Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 1 to 10 of 11

Publication Record

Connections

Females with FVIII and FIX deficiency have reduced joint range of motion.
Sidonio RF, Mili FD, Li T, Miller CH, Hooper WC, DeBaun MR, Soucie M, Hemophilia Treatment Centers Network
(2014) Am J Hematol 89: 831-6
MeSH Terms: Adolescent, Adult, Aged, Body Mass Index, Case-Control Studies, Child, Child, Preschool, Cross-Sectional Studies, Demography, Factor IX, Factor VIII, Female, Hemophilia A, Hemophilia B, Humans, Joints, Middle Aged, Range of Motion, Articular, Severity of Illness Index
Show Abstract · Added October 7, 2014
Little is known about rates of joint bleeding among females with FVIII/FIX deficiency or hemophilia carriers. In a cross-sectional study, we tested the hypothesis that females with FVIII or FIX deficiency enrolled in the Universal Data Collection (UDC) project had a reduced mean overall joint range of motion (ROM) compared with historic controls from the Normal Joint Study. Demographics, clinical characteristics, and joint ROM measurements on 303 females without a bleeding disorder and 148 females with FVIII and FIX deficiency, respectively, between the ages of 2-69 years and a body mass index (BMI) ≤ 35 were compared. Multivariate linear regression was performed with the overall joint ROM (sum of the right and left ROM measurements of five joints) as the dependent variable and FVIII or FIX activity as the independent variable adjusting for age, race, BMI, and number of joint bleeds reported over the last 6 months. As FVIII and FIX activity decreased, the mean overall joint ROM became reduced and in most cases was significantly lower than that of the controls regardless of age and clinical hemophilia severity. Further investigation of reduced joint ROM as evidence of subclinical joint bleeding in females with FVIII and FIX deficiency is warranted.
© 2014 Wiley Periodicals, Inc.
0 Communities
1 Members
0 Resources
19 MeSH Terms
Both hemophilia health care providers and hemophilia a carriers report that carriers have excessive bleeding.
Paroskie A, Oso O, Almassi B, DeBaun MR, Sidonio RF
(2014) J Pediatr Hematol Oncol 36: e224-30
MeSH Terms: Adult, Cross-Sectional Studies, Data Collection, Factor VIII, Female, Health Personnel, Hemophilia A, Hemorrhage, Heterozygote, Humans, Male, Middle Aged, Surveys and Questionnaires
Show Abstract · Added February 19, 2014
INTRODUCTION - Hemophilia A, the result of reduced factor VIII activity, is an X-linked recessive bleeding disorder. Previous reports of hemophilia A carriers suggest an increased bleeding tendency. Our objective was to determine the attitudes and understanding of the hemophilia A carrier bleeding phenotype, and opinions regarding timing of carrier testing from the perspective of both medical providers and affected patients. Data from this survey were used as preliminary data for an ongoing prospective study.
MATERIALS AND METHODS - An electronic survey was distributed to physicians and nurses employed at Hemophilia Treatment Centers, and hemophilia A carriers who were members of Hemophilia Federation of America. The questions focused on the clinical understanding of bleeding symptoms and management of hemophilia A carriers, and the timing and intensity of carrier testing.
RESULTS - Our survey indicates that 51% (36/51) of providers compared with 78% (36/46) of carriers believe that hemophilia A carriers with normal factor VIII activity have an increased bleeding tendency (P<0.001); 72% (33/36) of hemophilia A carriers report a high frequency of bleeding symptoms. Regarding carrier testing, 72% (50/69) of medical providers recommend testing after 14 years of age, conversely 65% (29/45) of hemophilia A carriers prefer testing to be done before this age (P<0.001).
DISCUSSION - Hemophilia A carriers self-report a higher frequency of bleeding than previously acknowledged, and have a preference for earlier testing to confirm carrier status.
0 Communities
1 Members
0 Resources
13 MeSH Terms
Immunohistochemistry in the evaluation of neovascularization in tumor xenografts.
Wang D, Stockard CR, Harkins L, Lott P, Salih C, Yuan K, Buchsbaum D, Hashim A, Zayzafoon M, Hardy RW, Hameed O, Grizzle W, Siegal GP
(2008) Biotech Histochem 83: 179-89
MeSH Terms: Animals, Antibodies, Cell Line, Tumor, Factor VIII, Female, Humans, Immunohistochemistry, Mice, Mice, Inbred BALB C, Microvessels, Neoplasms, Neovascularization, Pathologic, Platelet Endothelial Cell Adhesion Molecule-1, Transplantation, Heterologous
Show Abstract · Added March 21, 2014
Angiogenesis, or neovascularization, is known to play an important role in the neoplastic progression leading to metastasis. CD31 or Factor VIII-related antigen (F VIII RAg) immunohistochemistry is widely used in experimental studies for quantifying tumor neovascularization in immunocompromised animal models implanted with transformed human cell lines. Quantification, however, can be affected by variations in the methodology used to measure vascularization including antibody selection, antigen retrieval (AR) pretreatment, and evaluation techniques. To examine this further, we investigated the microvessel density (MVD) and the intensity of microvascular staining among five different human tumor xenografts and a mouse syngeneic tumor using anti-CD31 and F VIII RAg immunohistochemical staining. Different AR methods also were evaluated. Maximal retrieval of CD31 was achieved using 0.5 M Tris (pH 10) buffer, while maximum retrieval of F VIII RAg was achieved using 0.05% pepsin treatment of tissue sections. For each optimized retrieval condition, anti-CD31 highlighted small vessels better than F VIII RAg. Furthermore, the MVD of CD31 was significantly greater than that of F VIII RAg decorated vessels (p<0.001). The choice of antibody and AR method has a significant affect on immunohistochemical findings when studying angiogenesis. One also must use caution when comparing studies in the literature that use different techniques and reagents.
0 Communities
1 Members
0 Resources
14 MeSH Terms
Reduction of the antigenicity of factor VIII toward complex inhibitory antibody plasmas using multiply-substituted hybrid human/porcine factor VIII molecules.
Barrow RT, Healey JF, Gailani D, Scandella D, Lollar P
(2000) Blood 95: 564-8
MeSH Terms: Animals, Cross Reactions, Dimerization, Factor VIII, Factor Xa, Hemophilia A, Humans, Macromolecular Substances, Protein Multimerization, Recombinant Proteins, Reference Values, Swine, Thrombin
Show Abstract · Added May 19, 2014
Factor VIII (fVIII) circulates as a heavy chain/light chain (A1-A2-B/ap-A3-C1-C2) heterodimer. The 41-residue light chain activation peptide, ap, is cleaved from fVIII during proteolytic activation by thrombin or factor Xa. We constructed 7 active recombinant hybrid B-domainless human/porcine fVIII molecules that contained combinations of porcine sequence replacements within the A2, ap-A3, and C2 domains. The cross-reactivity of 23 high-titer inhibitory antibodies between human fVIII and the hybrids was inversely related to the degree of porcine substitution. In all plasmas, the substitution of all 3 regions yielded cross-reactivities that were not significantly different from those of porcine fVIII. To differentiate between inhibitor binding to the ap region and the A3 domain, we constructed 2 additional hybrids that contained porcine A2 and C2 domain substitutions and either porcine A3 or porcine ap substitutions. The porcine ap segment was less antigenic than the human ap segment in several plasmas that had activity against the ap-A3 region. This indicates that some inhibitor plasmas contain antibodies directed against the fVIII ap segment in addition to A2, A3, and C2 domain epitopes identified in previous studies. Substitution of porcine sequences within the A2, A3, C2, and ap regions of human fVIII is necessary and sufficient to achieve a maximal reduction in antigenicity relative to porcine fVIII with respect to most inhibitory antibody plasmas. (Blood. 2000;95:564-568)
0 Communities
1 Members
0 Resources
13 MeSH Terms
Expression patterns of adhesion receptors in the developing mouse lung: functional implications.
Buck CA, Edelman JM, Buck CE, Kennedy G, Baldwin HS
(1996) Cell Adhes Commun 4: 69-87
MeSH Terms: Actins, Animals, Antigens, CD, Bronchi, Cell Adhesion Molecules, Endothelium, Factor VIII, Gene Expression Regulation, Developmental, Gestational Age, Integrin alpha4, Integrin alpha6, Integrins, Intercellular Adhesion Molecule-1, Lung, Mice, Morphogenesis, Muscle, Smooth, Muscle, Smooth, Vascular, Neovascularization, Physiologic, Platelet Endothelial Cell Adhesion Molecule-1, Thrombin, Thrombomodulin, Vascular Cell Adhesion Molecule-1
Show Abstract · Added June 11, 2010
A detailed, immunohistological study of mouse lung development from the first appearance of primary lung buds off the laryngo tracheal groove through the formation of the mature, adult lung has been carried out using monoclonal antibodies specific for endothelial cells, smooth muscle cells, adhesion receptors and markers of mature endothelial cell function. These included mAbs specific for PECAM-1, alpha-smooth muscle actin, ICAM-1, ICAM-2, VCAM-1, alpha 4 and alpha 6 integrin subunits, thrombomodulin and factor VIII. The results document a dynamic pattern of receptor expression and indicate that the expansion of the pulmonary vascular system may take place by both angiogenic and vasculogenic processes. They further document differences in receptor expression by vascular and airway smooth muscle. ICAM-1 expression was primarily extravascular during development. The expression patterns of alpha 4 integrin and its counter receptor VCAM-1 lacked the complementarity that might be expected if they were functioning as a receptor/counter-receptor pair in lung development. Thrombomodulin expression patterns support a major role for the thrombin/ thrombomodulin system in lung development. The expression of thrombomodulin only at sites of airway branching suggests that the thrombin/thrombomodulin system could play a pivotal, regulatory role in branching morphogenesis.
1 Communities
1 Members
0 Resources
23 MeSH Terms
Anti-transforming growth factor (TGF)-beta antibodies inhibit breast cancer cell tumorigenicity and increase mouse spleen natural killer cell activity. Implications for a possible role of tumor cell/host TGF-beta interactions in human breast cancer progression.
Arteaga CL, Hurd SD, Winnier AR, Johnson MD, Fendly BM, Forbes JT
(1993) J Clin Invest 92: 2569-76
MeSH Terms: Animals, Antibodies, Breast Neoplasms, Cell Division, Collagen, Cytotoxicity, Immunologic, Factor VIII, Female, Humans, Immunoglobulin G, Killer Cells, Natural, Lung Neoplasms, Mice, Mice, Nude, Neoplasm Metastasis, Neoplasm Transplantation, Neovascularization, Pathologic, Recombinant Proteins, Spleen, Transforming Growth Factor beta, Transplantation, Heterologous, Tumor Cells, Cultured
Show Abstract · Added March 5, 2014
TGF-beta effects on angiogenesis, stroma formation, and immune function suggest its possible involvement in tumor progression. This hypothesis was tested using the 2G7 IgG2b, which neutralizes TGF-beta 1, -beta 2, and -beta 3, and the MDA-231 human breast cancer cell line. Inoculation of these cells in athymic mice decreases mouse spleen natural killer (NK) cell activity. Intraperitoneal injections of 2G7 starting 1 d after intraperitoneal inoculation of tumor cells suppressed intraabdominal tumor and lung metastases, whereas the nonneutralizing anti-TGF-beta 12H5 IgG2a had no effect. 2G7 transiently inhibited growth of established MDA-231 subcutaneous tumors. Histologically, both 2G7-treated and control tumors were identical. Intraperitoneal administration of 2G7 resulted in a marked increase in mouse spleen NK cell activity. 2G7 did not inhibit MDA-231 primary tumor or metastases formation, nor did it stimulate NK cell-mediated cytotoxicity in beige NK-deficient nude mice. Finally, serum-free conditioned medium from MDA-231 cells inhibited the NK cell activity of human blood lymphocytes. This inhibition was blocked by the neutralizing anti-TGF-beta 2G7 antibody but not by a nonspecific IgG2. These data support a possible role for tumor cell TGF-beta in the progression of mammary carcinomas by suppressing host immune surveillance.
0 Communities
1 Members
0 Resources
22 MeSH Terms
Adsorption of von Willebrand factor/factor VIII by the genetically distinct interstitial collagens.
Santoro SA
(1981) Thromb Res 21: 689-91
MeSH Terms: Adsorption, Antigens, Blood Coagulation Factors, Calmodulin, Collagen, Factor VIII, Humans, Serotonin, von Willebrand Factor
Added March 5, 2014
1 Communities
1 Members
0 Resources
9 MeSH Terms
Preferential binding of high molecular weight forms of von Willebrand factor to fibrillar collagen.
Santoro SA
(1983) Biochim Biophys Acta 756: 123-6
MeSH Terms: Animals, Blood Coagulation Factors, Collagen, Factor VIII, Humans, Immunoelectrophoresis, Two-Dimensional, Molecular Weight, Protein Binding, Rats, von Willebrand Factor
Show Abstract · Added March 5, 2014
The time- and concentration-dependent binding of von Willebrand factor to fibrillar collagen was examined by following the disappearance from plasma of ristocetin cofactor activity and factor VIII-related antigen, the functional and immunologic determinants of von Willebrand factor. Examination of both bound and unbound factor VIII-related antigen by crossed immunoelectrophoresis revealed a preferential binding of the higher molecular weight forms of von Willebrand factor to fibrillar collagen.
1 Communities
1 Members
0 Resources
10 MeSH Terms
Thrombin-induced exposure and prostacyclin inhibition of the receptor for factor VIII/von Willebrand factor on human platelets.
Fujimoto T, Ohara S, Hawiger J
(1982) J Clin Invest 69: 1212-22
MeSH Terms: Binding Sites, Antibody, Blood Platelets, Bucladesine, Chymotrypsin, Edetic Acid, Epoprostenol, Factor VIII, Glutaral, Humans, Membrane Proteins, Platelet Membrane Glycoproteins, Prostaglandins, Receptors, Cell Surface, Thrombin, Time Factors
Show Abstract · Added December 10, 2013
The receptor for Factor VIII/von Willebrand factor (F. VIIIVWF) is readily available on circulating platelets. We have found that the stimulation of platelets with traces of thrombin at concentrations that are generated physiologically (0.008 U-0.05 U/ml) induced concentration-dependent binding of 125I-labeled F. VIIIVWF in a steady-state system. The binding induced by thrombin was specific because it was inhibited by a 100-fold molar excess of unlabeled F. VIIIVWF factor, by rabbit monospecific antibody against Factor VIII, and was not inhibited by an excess of fibrinogen or fibronectin. Binding induced by thrombin required metabolically active platelets, in contrast to a system with ristocetin that also prompted binding to glutaraldehyde-treated platelets. The thrombin effects on binding of 125I-F. VIIIVWF was not observed when platelets were washed with EDTA-containing buffers; EDTA and EGTA both inhibited thrombin-induced binding. Platelet membrane glycoproteins were required because enzymatic stripping od them from the platelet surface with chymotrypsin reduced binding 2.5-5.0-fold. Prostacyclin, in the concentration range of 1 to 50 nM, had two distinct effects on the receptor for F. VIIIWVF: (a) it prevented exposure of this receptor when added 10 min before thrombin, and (b) it reversed the binding of 125I-F. VIIIVWF to the platelet receptor when added 30 min after thrombin and the ligand, ie., when binding was at equilibrium. The dual effect of prostacyclin on the receptor for F. VIIIVWF was reproduced by dibutyryl cyclic AMP.
0 Communities
1 Members
0 Resources
15 MeSH Terms
Evaluation of ristocetin-Willebrand factor assay and ristocetin-induced platelet aggregation.
Olson JD, Brockway WJ, Fass DN, Magnuson MA, Bowie EJ
(1975) Am J Clin Pathol 63: 210-8
MeSH Terms: Anticoagulants, Antigens, Blood Coagulation Disorders, Blood Coagulation Factors, Blood Platelets, Factor VIII, Humans, Platelet Adhesiveness, Platelet Aggregation, Ristocetin, von Willebrand Diseases
Show Abstract · Added February 23, 2011
Normal subjects, patients with various bleeding disorders, and patients with von Willebrand's disease were studied. All patients with von Willebrand's disease had decreased levels of ristocetin-Willebrand factor (range, 0 to 41%) as compared with all other subjects (range, 79 to 202%). Ristocetin-induced platelet aggregation of platelet-rich plasma was abnormal in all patients with von Willebrand's disease tested, and it was possible to correct this abnormal response by addition of normal platelet-poor plasma. Abnormal ristocetin-induced platelet aggregation was seen in patients with intrinsic platelet disorders or, on some occasions, in normal patients who had ingested aspirin. Ristocetin-induced platelet aggregation is not diagnostic, but it may be useful as a simple screening test for patients with possible von Willebrand's disease. In conjunction with other tests, the assay for ristocetin-Willebrand factor will be useful in diagnosis and evaluation of these patients.
1 Communities
1 Members
0 Resources
11 MeSH Terms