation of double-stranded half-staggered oligomers that lengthen into protofibrils...

show abstract

supporting

confidence: 70%

Section: The Aiit Structurementioning

confidence: 99%

The role of the annexin A2 heterotetramer in vascular fibrinolysis

Madureira¹,

Surette²,

Phipps³

et al. 2011

Blood

110

129

View full text Add to dashboard Cite

show abstract

“…It has become evident from cell fractionation, morphologic and immunochemical studies that p36, or at least a fraction of it, is closely associated with plasma membranes (Cooper and Hunter, 1982;Amini and Kaji, 1983;Courtneidge et al, 1983;Nigg et al, 1983), with detergent-resistant cytoskeletal structures (Cheng and Chen, 1981;Cooper and Hunter, 1982) or, according to one study, with ribonucleoprotein particles (Arrigo et al, 1983). However, distinctly specific interactions, such as that of vinculin, another important tyrosine kinase substrate, and focal adhesion sites (Sefton et al, 1981), have not been found between p36 and other membrane or cytoskeletal components.…”

Section: Discussionmentioning

confidence: 99%

The p36 substrate of tyrosine-specific protein kinases co-localizes with non-erythrocyte alpha-spectrin antigen, p230, in surface lamina of cultured fibroblasts.

Lehto¹,

Virtanen²,

Paasivuo³

et al. 1983

The EMBO Journal

View full text Add to dashboard Cite

Biochemical and immunofluorescence studies have demonstrated that p36, a major substrate for the tyrosinespecific protein kinases induced by several sarcoma viruses and epidermal growth factor, is associated with plasma membranes and detergent-resistant cytoskeletal structures of cultured cells. We have used here polyclonal antisera and monoclonal antibodies in indirect immunofluorescence microscopy to study the subcellular location of p36 and the p230, which is a subplasmalemmal polypeptide showing immunologic cross-reactivity with erythrocyte a-spectrin. Both p36 and p230 showed a diffuse distribution in fixed and permeabilized cells and were localized in a surface lamina-like network in Triton-extracted cells. In double-staining experiments, an extensive co-distribution between these proteins was seen in detergent-treated cultured fibroblasts. These results, together with our previous work, suggest that the p36 protein is an integral part of the detergent-resistant proteinaceous network at the cytoplasmic face of the plasma membrane.

show abstract

“…It was also shown that ANXA2 immunoprecipitated from UV-irradiated cultured cells associated with RNA and formed a RNA-ANXA2 cross-linked ribonucleoprotein complex. These authors also showed by biochemical fractionation experiments that about 10 -15% of the total cellular ANXA2 was associated with the nucleus (31). Ensuing studies showed that ANXA2 could bind to deoxyribonucleic acid structures such as Z-DNA (32) or Alu subsequences (33).…”

mentioning

confidence: 93%