Isolated post-translationally modified mammalian proteins...

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

Reexamination Certificate

active

10270838

ABSTRACT:
Isolated phosphorylated troponin I proteins useful in diagnosing and monitoring the phosphorylation state of injured muscle tissue are provided. Also provided are compounds, kits and methods for assessing the phosphorylation state of these troponin I proteins and modulating the phosphorylation state of these troponin I proteins in a subject.

REFERENCES:
patent: 5834220 (1998-11-01), Wicks et al.
patent: 6248549 (2001-06-01), Van Eyk et al.
patent: 2243372 (1998-07-01), None
patent: WO 94/27156 (1994-11-01), None
patent: WO 96/10078 (1996-04-01), None
patent: WO 96/33415 (1996-10-01), None
Ardelt et al. 1998; Microanalysis and distribution of cardiac troponin I phopho species in heart areas. Biol. Chem. 379:341-347.
Jaquet et al. 1995; Pattern formation on cardiac troponin by consecutive phosphorylation and dephosphorylation. Eur. J. Biochem. 231: 486-490.
Swiderek et al. 1990; Sites phosphorylated in bovine cardiac troponin T and I. Eur. J. Biochem. 190:575-582.
Buscemi et al., “p21-Activated Kinase Increases the Calcium Sensitivity of Rat Triton-Skinned Cardiac Muscle Fiber Bundles via a Mechanism Potentially Involving Novel Phosphorylation of Troponin I”, Circ. Res. 2002 91:509-516.
Härtner and Pette, “Fast and slow isoforms of troponin I and troponin C. Distribution in normal rabbit muscles and effects of chronic stimulation”, Eur. J. Biochem. 1990 188:261-267.
U.S. Appl. No. 09/419,901, filed Oct. 18, 1999, Van Eyk et al.
Bartel, S., et al., Protein Phosphorylation in Isolated Trabeculae from Nonfailing and Failing Human Hearts. (Abstract)Mol. Cell Biochem., 157: 171-179 (1996).
Bodor, G. S., et al., Troponin I Phosphorylation in the Normal and Failing Adult Human Heart.Circulation, 96: 1495-1500 (1997).
Collinson, P.O., et al., Measurement of Cardiac Troponins.Ann. Clin. Biochem. 38(Pt 5): 423-449 (2001).
Jideama, N.M., et al., Phosphorylation Specificities of Protein Kinase C Isozymes for Bovine Cardiac Troponin I and Troponin T and Sites Within there Proteins and Regulation of Myofilament Properties.J. Biol. Chem., 271: 23277-23283 (1996).
Kaumann, A., et al., Activation of β2-Adrenergic Receptors Hastens Relaxation and Mediates Phosphorylation of Phospholamban, Troponin I, and C-Protein in Ventricular Myocardium from Patients with Terminal Heart Failure.Circulation99: 65-72 (1999).
Matejovicova, M., et al., Phosphorylation by Protein Kinases A and C of Myofibrillar Proteins in Rabbit Stunned and Non-Stunned Myocardium.J. Mol. Cell Cardiol. 29: 3189-3202 (1997).
McConnell, B. K., et al., Troponin I Phosphorylation and Myofilament Calcium Sensitivity During Decompensated Cardiac Hypertrophy.Amer. J. Physiol. 274 (Heart Circ. Physiol. 43): H385-H396 (1998).
Takahashi, M., et al., Use of Enzyme Immunoassay for Measurement of Skeletal Troponin-I Utilizing Isoform-Specific Monoclonal Antibodies.Clin. Biochem. 29 (4): 301-308 (1996).
Database EMBL Accession No. P02643 1986 XP-002275449.
Filatov et al., “Troponin:Structure, Properties, and Mechansim of Functioning”, Biochemistry 1999 64(9) :969-985 XP008028931.
Huang et al., “The Amino Acid Sequences of the Phosphorylated Sites in Troponin-I from Rabbit Skeletal Muscle”, FEBS Letters 1974 42(3) :249-252 XP-001188933.
Labugger et al., “Extensive Troponin I and T Modification Detected in Serum From Patients With Acute Myocardial Infarction”, Circulation 2000 102:1221-1226 XP-001080442.
Li et al., “Phosphorylation and Mutation of Human Cardiac Troponin I Deferentially Destabilize the Interaction of the Functional Regions of Troponin I with Troponin C”, Biochemistry 2003 42:14460-14468 XP-002275176.
Li Monica et al., “Novel Phosphorylation of Ser 149 in Cardiac Troponin I (cTnI) by PAK Reduces the Affinity of cTnI for Cardiac Troponin C (cTnC)”, 46th Annual Meeting of the Biophysical Society 2002 p. 389a 1894-Pos XP008028764.
McDonough et al., “Troponin I Degradation and Covalent Complex Formation Accompanies Myocardial Ischemia/Reperfusion Injury”, Circ Res 1999 84:9-20 XP002275174.
Moir et al., “The Phosphorylation Sites of Troponin I from White Skeletal Muscle of the Rabbit”, FEBS Letters 1974 42(3) :253-256 XP-001189064.
Simpson et al., “Differential Detection of Skeletal Troponin I Isoforms in Serum of a Patient with Rhabdomyolysis:Markers of Muscle Injury?”, Clinical Chemistry 2002 48(7) :1112-1114 XP-002275173.
Solaro et al., “Altered Interactions Among Thin Filament Proteins Modulate Cardiac Function”, J Mol Cell Cardiol 1996 28(2) :217-230 XP-002275175.
Van Eyk et al., “Cardiac Disease-Induced Post-Translational Modifications of Troponin I:Differential Proteolysis, Phosphorylation and Covalent Complex Formation”, 44th Annual Meetinf of the Biophysical Society Feb. 12-16, 2000 632-POS XP008028766.
Wilkinson et al., “The Amino Acid Sequence of Troponin I from Rabbit Skeletal Muscle”, Biochem. J. 1975 149:493-496 XP008028897.
Takeishi et al., “In Vivo Phosphorylation of Cardiac Troponin I by Protein Kinase Cβ2 Decreases Cardiomyocyte Calcium Responsiveness and Contractility in Transgenic Mouse Hearts”, J. Clin. Invest. 1998 102:72-78.
Andres et al., “Contractile proteins in globally “stunned” rabbit myocardium”, Basic Res. Cardiol. 1991 86:219-226.
Chan et al., “Rapid analysis of fatty acid-binding proteins with immunosensors and immunotests for early monitoring of tissue injury”, Biosensors and Bioelectronics 2005 20:2566-2580.
Härtner et al., “Fast and slow isoforms of troponin I and troponin c—Distribution in normal rabbit muscles and effects of chronic stimulation”, Eur. J. Biochem. 1990 188:261-267.
Konagaya et al., “Increased Serum Myosin Light Chain 3 Level in Neuromusclar Diseases”, Muscle & Nerve 1987 10:415-421.
Larue et al., “Immunoradiometric Assay of Myosin Heavy Chain Fragments in Plasma for Investigation of Myocardial Infarction”, Clin. Chem. 1991 37/1:78-82.
Morano et al., “Phosphorylation and Thiophosphorylation by Myosin Light Chain Kinase:Different Effects on Mechanical Properties of Chemically Skinned Ventricular Fibers from the Pig”, J Mol Cell Cardiol 1990 22:805-813.
Ravkilde, J., “Creatine kinase isoenzyme MB mass, cardiac troponin T, and myosin light chain isotype 1 as serological markers of myocardial injury and their prognostic importance in acute coronary syndrome”, Dan. Med. Bull. 1998 45(1):34-50.
Thompson et al., “Signalling Pathways Regulating Protein Turnover in Skeletal Muscle”, Cell. Signal. 1998 10(1):1-11.
Wolff et al., “Myofibrillar Calcium Sensitivity of Isometric Tension Is Increased in Human Dilated Cardiomyopathies”, J. Clin. Invest. 1996 98:167-176.
Yuasa et al., “A Novel Interaction of cGMP-dependent Protein Kinase I with Troponin T”, J. Biol. Chem. 1999 274(52):37429-37434.
U.S. Appl. No. 11/138,184, filed May 26, 2005.
U.S. Appl. No. 09/115,589, filed Jul. 15, 1998.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Isolated post-translationally modified mammalian proteins... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Isolated post-translationally modified mammalian proteins..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Isolated post-translationally modified mammalian proteins... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3724118

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.