Abstract: Disclosed are compositions for treating blood coagulation disorders and allows for manipulation of the blood coagulation cascade. More particularly the invention, relates to compositions for altering bleeding that include a mixture of at least one blood coagulation factor in a low dose and phospholipid vesicles. The invention has a variety of important uses including controlling bleeding in a mammal that has or is suspected of having a potentially life-threatening blood coagulation disorder.

Abstract: The present invention provides methods for inhibiting blood clotting. In general, the methods include adding corn trypsin inhibitor (CTI) to blood or a blood product in an amount sufficient to inhibit the clotting. The CTI can be used alone or in combination with other anti-coagulants. In one aspect, the invention features plasma clotting assays featuring substantially prolonged clotting times. Clotting assays using whole or minimally altered blood are also provided. Further provided are methods for storing blood or blood products at low temperature with the CTI.

Abstract: The present invention provides methods for inhibiting blood clotting. In general, the methods include adding corn trypsin inhibitor (CTI) to blood or a blood product in an amount sufficient to inhibit the clotting. The CTI can be used alone or in combination with other anti-coagulants. In one aspect, the invention features plasma clotting assays featuring substantially prolonged clotting times. Clotting assays using whole or minimally altered blood are also provided. Further provided are methods for storing blood or blood products at low temperature with the CTI.

Abstract: The present invention features isolated angiogenesis inhibitors having a molecular weight of between about 40 kDa to 50 kDa and having an amino acid sequence substantially similar to that of the amino acid sequence shown in SEQ ID NO. 2 or SEQ ID NO. 3. Further provided are methods of making and using the angiogenesis inhibitors, e.g., to inhibit vascularization or to block osteonectin and plasminogen interaction.

Abstract: Persons having the Factor VLEIDEN mutation and a lower than average plasma level of TFPI have been found to be at elevated risk of thrombosis. Prophylactic methods for reducing the risk of thrombosis employ the administration of TFPI to achieve higher levels in the plasma.

Abstract: Methods for detecting and/or quantifying catalytically-active, serine proteases in a biological fluid are disclosed. The methods are useful for measuring the active enzymes of the coagulation/fibrinolytic system and evaluating the system or components of the system as indicative of thrombosis-related disorders. The methods involve the combined use of halomethyl ketone probes having broad specificity for catalytically-active serine proteases and immunological reagents specific for serine proteases of particular types. The halomethyl ketone probes are active site specific; they are only incorporated into catalytically-active serine proteases. An antibody is used to provide specificity for the particular type of serine protease. By the combined active-site-specificity of the halomethyl ketone probes and the type-specificity of the antibody, the catalytically-active fraction of a particular serine protease is determined.

Abstract: Persons having the Factor V.sup.LEIDEN mutation and a lower than average plasma level of TFPI have been found to be at elevated risk of thrombosis. Prophylactic methods for reducing the risk of thrombosis employ the administration of TFPI to achieve higher levels in the plasma.

Abstract: Disclosed are methods, compositions and uses of bone precursor cells. Bone precursor cells are cells which are not hematopietic and which can differentiate into osteoblasts upon exposure to a bone growth factor and deposit calcium into the extracellular matrix. In addition, methods of differentiating bone precursor cells into osteoblasts are disclosed. Bone precursor cells are useful in the treatment of certain bone related disorders and diseases such as, promoting fracture repair.

Abstract: The present invention is directed to immunochemical detection procedures, e.g., using both Western blotting and direct immunoassays, for fragments of Factor Va, which can thus be used; (a) in a predictive manner to evaluate the existence and/or extent of a thrombotic complication; (b) to monitor the efficacy of prophylaxis for a thrombotic condition; and (c) as a means to evaluate potential risk of hemorrhage during thrombolytic therapy.

Abstract: The present invention encompasses compounds of formula I: ##STR1## and the pharmaceutically acceptable non-toxic salts thereof; wherein R.sub.1 is hydrogen, lower alkyl, alkenyl, alkynyl, cycloalkyl, alkylcycloalkyl, cycloalkylalkyl, or phenylalkyl;R.sub.2 is hydrogen, alkyl, alkenyl, alkynyl, cycloalkyl, alkylcycloalkyl, cycloalkylalkyl, or phenylalkyl; orNR.sub.1 R.sub.2 forms a nitrogen heterocycle; andR.sub.3 is hydrogen, an amino acid or a peptide residue.These compounds may be employed as substrates in assays for determining proteolytic enzyme activity or as enzyme inhibitors. The invention also encompasses methods for determining proteolytic enzyme activity using the compounds of formula I.

Abstract: A novel human megakaryocytopoietic growth promoting activity factor capable of stimulating the growth of megakaryocytes and augments the differentiation or maturation of megakaryocytes. Also provided are processes for obtaining the factor in homogeneous form and producing it by recombinant genetic engineering techniques.

Abstract: The present invention is directed to immunochemical detection procedures, e.g., using both Western blotting and direct immunoassays, for Factor V/Va and Factor V/Va fragments, which can thus be used; (a) in a predictive manner to evaluate the existence and/or extent of a thrombotic complication; (b) to monitor the efficacy of prophylaxis for a thrombotic condition; and (c) as a means to evaluate potential risk of hemorrhage during thrombolytic therapy.

Abstract: Factor VIII:C deficiency in a hemophilic mammal may be bypassed by infusion of a synergistic mixture of a phospholipid and Factor Xa so that the cascade process of blood clotting may continue. The proportions of phospholipid and Factor Xa in the mixture are critical as too little Xa has no effect while too much is toxic (thrombogenic). Infusion of the phosphilipid-Factor Xa mixture into normal mammals enhances the natural clotting rate and provides a method for rapidly controlling bleeding in emergency situations.

Abstract: A composition of matter for controlling Hemophilia A (Antihemophilic Factor (F. VIII:C) deficiency) in mammals is described. Factor VIII:C deficiency in the mammal is bypassed by infusion of a synergistic mixture of a phospholipid and Factor Xa so that the cascade process of blood clotting may continue. The proportions of phospholipid and Factor Xa in the mixture are critical as too little Xa has no effect while too much is toxic (thrombogenic).

Abstract: A method for controlling HemophiliaA (Antihemophilic Factor (F. VIII:C) deficiency) in mammals is described. Factor VIII:C deficiency in the mammal is bypassed by infusion of a synergistic mixture of a phospholipid and Factor Xa so that the cascade process of blood clotting may continue. The proportions of phospholipid and Factor Xa in the mixture are critical as too little Xa has no effect while too much is toxic (thrombogenic).