Administration of FFP Repletes and Sustains the Megakaryocyte/Platelet-Derived Factor V Pool To Confer Hemostatic Competence in a Factor V-Deficient Individual.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 1779-1779 ◽  
Author(s):  
Beth A. Bouchard ◽  
John Chapin ◽  
Nigel S. Key ◽  
Paula B. Tracy

Abstract Recent studies by our laboratory have demonstrated unequivocally that factor V is endocytosed by megakaryocytes from plasma to form the platelet-derived factor V pool. In the current study, we have determined the time-dependent acquisition of factor V by platelets in a 67 year old factor V-deficient patient, previously shown to be completely devoid of plasma- and platelet-derived factor V. The patient now receives weekly tranfusions of two units of FFP to prevent gastrointestinal bleeding. Plasma and platelet lysate samples were prepared from fresh, whole blood drawn prior to (0 hrs), and following (2, 6, 24, 96, 168 hrs) patient transfusion. A factor V radioimmunoassay (RIA), which can detect factor V concentrations as low as 0.075 μg/mL, a standard factor V clotting-based activity assay, and/or western blotting analyses, which utilize a mixture of anti-human factor V light chain and heavy chain mAbs, were used to evaluate the appearance, and subsequent disappearance, of factor V in these two blood compartments. Prior to transfusion (t = 0 hr), the patient’s plasma-derived factor V could not be detected by any of the three factor V assays. The patient’s plasma-derived factor V level peaked immediately following transfusion (t = 2 hr) reaching a concentration of 1.3 +/− 0.08 μg/mL as measured by RIA, and declined until it reached an undetectable level at 96 hrs post transfusion. These data were confirmed by the results of both the clotting-based assays and western blotting analyses. As the patient’s platelet-derived factor V levels were below the sensitivity of both the RIA and clotting assay, they were analyzed by western blotting. Such analyses confirmed that subsequent to its endocytosis, the patient’s platelet-derived factor V is stored in a partially protelytically activated form similar to that of a control individual. Due to the partially proteolytically activated state of the platelet-derived cofactor, platelet lysates treated with thrombin to activate the factor V to factor Va were used for quantative western blotting. Interestingly, and perhaps consistent with the patient’s receipt of weekly FFP transfusions, factor V/Va could still be detected in platelets immediately prior to transfusion. Subsequent to transfusion and in marked contrast to changes in the plasma-derived cofactor pool, a significant increase in the patient’s platelet-derived factor V/Va level was not observed until 24 hrs post transfusion. These data are consistent with previous studies demonstrating that platelets do not endocytose factor V. Although the concentration of the platelet-derived factor V/Va pool decreased over the subsequent 6 days, antigen remained detectable even though the plasma-derived pool had been depleted 3 days earlier. These combined observations indicate that, subsequent to FFP administration, the patient’s megakaryocytes acquire and proteolytically process plasma-derived factor V normally. Furthermore, the consistent presence of factor V/Va within the patient’s platelets is in all likelihood preventing gastrointestinal bleeding in this individual, which supports the concept that platelet-derived factor V represents the hemostatically relevant factor V pool.

Blood ◽  
1983 ◽  
Vol 61 (6) ◽  
pp. 1060-1067 ◽  
Author(s):  
WB Foster ◽  
MM Tucker ◽  
JA Katzmann ◽  
RS Miller ◽  
ME Nesheim ◽  
...  

Abstract BALB/c mice were immunized with human factor V. The immunogen was a mixture of procofactor (factor V) and thrombin-activated cofactor (factor Va). Spleen cells were obtained from an immunized animal and fused with NS-1 murine myeloma cells. Hybrid cell cultures were assayed for the production of antibodies to human factor V and factor Va by a solid-phase radioimmunoassay. Factor V and/or factor-Va-specific antibodies were detected in 38 of the 96 cultures assayed. The cells from 10 of these positive cultures were subcloned by limiting dilution and grown as ascites tumors in BALB/c mice. Ascitic fluids were obtained and characterized with respect to their binding interaction with human factor V and factor Va. Three hybridoma cell lines produce monoclonal antibodies that react equally well with factor V and factor Va. Another antibody reacts with both antigens, but the reactivity with factor V is better than with factor Va. An additional two antibodies react with factor Va better than factor V in the radioimmunoassay (RIA). The remaining four antibodies react exclusively with factor V. A previously described murine monoclonal antibody to human factor V (alpha HFV-1) has been used to study the peptides produced during the thrombin-catalyzed activation of human factor V. This antibody binds both factor V and factor Va, releases them at high ionic strength, and has an apparent dissociation constant for factor Va of 3 x 10(-9)M. When human factor V (mol wt 330,000) is activated by thrombin and passed over an alpha HFV-1-Sepharose affinity resin, factor Va binds and subsequently can be eluted. The eluate in 1.2 M NaCl contains two fragments of apparent mol wt 93,000 and 70,000. EDTA, which inactivates factor Va, promotes release of the mol wt 93,000 fragment from factor Va bound to the antibody. Subsequent elution with 1.2 M NaCl releases the mol wt 70,000 fragment. These observations indicate that human factor Va is a two subunit protein and that the epitope for alpha HFV-1 is on the mol wt 70,000 fragment.


1999 ◽  
Vol 274 (26) ◽  
pp. 18635-18643 ◽  
Author(s):  
Kumudini R. Dharmawardana ◽  
Steven T. Olson ◽  
Paul E. Bock
Keyword(s):  
Factor V ◽  

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 4022-4022
Author(s):  
Debra A. Hoppensteadt ◽  
Vinod Bansal ◽  
Josephine Cunanan ◽  
Kuldeep Patel ◽  
Rakesh Wahi ◽  
...  

Abstract Several reports have described the presence of antibodies to bovine coagulation factors, such as factor V, prothrombin and factor X in plasma samples obtained from patients exposed to topical bovine thrombin. Other reports have also demonstrated the presence of anti-bovine coagulation factors in patients who have not been exposed to bovine thrombins, suggesting that anti-bovine protein antibodies can be generated in normal individuals. It has been suggested that surgical patients treated with topical bovine thrombin develop specific antibodies to bovine factor V which may be responsible for the bleeding and thrombotic complications. However, there is no definitive clinical study demonstrating a relationship between the apparent hemostatic defects and the presence of bovine factor Va antibodies. It was hypothesized that bovine factor Va antibodies are usually present in patients plasma because of the exposure to dietary bovine products. To test this hypothesis plasma samples from patients with end state renal disease (ESRD)(n=80), acute coronary syndrome (ACS)(n=160), burns (n=40) and healthy normal volunteers (n=140) were profiled for the presence of human factor V antigen (HFVA), bovine FVa antigen as measured by using a modified Elisa method and western blotting methods where bovine factor Va light chain fragment is used as a probe. In contrast to the normals (89±12%), the factor V antigen levels were found to be increased in the ESRD (148±30%), ACS (164±41%) and burn (145±27%) patients. Thus, there appears to be an up regulation of factor V antigen in these patients. All of the groups tested for the presence of immunoreactive material to the bovine factor Va light chain exhibited 2–3 ug/ml levels which were not significantly different. However, in the western blotting studies all groups exhibited cross reactivity with the factor Va light epitopes. There were bands present in the molecular weight range of 22, 36, 45 and 97 Kda in both the ESRD and burn patients. In the ACS patients there was an additional band observed at 166 Kda. These observations underscore the notion that bovine antifactor Va antibodies are non-specific and highly prevalent in both the surgical/interventional patients and normal population. A possible explanation for the presence of these antibodies is that most normal individual and patients problem are exposed to bovine proteins. Moreover, the higher prevalence of these antibodies in the ESRD and ACS patients may be due to additional exposure to heparin and aprotonin.


1987 ◽  
Author(s):  
B Dahlbäck ◽  
A LundWall

Coagulation factor V is a single chain, 330 kDa glycoprotein functioning as a cofactor to factor Xa in the activation of prothrombin. Thrombin cleaves factor V into four major fragments, out of which the N-terminal (105kDa) and the C-terminal (71-74kDa) fragments together constitute the active factor V species. To isolate cDNA clones a λ-gt 11 liver library was screened with a polyclonal, monospecific antiserum against human factor V. Four positive clones (two "weak", Aland A2 and two "strong", A3 and A4) were identified and isolated. Al(0.7kb), A2 (1.25kb) and A4 (0.85kb) reacted strongly with an antiserum against the 105 kDa, N-terminal fragment (heavy chain of factor Va), whereas A3 (1.25kb) gave the best signal with an antiserum against the 71-74 kDa, C-terminal fragment (light chain of factor Va). A1 hybridized with A2 and A4, whereas A2 only hybridized with Al. A3, which did not hybridize to any of the other clones, was used to rescreen the library and 9 positive clones (Bl-9) were isolated. B9 (3kb) coded for the entire C-terminal factor V fragment and the 3' noncoding sequence. B8 (1.8kb) partially overlapped B9 but extented the 5' sequence with 0.8kb. In a third screening round Al was used in combination with B8 and a 1.1 kb clone (CIO) was identified which hybridized to both. C10 did not hybridize with A2. The following overlapping cDNA clones can be orderedfrom the 5´end: A2-A1-C10-B8-B9 and together they cover 6 kb of coding sequence


Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 121-121
Author(s):  
Shekhar Kumar ◽  
Steven Stayrook ◽  
Rodney M. Camire ◽  
Sriram Krishnaswamy

Abstract Coagulation factor V (FV) circulates as an inactive procofactor with a domain organization of A1-A2-B-A3-C1-C2. Factor Va (FVa), the active cofactor, is produced in steps essential for rapid thrombin formation, by the proteolytic excision of the B domain which resolves the molecule into a heterodimer (A1-A2/A3-C1-C2). Removal of the B domain imbues the resulting FVa with the ability to bind factor Xa (Xa) on a membrane surface to assemble prothrombinase and greatly enhance the rate of thrombin formation. A recombinant variant of human factor V (HFVDT) with a shortened B domain exhibits constitutive cofactor activity. Cofactor activity even without proteolysis arises from its lack of a conserved basic region (BR) located in the large B domain of FV. Exogenously added BR peptide binds tightly to HFVDT in a Ca2+-dependent fashion and restores procofactor-like properties. The BR is proposed to restrict Xa binding and cofactor function by interacting with an acidic region at the C terminus of the B domain (AR2) and likely also an acidic sequence at the C terminus of the A2 domain (AR1). These two sequences are ~800 residues apart in FV with no structural information to explain how AR1 and AR2 might cooperate to engage the BR in the central portion of the B domain to autoinhibit FV. The available structures of an inactivated form of bovine factor Va (BFVai), of a FV ortholog from Pseudonaja textilis (FVPtex) and a lower resolution structure of B domainless human factor VIII (HFVIII) shed no light on this problem. We obtained diffraction quality crystals of HFVDT complexed with a single chain antibody (scFvE10) directed to FVa. Crystals were not obtained in the absence of scFvE10. The crystals diffracted to a resolution of 2.8 Å and the structure was solved by molecular replacement. The refined structure shows high similarity to BFVai, FVPtex and HFVIII. Insufficient electron density precluded the placement of scFvE10 in the modeled structure. The three homologous A domains in HFVDT adopt a typical cupredoxin-fold with the A domains arranged in a pseudo-three-fold axis of symmetry. The two C domains are cylindrical and oriented side-by-side to form the base of the A domain rosette. These features are equivalent to those seen in structures of BFVai, HFVIII and FVPtex. Two bound calcium ions are evident, one in A1 and the other in the A3 domain. The most important feature newly revealed in the structure of HFVDT is the close spatial proximity of AR1 and AR2 at the outer edge of the A domain rosette at the 3 o'clock position in the standard orientation. These acidic regions form adjacently positioned surfaces in spite of being bisected by the long primary sequence of the intervening B domain. Our observations provide the first structural evidence that the two distinct acidic regions come together in space to provide an extended surface. This provides a plausible explanation for how the BR in the middle of the B domain may bind to both AR1 and AR2 to restrict cofactor function in FV. The need for this extended but bipartite acidic surface, to which the BR may bind, also provides a plausible explanation for how proteolytic cleavage at position 1545 at the C terminus of AR2 destabilizes BR binding and results in cofactor formation. The Ca2+-stabilized loop in the A3 domain abuts the bisegmental acidic cluster potentially explaining why BR binding to HFVDT is strongly dependent on Ca2+. In the structure of FVPtex bound to snake venom factor X, AR1 extends away from the body of the cofactor to make intimate contacts with factor X. If this is mirrored in human prothrombinase, then our findings provide a structure-based model to phrase the long-standing procofactor activation paradox. BR binding to the AR1/AR2 extended surface ties up surfaces necessary for Xa binding and restricts cofactor activity. Proteolytic processing of the B domain and probably most importantly following AR2 destabilizes the BR/AR1/AR2 complex to free up surfaces including AR1 necessary to support Xa binding. This model reconciles the biochemical evidence with structural findings to provide new insights into the role played by the BR/AR1/AR2 complex in restricting Xa binding and cofactor function in FV. It provides a platform to further explore mechanistic details of FV and FVa function and for the development of novel strategies to modulate their functions to regulate thrombin formation for therapeutic gain. Disclosures Camire: Pfizer: Consultancy, Patents & Royalties, Research Funding; Novo Nordisk: Research Funding; Spark Therapeutics: Other: Scientific advisory board.


Blood ◽  
1983 ◽  
Vol 61 (6) ◽  
pp. 1060-1067 ◽  
Author(s):  
WB Foster ◽  
MM Tucker ◽  
JA Katzmann ◽  
RS Miller ◽  
ME Nesheim ◽  
...  

BALB/c mice were immunized with human factor V. The immunogen was a mixture of procofactor (factor V) and thrombin-activated cofactor (factor Va). Spleen cells were obtained from an immunized animal and fused with NS-1 murine myeloma cells. Hybrid cell cultures were assayed for the production of antibodies to human factor V and factor Va by a solid-phase radioimmunoassay. Factor V and/or factor-Va-specific antibodies were detected in 38 of the 96 cultures assayed. The cells from 10 of these positive cultures were subcloned by limiting dilution and grown as ascites tumors in BALB/c mice. Ascitic fluids were obtained and characterized with respect to their binding interaction with human factor V and factor Va. Three hybridoma cell lines produce monoclonal antibodies that react equally well with factor V and factor Va. Another antibody reacts with both antigens, but the reactivity with factor V is better than with factor Va. An additional two antibodies react with factor Va better than factor V in the radioimmunoassay (RIA). The remaining four antibodies react exclusively with factor V. A previously described murine monoclonal antibody to human factor V (alpha HFV-1) has been used to study the peptides produced during the thrombin-catalyzed activation of human factor V. This antibody binds both factor V and factor Va, releases them at high ionic strength, and has an apparent dissociation constant for factor Va of 3 x 10(-9)M. When human factor V (mol wt 330,000) is activated by thrombin and passed over an alpha HFV-1-Sepharose affinity resin, factor Va binds and subsequently can be eluted. The eluate in 1.2 M NaCl contains two fragments of apparent mol wt 93,000 and 70,000. EDTA, which inactivates factor Va, promotes release of the mol wt 93,000 fragment from factor Va bound to the antibody. Subsequent elution with 1.2 M NaCl releases the mol wt 70,000 fragment. These observations indicate that human factor Va is a two subunit protein and that the epitope for alpha HFV-1 is on the mol wt 70,000 fragment.


1995 ◽  
Vol 73 (04) ◽  
pp. 730-731 ◽  
Author(s):  
Katalin Váradi ◽  
Jan Rosing ◽  
Guido Tans ◽  
Hans Peter Schwarz

1999 ◽  
Vol 82 (11) ◽  
pp. 1462-1468 ◽  
Author(s):  
José Fernández ◽  
Jari Petäjä ◽  
John Griffin

SummaryUnfractionated heparin potentiates the anticoagulant action of activated protein C (APC) through several mechanisms, including the recently described enhancement of proteolytic inactivation of factor V. Possible anticoagulant synergism between APC and physiologic glycosaminoglycans, pharmacologic low molecular weight heparins (LMWHs), and other heparin derivatives was studied. Dermatan sulfate showed potent APC-enhancing effect. Commercial LMWHs showed differing abilities to promote APC activity, and the molecular weight of LMWHs correlated with enhancement of APC activity. Degree of sulfation of the glycosaminoglycans influenced APC enhancement. However, because dextran sulfates did not potentiate APC action, the presence of sulfate groups per se on a polysaccharide is not sufficient for APC enhancement. As previously for unfractionated heparin, APC anticoagulant activity was enhanced by glycosaminoglycans when factor V but not factor Va was the substrate. Thus, dermatan sulfate and LMWHs exhibit APC enhancing activity in vitro that could be of physiologic and pharmacologic significance.


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