Functional proteomic analysis of Ankaferd® Blood Stopper

Abstract

Objective: Ankaferd® Blood Stopper (ABS) comprises a standardized mixture of the plants Thymus vulgaris, Glycyrrhiza glabra, Vitis vinifera, Alpinia officinarum, and Urtica dioica. The basic mechanism of action for ABS is the formation of an encapsulated protein network that provides focal points for vital erythrocyte aggregation. ABSinduced protein network formation with blood cells, particularly erythrocytes, covers the primary and secondary hemostatic system without disturbing individual coagulation factors. Materials and Methods: To understand the effect mechanisms of ABS on hemostasis, a proteomic analysis using 2D gel electrophoresis and mass spectrometer was performed. Results: Proteins of plant origin in Ankaferd ® were NADP-dependent-malic enzyme, ribulose bisphosphatecarboxylase-large chain, maturase K, ATP synthase subunit-beta, ATP synthase subunit-alpha, chalcone-flavanone isomerase-1, chalcone-flavanone isomerase-2, and actin-depolymerizing factor. Furthermore, functional proteomic studies revealed that proteins resembling human peptides have been detected within Ankaferd ® , including ATP synthase, mucin-16 (CD164 sialomucin-like 2 protein), coiled-coil domain containing 141 hypothetical protein LOC283638 isoform 1, hypothetical protein LOC283638 isoform 2, dynactin 5, complex I intermediate-associated protein 30, mitochondrial, NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, TP synthase, H+ transporting, mitochondrial actin binding 1 isoform, LIM domain and actin binding 1 isoform a, LIM domain and actin binding 1 isoform b, spectrin alpha non erythrocytic 1, prolactin releasing hormone receptor, utrophin, tet oncogene family member 2 isoform b, protein phosphatase 1 regulatory subunit 12A, NIMA (never in mitosis gene a)-related kinase, ATP-binding cassette protein C12, Homo sapiens malic enzyme 1, mitochondrial NADP(+)-dependent malic enzyme 3, ME2 protein, nuclear factor 1 B-type, abhydrolase domain-containing protein 12B, E3 SUMO-protein ligase PIAS2, alpha-1, 2-glucosyltransferase ALG10-A, cofilin, non-muscle isoform, 18 kDa phosphoprotein, p18, actin-depolymerizing factor (ADF), twinfilin-1, ankyrin repeat and FYVE domain-containing protein 1, usherin precursor, urotensin II receptor, interleukin 4, and midkine. Conclusion: Proteomic analysis of Ankaferd ® represents a true basis for the upcoming Ankaferd ® studies focusing on its wound healing, hemostatic, anti-infective, antineoplastic, and preservative biological actions. (Turk J Hematol 2010; 27: 70-7)

Morphometric and Hormonal Study of the Effect of Utrica diocia Extract on Mammary Glands in Rats

“…This finding may indicate that Utrica diocia may induce more proliferation and more differentiation in mammary glands of all experimental groups when compared with their controls. These findings coincided with the results obtained by (Demiralp et al, 2010). Utrica diocia contains numerous antioxidants as well as phenolic and flavonoid compounds (Inic & Kujundzic, 2012), also flavonoids belong to such compounds called phytoestrogens (Papiez, 2004), and phytoestrogens are natural compounds derived from the plants that are structurally similar to estrogen (Panjeshahin et al, 2005).…”

Histopathological Alterations in the Kidney Tissue Following Topical Ankaferd Hemostat Application in a Rat Renal Injury Model

“…ABS also up-regulates GA-TA/FOG transcription system affecting erythroid functions and urotensin II. [4][5][6] Therefore, our results indicating red blood cell accumulation and siderophages following the use of ABS are compatible with the suggested 'mechanism-of-action' of ABS that ABS-induced formation of the protein network with vital erythroid aggregation covers the entire physiological hemostatic process. Further experimental search is needed to find out the molecules inside the ABS protein library leading to the ABSinduced aggregation at the renal tissue level.…”

“…Those proteins and the required ATP bioenergy are included in the ABS protein library. [4][5][6] Ankaferd also upregulates GATA/FOG transcription system affecting erythroid functions. Urotensin II is also an essential component of Ankaferd and represents the link between injured vascular endothelium, adhesive proteins, and active erythroid cells.…”

“…Those concepts have been developed via MALDI-TOF proteomic molecular analyses, cytometric arrays, transciption analysis, and SEM ultrastructural examinations as well as numerous investigations interacting with in vitro and in vivo research settings. 1,[3][4][5][6][7][8] ABS has many cellular effects. ABS has been shown to affect renal tubular apoptosis based on the level of hemorrhage.…”

The effects of Ankaferd Blood Stopper on transcription factors in HUVEC and erythrocyte protein profile

“…Vital erythroid aggregation occurs with spectrinankyrin and actin proteins on the membranes of red blood cells. Essential erythroid proteins (ankyrin recurrent and FYVE bundle-containing protein 1, spectrin alpha, actin depolymerizing factor, LIM bundle and actin-binding subunit 1 isoform a, LIM bundle and actin-binding subunit 1 isoform b, NADP-dependent malic enzyme, NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, mitochondrial NADP (+)-dependent malic enzyme 3, ribulose bisphosphate carboxylase large chain, and maturase K) and the required ATP bioenergy (ATP synthase, ATP synthase beta subunit, ATP synthase alpha subunit, ATP-binding protein C12, TP synthase H+ transporter protein, ADF, and alpha-1, 2-glycosyltransferase ALG10-A) are included in the ABS protein library [7]. The physiological protein profile of red blood cell membranes ( Figure 1) and the ABS protein library are similar [7]; therefore, vital erythroid aggregation is crucial to the ABS-induced hemostatic network.…”