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Gene Review

ANGPTL6  -  angiopoietin-like 6

Homo sapiens

Synonyms: AGF, ARP5, Angiopoietin-like protein 6, Angiopoietin-related growth factor, Angiopoietin-related protein 5, ...
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Disease relevance of ANGPTL6

  • We assessed the consequences of transitory global cerebral ischemia and the influence of monosialoganglioside inner ester (AGF 2) treatment on neurologic outcome, cerebral blood flow, and cerebral metabolic rate in monkeys over 48 hours [1].
  • Binding of anti-EMA, AGF 4:48 and the lectin UEA-1 to human ovarian carcinomas: histological and clinical correlations [2].
  • A series of 50 specimens of Hodgkin's disease and 10 of reactive follicular hyperplasia were examined by means of indirect immunoperoxidase staining with a monoclonal antibody AGF 4.48: this is known to bind to 3-fucosyl-N-acetyllactosamine, which, in particular, is expressed by granulocyte series cells [3].
  • Since blockage of nuclear translocation of AGF in endothelial cells with neomycin resulted in inhibition of the growth factor capacity to induce angiogenesis, we treated glioma cells with neomycin and assessed its effects on cell proliferation [4].
  • There was no significant difference in pseudarthrosis rates between the AGF treatment group and historical cohort [5].

High impact information on ANGPTL6

  • These findings demonstrate that biological functions of AGF in epidermal keratinocytes could lead to novel therapeutic strategies for wound care and epidermal regenerative medicine [6].
  • Furthermore, we observed that AGF is expressed in platelets and mast cells, and detected at wounded skin, whereas there was no expression of AGF detected in normal skin tissues, suggesting that AGF derived from these infiltrated cells affects epidermal proliferation and thereby plays a role in the wound healing process [6].
  • An in vitro chamber assay revealed that AGF directly promotes chemotactic activity of vascular endothelial cells [7].
  • Furthermore, we found that plasma leakage occurred after direct injection of AGF into the mouse dermis, suggesting that AGF directly induces a permeability change in the local vasculature [7].
  • We showed that AGF is a secreted protein and does not bind to tyrosine kinase with immunoglobulin and EGF-homology domain (Tie1) or Tie2 receptors [7].

Chemical compound and disease context of ANGPTL6

  • The staining reactions of the monoclonal antibodies anti-EMA, AGF 4:48 and the lectin UEA-1 from Ulex europaeus were investigated in formalin-fixed, paraffin-embedded sections of 36 primary ovarian carcinomas [2].

Biological context of ANGPTL6

  • Optimal AGF production was obtained after 24 h of culture at a cell density ranging from 2.5 to 5 million cells/ml [8].
  • In consequence, IC and AGF may induce two different activation phenotypes in EC that appear in a temporally and/or spatially coordinated manner in inflammatory tissues [9].
  • Platelet counts from the AGF platelet concentrates demonstrated an average 3.5-fold increase compared with preoperative serum levels [10].
  • SUMMARY OF BACKGROUND DATA: AGF has been shown to promote bone formation in vitro and in vivo in animal studies [11].
  • More recently, AGF (also called Angptl6) has been shown to counteract obesity and related insulin resistance [12].

Anatomical context of ANGPTL6

  • We found that three myeloma cell lines (RPMI 8226, U266, and IM9) produce an autostimulatory growth factor (AGF) and thus increase their own proliferation by 2- to 3-fold in cells cultured at low density [8].
  • Autologous growth factor concentrate (AGF) prepared by ultraconcentration of platelets contains multiple growth factors having a chemotactic and mitogenic effect on mesenchymal stem cells and osteoblasts and may play a role in initiating bone healing [13].
  • Angiopoietin-related growth factor (AGF) supports adhesion, spreading, and migration of keratinocytes, fibroblasts, and endothelial cells through interaction with RGD-binding integrins [14].
  • In contrast, angiogenic growth factors (AGF) activate EC proliferation and inhibit cell adhesiveness for leukocytes [9].
  • Presence of 3-fucosyl-N-acetyllactosamine shown by monoclonal antibody AGF 4.48 in Reed-Sternberg cells [3].

Associations of ANGPTL6 with chemical compounds

  • An AGF stimulation of prostacyclin production was also observed in the presence of the calcium ionophore A23187; it therefore seemed likely that the key event required for EGF to stimulate prostacyclin production might be an increase in the available cellular Ca2+ [15].
  • AGF was used with autograft and coraline hydroxyapatite in all posterior fusions, and autograft, coral, and intradiscal spacer (carbon fiber spinal fusion cages or Synthes femoral ring) in intradiscal fusions [13].
  • Our results strongly suggest that AGF is an integrin ligand as well as a mitogenic growth factor and theoretically participates in cutaneous wound healing in a more complex mechanism [14].
  • The distribution in renal tumours of 3-fucosyl-N-acetyl lactosamine has been studied by using the monoclonal antibodies AGF 4.36 and AGF 4.48 and immunoperoxidase methods on tissue sections [16].
  • The extracellular accumulation of hyaluronic acid was higher in FGF than in AGF, whilst the reverse pattern was observed intracellularly [17].

Analytical, diagnostic and therapeutic context of ANGPTL6

  • The BCGF produced by RPMI 8226 can be absorbed onto RPMI 8226 cells together with the RPMI 8226 AGF, and the two are copurified on gel filtration in a peak with an apparent molecular weight of 70,000 [8].
  • When used as an adjunct to autograft, AGF offers theoretical advantages that need to be examined in controlled studies [13].
  • To date, AGF has been used in 39 patients having lumbar spinal fusion [13].
  • The purpose of this retrospective study is to review our results with AGF in lumbar spinal fusions [13].
  • The staining patterns obtained with antiepithelial membrane antigen (anti-EMA) and the monoclonal antibody to 3-fucosyl-N-acetyllactosamine (AGF 4:48) in the uterine cervix in intraepithelial and invasive neoplasia were compared to determine a possible role in differential diagnosis of reactive and neoplastic conditions [18].


  1. Influence of monosialoganglioside inner ester on neurologic recovery after global cerebral ischemia in monkeys. Cahn, R., Borzeix, M.G., Aldinio, C., Toffano, G., Cahn, J. Stroke (1989) [Pubmed]
  2. Binding of anti-EMA, AGF 4:48 and the lectin UEA-1 to human ovarian carcinomas: histological and clinical correlations. Bradgate, M.G., Redman, C.W., Rollason, T.P., Williams, A., Byrne, P., Kelly, K. British journal of obstetrics and gynaecology. (1989) [Pubmed]
  3. Presence of 3-fucosyl-N-acetyllactosamine shown by monoclonal antibody AGF 4.48 in Reed-Sternberg cells. Crocker, J., Skilbeck, N., Brown, G., Bunce, C. J. Clin. Pathol. (1986) [Pubmed]
  4. Antiproliferative effect of neomycin in glioma cells. Cuevas, P., Diaz-González, D., Dujovny, M. Neurol. Res. (2002) [Pubmed]
  5. Do autologous growth factors enhance transforaminal lumbar interbody fusion? Hee, H.T., Majd, M.E., Holt, R.T., Myers, L. European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society. (2003) [Pubmed]
  6. Angiopoietin-related growth factor (AGF) promotes epidermal proliferation, remodeling, and regeneration. Oike, Y., Yasunaga, K., Ito, Y., Matsumoto, S., Maekawa, H., Morisada, T., Arai, F., Nakagata, N., Takeya, M., Masuho, Y., Suda, T. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  7. Angiopoietin-related growth factor (AGF) promotes angiogenesis. Oike, Y., Ito, Y., Maekawa, H., Morisada, T., Kubota, Y., Akao, M., Urano, T., Yasunaga, K., Suda, T. Blood (2004) [Pubmed]
  8. Production of growth factors by human myeloma cells. Klein, B., Jourdan, M., Vazquez, A., Dugas, B., Bataille, R. Cancer Res. (1987) [Pubmed]
  9. Human guanylate binding protein-1 (hGBP-1) characterizes and establishes a non-angiogenic endothelial cell activation phenotype in inflammatory diseases. Naschberger, E., Bauer, M., Stürzl, M. Adv. Enzyme Regul. (2005) [Pubmed]
  10. Role of activated growth factors in lumbar spinal fusions. Castro, F.P. Journal of spinal disorders & techniques. (2004) [Pubmed]
  11. Efficacy of autologous growth factors in lumbar intertransverse fusions. Weiner, B.K., Walker, M. Spine. (2003) [Pubmed]
  12. Angiopoietin-like proteins: potential new targets for metabolic syndrome therapy. Oike, Y., Akao, M., Kubota, Y., Suda, T. Trends in molecular medicine. (2005) [Pubmed]
  13. Use of autologous growth factors in lumbar spinal fusion. Lowery, G.L., Kulkarni, S., Pennisi, A.E. Bone (1999) [Pubmed]
  14. Angiopoietin-related growth factor (AGF) supports adhesion, spreading, and migration of keratinocytes, fibroblasts, and endothelial cells through interaction with RGD-binding integrins. Zhang, Y., Hu, X., Tian, R., Wei, W., Hu, W., Chen, X., Han, W., Chen, H., Gong, Y. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  15. Epidermal growth factor stimulation of prostacyclin production by cultured aortic smooth muscle cells: requirement for increased cellular calcium levels. Blay, J., Hollenberg, M.D. J. Cell. Physiol. (1989) [Pubmed]
  16. The expression of 3-fucosylated-N-acetyl lactosamine carbohydrate determinants in renal tumours. Fleming, S., Brown, G. Histopathology (1987) [Pubmed]
  17. Heterogeneity of fibroblasts derived from human free and attached gingiva. Glycosaminoglycan synthesis and effects of phenytoin (PHT) treatment. Pagliarini, A., Stabellini, G., Carinci, F., Calura, G., Tognon, M., Evangelisti, R. J. Oral Pathol. Med. (1995) [Pubmed]
  18. Expression of epithelial membrane and 3-fucosyl-N-acetyllactosamine antigens in cervix uteri with particular reference to adenocarcinoma in situ. Rollason, T.P., Byrne, P., Williams, A., Brown, G. J. Clin. Pathol. (1988) [Pubmed]
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