35 results about "Cardiac myosin" patented technology

Certain substituted urea derivatives selectively modulate the cardiac sarcomere, for example by potentiating cardiac myosin, and are useful in the treatment of systolic heart failure including congestive heart failure.

Peptide constructs including a first peptide segment which includes an amino acid sequence associated with autoimmune disease, asthma, allergy or xeno- or allograft transplantation rejections bonded directly or via a linker or spacer to a second peptide which binds to T cells and which will redirect the immune response from a harmful Th1 response to a less harmful Th2 response, or which will bind to T cells to initiate, but not complete, an immune response causing the T cells to which the first peptide binds, to undergo anergy and apoptosis, are useful in treating autoimmune conditions. For instance, the peptide construct NGQEEKAGVVSTGLIGGGDSAFDVLSFTAEEKAGVYK (SEQ ID NO:14) wherein Th2 stimulating Peptide G (SEQ ID NO:15) is covalently linked, via spacer GGG, to cardiac myosin molecule My1 (SEQ ID NO:16), can be used for treatment or prevention of myocarditis.

The invention pertains to methods for detecting the presence or absence of a mutation associated with hypertrophic cardiomyopathy (HC). The methods include providing DNA which encodes a cardiac myosin binding protein and detecting the presence or absence of a mutation in the amplified product which is associated with HC. The invention further pertains to methods for diagnosing HC in a subject. These methods typically include obtaining a sample of DNA which encodes a cardiac myosin binding protein from a subject being tested for FHC and diagnosing the subject for FHC by detecting the presence or absence of a mutation in the sarcomeric thin filament protein which causes FHC as an indication of the disease. Other aspects of the invention include kits useful for diagnosing HC and methods for treating HC.

Certain substituted sulfonamide derivatives selectively modulate the cardiac sarcomere, for example by potentiating cardiac myosin, and are useful in the treatment of systolic heart failure including congestive heart failure.

The invention pertains to methods for detecting the presence or absence of a mutation associated with hypertrophic cardiomyopathy in cats, particularly domesticated cats, and more particularly Maine Coon cats. The methods include detecting the presence or absence of a mutation in the feline MYBPC gene, and identifying feline subjects that have or are at risk of developing hypertrophic cardiomyopathy.

The invention relates to markers for acute myocardial infarction (AMI), particularly markers that may be used in the rapid and accurate diagnosis of AMI or reinfarction. A method of diagnosing cardiac injury comprising identifying an elevated concentration of cardiac myosin binding protein C (cMyBP-C) or a fragment thereof or myosin regulatory light chain 2 (MLC2) or a fragment thereof in a sample obtained from a subject.

The invention provides an immunomagnetic bead-based time-resolved fluorescence immunoassay kit of cardiac myosin binding protein C (cMyBP-C). The kit includes a calibrator, immunomagnetic beads, immunofluorescence microspheres, analysis buffering liquid and wash liquid. The magnetic beads are coupled with antibodies, and the time-resolved fluorescence microspheres are coupled with the antibodies;thus the two parts form immunomagnetic beads-cMyBP-C antigen-immunofluorescence microsphere complexes with cMyBP-C antigens in a sample in a reaction tube after shaking incubation; a time-resolved instrument is used to determine intensity of fluorescence emitted thereby under excitation of ultraviolet light; and comparison of a standard curve is carried out to determine the amount of the cMyBP-C antigens in the sample. The kit of the invention greatly shortens reaction time, and improves efficiency and sensitivity of detection.

The present invention relates to a cardio myopeptidin which is isolated from the hearts of non-human healthy mammals. The molecular weight of the cardio myopeptidin is less than 10000 Dalton, the peptide content thereof being 75%˜90%, the free amino acid content 6%˜15%, the ribonucleic acid content less than 2%, and the deoxyribonucleic acid content less than 7.5%. The present invention further provides a method of producing the cardio myopeptidin and the use thereof in producing pharmaceuticals for treating cardiac disorders, specifically the use in producing pharmaceuticals for treating myocardial ischemic and reperfusion injury. The cardio myopeptidin of the present invention can work directly on myocytes, promoting the repair of injuries caused by various reasons, and providing a new way to relieve ischemic and reperfusion injury, and to promote the repair of injured myocardium.

Certain substituted urea derivatives selectively modulate the cardiac sarcomere, for example by potentiating cardiac myosin, and are useful in the treatment of systolic heart failure including congestive heart failure.

The invention discloses a preparation method of an anti-myocardial antibody quadruple diagnostic kit. The anti-myocardial antibody quadruple diagnostic kit provided by the invention is formed by respectively coating four segments of anti-myocardial antibody peptides, namely an anti-myocardial mitochondrial adenosine transferase antibody, a beta1 adrenoceptor antibody, an anti-calcium channel antibody and a cardiac myosin heavy chain antibody. The kit provided by the invention is used to detect an anti-cardiomyopeptidin antibody in serum of a suspected DCM patient. By the kit, diagnosis level of DCM can be improved, and early diagnosis is realized.

The invention discloses a nanometer gold cage compound, and applications thereof in preparation of a kit used for detecting cMyBP-C in human urine or blood. The nanometer gold cage compound is capableof realizing covalent boding with a pair of anti-human cardiac myosin C monoclonal antibody BT09 and BT10, and forming the kit used for rapid detection of cMyBP-C in human urine or blood. The nanometer gold cage compound is used for replacing conventional spherical nanometer particles commonly used in colloidal gold test strips, is extremely high in human blood and/or urea cMyBP-C detection sensitivity and specificity; distinguishing light signals better that those of the spherical nanometer particles are generated based on the white background. At specific application conditions (size and diameter), the cube hollow nanometer crystal is capable of realizing covalent bond combination with DNA and proteins, biotin labelled single chain DNA is capable of connecting nanometer antibodies of two sizes, the detection signal is increased by 5000 to 10000 times of that of colloidal gold nanometer sphere POCT product. It is observed in results that the sensitivity is as high as 100fg/mL, reading of results is realized in 15min, and excellent stability and repeatability are achieved.

The invention discloses a quantitative determination method of cardiac myosin binding protein C. According to the method, firstly, antibody coupling super paramagnetic micro particles and samples to be tested take specific combination reaction to obtain a first reactant, wherein the antibody coupling super paramagnetic micro particles are products obtained by coupling super paramagnetic micro particles and anti-cMyBP-C monoclonal antibodies A; then, the first reactant is taken to perform specific combination reaction with enzyme-labeled articles to obtain a second reactant, wherein the enzyme-labeled articles are products obtained by coupling enzymes and anti-cMyBP-C monoclonal antibodies B; finally, chemiluminescence substrates and the second reactant are taken to take enzymatic reaction;luminous signals are determined; the concentration value of cMyBP-C is obtained. The technology mode of the invention is a sandwich method. Compared with a cMyBP-C ELISA kit, the detection method andthe prepared kit have the advantages that the detection sensitivity and the linear range can be greatly improved. The technology evaluation on the prepared kit shows that the analysis sensitivity is0.05 ng/ml; the detection range is 0.1 to 50 ng/ml; high correlation and coincidence rate to clinic AMI patients are high.

Methods and kits adapted for risk prediction, diagnosis, and analysis of myocardial infarction (MI), myocardial failure, and reduced cardiac function such as heart failure. The methods include collecting a sample of human body fluid or tissue from a subject and then identifying the presence of cardiac myosin binding protein-C 25-nucleotide deletion and/or detecting the presence of cardiac myosin binding protein-C, its peptides, its phosphorylation status, and/or its autoantibodies in the human body fluid or tissue.

The invention can provide compounds, analogs of blebbistatin, effective and selective inhibitors of nonmuscle myosin II relative to cardiac myosin II. Compounds can be used in the method of treating adisease, disorder, or medical condition in a patient, comprising modulating myosin II ATPase, such as treatment of substance abuse relapse disorder, or of renal disease, cancer and metastasis, benignprostate hyperplasia, hemostasis or thrombosis, nerve injury including retinal damage, lung fibrosis, liver fibrosis, arthrofibrosis, wound healing, spinal cord injury, periodontitis, glaucoma and immune-related diseases including multiple sclerosis; or wherein the disease, disorder, or medical condition comprises addiction including abuse of or addiction to anything classified as a Substance-Related or Addictive Disorder in the Diagnostic and Statistical Manual of Mental Disorders (DSM), such as, but not limited to, cocaine, opioids, amphetamines, ethanol, cannabis/marijuana, nicotine, and activities including gambling Compounds are of general formula (I) with substituents as defined herein.

Methods and compositions for rapidly replacing cMyBP-C in sarcomeres featuring the creation of Spy-C mice, which are mice genetically engineered to express cMyBP-C with a protease recognition site and SpyTag peptide introduced into the cMyBP-C gene. In permeabilized myocytes from the Spy-C mice, the cMyBP-C protein can be cleaved at the protease recognition site, and the N-Terminus of cMyBP-C can be removed while the C-terminus remains anchored to the thick filament. A new peptide featuring the SpyCatcher sequence can be covalently bonded to the remaining portion of cMyBP-C, thereby creating a modified cMyBP-C protein. The methods and compositions of the present invention allow for the reconstitution of full-length cMyBP-C at the precise position of native cMyBP-C in the sarcomere and allow for a variety of modifications to be introduced to cMyBP-C in situ.