Specific binding of angiogenin to calf pulmonary artery endothelial cells.

Badet, Josette; Soncin, Fabrice; Guitton, Jean-Dominique; Lamare, Olivier; Cartwright, Terence; Barritault, Denis

doi:10.1073/pnas.86.21.8427

Cited by 123 publications

(114 citation statements)

References 45 publications

Supporting

Mentioning

106

Contrasting

Unclassified

Order By: Relevance

“…However, it has been shown that accumulation of ANG in the nucleolus of target endothelial cells is essential for its biological activity (23,24) and that ANG binds to a receptor on the surface of endothelial cells (25,26) and induces a variety of activities required for angiogenesis (26)(27)(28). ANG has been shown to be upregulated by hypoxia in cultured melanoma cells (29) and in human renal proximal tubular epithelial cells (30).…”

mentioning

confidence: 99%

Characterization of Human Angiogenin Variants Implicated in Amyotrophic Lateral Sclerosis

et al. 2007

View full text Add to dashboard Cite

Human angiogenin (ANG), the first member of the angiogenin family (from the pancreatic ribonuclease A superfamily) to be identified, is an angiogenic factor that induces neovascularization. It has received much attention due to its involvement in the growth of tumors and its elevated expression level in pancreatic and several other cancers. Recently the biological role of ANG has been shown to extend to the nervous system. Mutations in ANG have been linked with familial as well as sporadic forms of amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disorder characterized by selective destruction of motor neurons. Furthermore, mouse angiogenin-1 has been shown to be expressed in the developing nervous system and during the neuronal differentiation of pluripotent stem cells. We have now characterized the seven variants of ANG reported in ALS patients with respect to the known biochemical properties of ANG and further studied the biological properties of three of these variants. Our results show that the ribonucleolytic activity of six of the seven ANG-ALS implicated variants is significantly reduced or lost and some variants also show altered thermal stability. We report a significant reduction in the cell proliferative and angiogenic activities of the three variants that we chose to investigate further. Our studies on the biochemical and structural features of these ANG variants now form the basis for further investigations to determine their role(s) in ALS.Amyotrophic lateral sclerosis (ALS) 1 is a fatal neurodegenerative disorder characterized by selective destruction of motor neurons (1). In the past decade, a small number of genes involved in the etiology of the disease have been identified (for a recent review see ref 2). The best studied of these is SOD1 (3), the gene for Cu/Zn superoxide dismutase. More than a hundred SOD1 mutations have now been linked with ALS, and motor neuron death from many of these mutations has been shown to result from a toxic gain of function rather than loss of dismutase activity. However, mutations in SOD1 account for only 1-2% of all cases of ALS and 20% of the familial cases. Some of the other proteins implicated in ALS are the vesicle-trafficking protein VAPB (4); ALSIN, a putative guanine nucleotide factor for GTPase (5); and senataxin (6). In addition, vascular endothelial growth factor (VEGF), an angiogenic factor that plays an important role in motor neuron survival, has been linked with ALS (7-10). However, the causes and molecular mechanisms underlying ALS are still largely unclear, and effective therapies do not appear to be imminent. Angiogenin (ANG), which encodes an angiogenic protein, was recently identified as a candidate susceptibility gene for ALS in the Irish and Scottish population by Greenway et al. (11). In a further study of over 2500 individuals from five independent populations from northern Europe and North America, Greenway et al. (12) found seven missense mutations (Figure 1) in 11 unrelated individuals with sporadic ALS and in f...

show abstract

mentioning

confidence: 99%

Characterization of Human Angiogenin Variants Implicated in Amyotrophic Lateral Sclerosis

et al. 2007

View full text Add to dashboard Cite

show abstract

“…It has been demonstrated that Cu is required for angiogenesis [5,14,21,22,36]. Cu is a cofactor required for the function of several angiogenesis mediators, such as vascular endothelial growth factor (VEGF) and basic fibroblast growth factor (bFGF) [1,9,27,30,33]. Cu stimulates proliferation of endothelial cells in culture, which plays a pivotal role in the angiogenesis process [5,14].…”

mentioning

confidence: 99%

Trientine, a Copper-Chelating Agent, Induced Apoptosis in Murine Fibrosarcoma Cells In Vivo and In Vitro

Hayashi

Nishiya

Chiba

et al. 2007

The Journal of Veterinary Medical Science

View full text Add to dashboard Cite

ABSTRACT. Anti-copper treatments have been investigated to determine whether they suppress angiogenesis and tumor development since Cu is widely accepted as being required for angiogenesis. We examined the effects of treatment with trientine, a copper-chelating agent, on tumor development in a murine xenograft model using fibrosarcoma-derived transplantable QRsp-11 cells and C57BL/6 mice and induction of apoptosis in tumor cells and endothelial cells in vivo and in vitro. The tumor volumes increased more slowly in trientinetreated mice than in untreated mice. Tumor volumes in the treated mice were significantly smaller than those in the untreated mice at 24 days postinoculation (d.p.i.) of tumor cells. A cluster of pyknotic tumor cells and morphological abnormalities in capillary endothelial cells were observed in the tumors of trientine-treated mice but not in the tumors of untreated mice. The proportions of apoptotic and necrotic cells in the tumors of treated mice were approximately 3.5-fold higher than those in the tumors of untreated mice at 14 d.p.i. When the cells were treated with trientine in vitro, mouse endothelial cells and bovine primary endothelial cells showed an approximately 10-fold higher sensitivity to trientine than QRsp-11 cells in terms of D 37 . However, the proportion of apoptotic cells in endothelial cells was significantly lower than that in QRsp-11 cells after treatment with trientine. These results show that apoptosis was induced in tumor cells by treatment with trientine in vivo and in vitro.

show abstract

“…This protein potently elicits neovascularization (Fett et al, 1985;Strydom et al, 1985), induccs second-messenger responses in cultured endothelial cells Vallee, 1988, 1989), and interacts with putative cell-surface receptors (Hu et al, 1991;Badet et al, 1989;Chainoux et al, 1991 ). Eosinophil-derived neurotoxin (EDN) and eosinophil cationic protein (ECP) are also ribonucleases, homologous to pancreatic RNase Beintema et al, 1988b;Rosenberg et al, 1989b;Hamann et al, 1989;Barker el al., 1989;Slifman et al, 3986;Gullberg et al, 1986;Sorrentino and Glitz, 1991), that in this case act as neurotoxins and/or helminthotoxins (Durack et al, 1981 ;Fredens et al, 1982;McLaren et a]., 1984;Sorrentino et al, 1992).…”

mentioning

confidence: 99%

The amino acid sequence of human ribonuclease 4, a highly conserved ribonuclease that cleaves specifically on the 3′ side of uridine

Zhou

Strydom

1993

European Journal of Biochemistry

View full text Add to dashboard Cite

. (1986a) Biochemistry 25,7255-72641 was purified from human plasma and its amino acid sequence was determined. This protein is a 119-residue single-chain polypeptidc cross-linked by four disulfide bonds and has an amino-terminal pyroglutaminyl residue. No post-translational modifications were observed during extensive sequence studies on peptide fragments, except for the amino-terminal pyroglutamic acid and a possible deamidation of Asn66. The protein is homologous to the pancreatic ribonucleases and angiogenin, but differs substantially from both of these proteins; the protein sequence has 43% identity with human pancreatic ribonuclease and 39% identity with human angiogenin, as compared to 35% identity between human angiogenin and pancreatic ribonuclease. It is referred to as RNase 4, based on the nomenclature currently used for the genes of pancreatic RNase (RNase 1) and the eosinophil-derived RNases (RNase 2 and RNase 3).Virtually all of the RNasc active-site componcnts, including the catalytic residues Hisl2, His1 19 and Lys41, are preserved. However, some invariant residues of RNase 1 arc replaced, e.g. Lys7 by arginine, Asp14 by histidine, and Pro42 by arginine. RNase 4 contains a unique two-residue deletion at the position corresponding to amino acids 77 and 78 of pancreatic RNase, and its carboxyterminal sequence is truncated at position 122. The deletion in angiogenin at position 21 is also found in RNase 4.RNase 4 is very similar to two RNases isolated from bovine and porcine liver, and together they form a new fanlily in the RNase superfamily. The degree of inter-species similarity (90%) is much greater than within the pancreatic RNase and angiogenin families, which suggests that this ribonuclease could possess a physiologically important function other than general RNA catabolism.The ribonucleases (RNases) constitute a group of enzymes for which a large amount of chemical information now exists. This information mostly relates to the pancreatic RNases; sequences from more than 40 species are known (Beintema and van der Laan, 1986). Recent investigations and discoveries have suggested that these enzymes are but one subdivision of a much broader superfamily of structurally related proteins, some of which have important biochemical and physiological functions other than RNA digestion.One homologue of pancreatic RNase that has an unusual ribonucleolytic activity is angiogenin (Shapiro et al., 1986b). This protein potently elicits neovascularization (Fett et al., 1985; Strydom et al., 1985), induccs second-messenger responses in cultured endothelial cells (Bicknell and Vallee, Con-rsyondeirce ro D. J. Strydom,

show abstract

Specific binding of angiogenin to calf pulmonary artery endothelial cells.

Cited by 123 publications

References 45 publications

Characterization of Human Angiogenin Variants Implicated in Amyotrophic Lateral Sclerosis

Characterization of Human Angiogenin Variants Implicated in Amyotrophic Lateral Sclerosis

Trientine, a Copper-Chelating Agent, Induced Apoptosis in Murine Fibrosarcoma Cells In Vivo and In Vitro

The amino acid sequence of human ribonuclease 4, a highly conserved ribonuclease that cleaves specifically on the 3′ side of uridine

Contact Info

Product

Resources

About