Abstract: Methods for repurposing a therapeutically effective amount of drugs that reduce circulating testosterone levels and/or activity (androgen-deprivation drugs) for treating, ameliorating, and/or preventing progression of dilated cardiomyopathy and heart failure. Reduction in circulating testosterone levels and/or activity is effective for treating, ameliorating, and/or preventing progression of dilated cardiomyopathy and/or heart failure in the subject.

Abstract: Methods of using measured plasma renin activity assayed (PRA), plasma renin activity concentration (PRAC), active renin concentration (ARC), plasma renin activity concentration (PRAC) and/or active plasma renin concentration (APRC), pro-renin activity, (pro)-renin receptor (PRR) levels for diagnosing, prognosing, treating and monitoring heart failure (HF) or HF-associated conditions or other conditions that cause or are caused by altered (e.g., elevated) renin activity, pro-renin levels, PRR levels, PRC, APRC, and/or interaction of renin or pro-renin with PRR. These methods can be used for at-risk patients for personalized therapy of heart disease to reduce heart dysfunction progression, diminish HF, and prolong life. This technology stratifies patients with HF or those at risk for HF to determine the appropriate medication (agents that specifically interfere with plasma renin activity/pro-renin and/or PRR) or intervention and the appropriate dosage of medication to treat further HF progression.

Abstract: Methods of utilizing quantitative magnetic resonance (QMR) to non-invasively determine and quantify body fluid dynamics [e.g., extracellular water and total water levels] and body compositions (e.g., lean muscle mass and fat mass levels). These levels or changes therein are used as biomarkers to diagnose, prognose, tailor and monitor treatment for conditions that cause or caused by ECW retention (edema), lean muscle mass loss (sarcopenia), and/or fat loss (cachexia), including heart failure (HF) and HF-associated and HF-non-associated edema/sarcopenia/cachexia, kidney disease, liver disease, and other HF complications. Body fluid dynamics and body compositions measurements obtained from QMR technology are used as biomarkers to help a physician's assessment to determine the prognosis and personalized treatment strategies that are tailored for individual patients with heart dysfunction and/or HF, HF-associated conditions, and/or other conditions that cause or caused by edema, sarcopenia, and/or cachexia.

Abstract: A molecule that binds specifically to a human tissue plasminogen activator (TPA) or a TPA mutant is provided. The molecule having sub-nanomolar affinity to inhibit fibrin-dependent plasminogen activation with an IC50<5 nM, to inhibit degradation of human fibron clots without affecting TPA amidolytic activity or non-fibrin-dependent activation, and the amino acid sequence of the TPA mutant is at least 65% identical to SEQ ID NO: 1 or SEQ ID NO: 2. Further provided is a method for treating systemic bleeding and brain hemorrhage after TPA treatment in a patient in need of such treatment. The method comprises administering to said patient an effective amount of the molecule, wherein the molecule selectively inhibits fibrin-augmented plasminogen activation in the patient.

Abstract: A molecule that binds specifically to a human tissue plasminogen activator (TPA) or a TPA mutant is provided. The molecule having sub-nanomolar affinity to inhibit fibrin-dependent plasminogen activation with an IC50<5 nM, to inhibit degradation of human fibron clots without affecting TPA amidolytic activity or non-fibrin-dependent activation, and the amino acid sequence of the TPA mutant is at least 65% identical to SEQ ID NO: 1 or SEQ ID NO: 2. Further provided is a method for treating systemic bleeding and brain hemorrhage after TPA treatment in a patient in need of such treatment. The method comprises administering to said patient an effective amount of the molecule, wherein the molecule selectively inhibits fibrin-augmented plasminogen activation in the patient.

Abstract: A molecule that binds specifically to a human tissue plasminogen activator (TPA) or a TPA mutant is provided. The molecule having sub-nanomolar affinity to inhibit fibrin-dependent plasminogen activation with an IC50<5 nM, to inhibit degradation of human fibrin clots without affecting TPA amidolytic activity or non-fibrin-dependent activation, and the amino acid sequence of the TPA mutant is at least 65% identical to SEQ ID NO: 1 or SEQ ID NO: 2. Further provided is a method for treating systemic bleeding and brain hemorrhage after TPA treatment in a patient in need of such treatment. The method comprises administering to said patient an effective amount of the molecule, wherein the molecule selectively inhibits fibrin-augmented plasminogen activation in the patient.

Abstract: A molecule that binds specifically to a human tissue plasminogen activator (TPA) or a TPA mutant is provided. The molecule having sub-nanomolar affinity to inhibit fibrin-dependent plasminogen activation with an IC50<5 nM, to inhibit degradation of human fibrin clots without affecting TPA amidolytic activity or non-fibrin-dependent activation, and the amino acid sequence of the TPA mutant is at least 65% identical to SEQ ID NO: 1 or SEQ ID NO: 2. Further provided is a method for treating systemic bleeding and brain hemorrhage after TPA treatment in a patient in need of such treatment. The method comprises administering to said patient an effective amount of the molecule, wherein the molecule selectively inhibits fibrin-augmented plasminogen activation in the patient.

Abstract: A substantially pure platelet activation polypeptide including a sequence at least 70% identical to SEQ ID NO:1, and a DNA encoding such a polypeptide.

Abstract: A substantially pure platelet activation polypeptide including a sequence at least 70% identical to SEQ ID NO:1, and a DNA encoding such a polypeptide.

Abstract: Novel immunoinhibitors are capable of inhibiting thrombin-activated function of Factor XIII by binding to Factor XIII at a site other than the thrombin-cleavage site of Factor XIII.