Although within the normal range, the increased numbers of WBCs and neutrophils in patients with SCF suggest that SCF may be a subclinical inflammatory condition. Furthermore, increased RDW and PDW in SCF patients may cause microvascular blood flow resistance due to impaired cell deformability. The PCT provides reliable data regarding total platelet mass and may be a useful predictor of SCF.

Oral mucositis, characterized by ulcerative lesions in the oral mucosa of patients undergoing chemotherapy, is currently considered to be the most severe complication of anti-cancer therapy which is affecting 40-80% of those patients. Ankaferd hemostat, (ABS) is the first topical hemostatic agent regarding the red blood cell (RBC)-fibrinogen interactions tested in the clinical trials. ABS also has pleiotropic effects particularly in the tissue healing and has anti-infective properties. The aim of this study is to assess the safety and efficacy of ABS in the management of chemotherapy-induced oral mucositis in adult patients with hematological malignancies. ABS was topically applied to the patients with grade 3-4 mucositis according to the WHO classification. Patients were said to mouthwash and swallow the five milliliters of ABS. Twenty patients with oral mucositis were evaluated. Eleven patients with acute myeloid leukemia, four acute lymphoblastic leukemia, three non-hodgkin lymphoma, one hemophagocytosis with acute myleoid leukemia and one hemophagocytosis were included in study. Median extract amount was calculated as 74.50 ml (30-100 ml) and median healing time was 6.6 days (3-10). Consequently, ABS is an effective agent in the treatment of chemotherapy related severe oral mucositis in patients with hematological malignancies. Further experimental and clinical trials about ABS shall focus on the interrelationships between proteomic content, fibrinogen gamma, and vital erythroid aggregation due to ABS.

Ankaferd blood stopper is a standardized mixture of the plants Thymus vulgaris, Glycyrrhiza glabra, Vitis vinifera, Alpinia officinarum, and Urtica dioica and has been used as a topical hemostatic agent and with its clinical application established in randomized controlled trials and case reports. Ankaferd has been successfully used in gastrointestinal endobronchial mucosal and cutaneous bleedings and also in abdominal, thoracic, dental and oropharyngeal, and pelvic surgeries. Ankaferd’s hemostatic action is thought to form a protein complex with coagulation factors that facilitate adhesion of blood components. Besides its hemostatic action, Ankaferd has demonstrated pleiotropic effects, including anti-neoplastic and anti-microbial activities and tissue-healing properties; the underlying mechanisms for these have not been well studied. Ankaferd’s individual components were determined by proteomic and chemical analyses. Ankaferd also augments transcription of some transcription factors which is shown with transcriptomic analysis. The independent effects of these ingredients and augmented transcription factors are not known precisely. Here, we review what is known of Ankaferd blood stopper components from chemical, proteomic, and transcriptomic analyses and propose that individual components can explain some pleiotropic effects of Ankaferd. Certainly more research is needed focusing on individual ingredients of Ankaferd to elucidate their precise and effects.

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. ABS–induced protein network formation with blood cells particularly erythrocytes covers the primary and secondary haemostatic system without disturbing individual coagulation factors (Figure 1). The aim of this study is to perform functional proteomic analyses of ABS, which has been approved for the management of hemorrhages in Turkey (www.ankaferd.com). The protein samples for 2D gel electrophoresis were prepared: 10 ml of Ankaferd solution was precipitated with Trichloroacetic Acid Precipitation (TCA). 100 μl of 100% TCA. was added for each 1ml of sample. The total protein concentration was measured using the BCA protein assay Kit (Pierce, Rockford, USA). 2D Gel Electrophoresis of Proteins were performed. Gels were stained with SYPRO Ruby protein stain and images were acquired and analyzed using PDQuest software (Bio-Rad Laboratories, USA). Gel Digestion of Proteins: Selected spots from the gel were excised using a Proteome Works Spot Cutter (Bio-Rad Laboratories, USA) and transferred to a 96-well plate. The proteins were enzymatically digested and the tryptic peptides ZipTip (Millipore, France) purified. After ZipTip purification, the tryptic peptides were eluted from the ZipTip with 2 mg/ml cyano-4-hydroxycinnamic acid (CHCA) solution in 50% ACN/0.1% TriFlora acetic acid and spotted directly onto wax-coated matrix-assisted laser desorption/ionization (MALDI) target plates. Mass Spectrometry & Database Search: The tryptic peptides on the MALDI target plate were analyzed with MasLynx MALDI-time of flight mass spectrometer (Waters, UK). Mass spectra were recorded in the positive-ion mode. All spectra were acquiredwith external calibration of sub-P, anjiotensin, renine, ACTH and glu fib mix. PLGS (Waters, UK). Was optained with Swiss-Prot data base. With 50 ppm sensitivity. Proteins were evaluated by considering the number of matched tryptic peptides, the percentage coverage of the entire protein sequence, the apparent MW, and the pI of the protein. Results: Proteins of plant origin in Ankaferd were NADP-dependent malic enzyme, Ribulose bisphosphate carboxylase large chain, Mturase K, ATP synthase subunit beta, ATP synthase subunit alpha, Chalcone-flavonone isomerase 1, Chalcone-flavonone isomerase 2, and Actin-depolymerizing factor. Furthermore, functional proteomics 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 kinas, 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. Those proteins represent a true basis for the upcoming Ankaferd studies focusing on its wound healing hemostatic, anti-infective, preservative biological actions. Figure Figure

Atraumatic osteonecrosis has been associated with a variety of clinical conditions including corticosteroid usage, alcoholism, infections, hyperbaric events, storage disorders, marrow-infiltrating diseases, coagulation defects, and some autoimmune diseases. Osteonecrosis due to thrombophilia is an extremely rare condition with only few cases reported previously in the literature. Hormone-replacement therapies cause increased risk of venous thrombosis, probably by causing a synergistic effect with inherited clotting defects. In this article, we report a young female with Turner syndrome, who developed avascular necrosis of the femoral head during treatment with oral estrogen, which was associated with low protein S levels.