References

Troponin

      1. Gomes, A.V, Potter,J.D., Szczesna-Cordary, D. (2002) The role of Troponin in muscle contraction. Life, 54: 323-333.
      2. Marston,S.B., Redwood,C.S. (2003) Modulation of thin fi lament activation by breakdown or isoform witching of thin fi lament Proteins. Circ. Res., 93: 1170-1178.
      3. Sarko J, Pollack CV Jr. (2002) Cardiac troponins. J Emerg Med. 2002, 23(1), pp. 57-65.
      4. Cummins B, Auckland ML, Cummins P. (1987) Cardiac-specific troponin-I radioimmunoassay in the diagnosis of acute myocardial infarction. Am Heart J. 113(6): 1333-1344.
      5. Katus HA, Remppis A, Looser S, Hallermeier K, Scheffold T, Kubler W. (1989) Enzyme linked immunoassay of cardiac troponin T for the detection of acute myocardial infarction in patients. J Mol Cell Cardiol. 21(12): 1349-1353.
      6. Hamm CW. (2001) Acute coronary syndromes. The diagnostic role of troponins. Thromb Res., 103 Suppl 1:S63-9.
      7. Labugger R, Organ L, Collier C, Atar D, Van Eyk JE. (2000) Extensive troponin I and T modification detected in serum from patients with acute myocardial infarction. Circulation. 102(11): 1221-1226.
      8. Reiffert SU, Jaquet K, Heilmeyer LM Jr, Herberg FW (1998) Stepwise subunit interaction changes by mono- and bisphosphorylation of cardiac troponin I. Biochemistry, 37(39): 13516-13525.
      9. Katrukha AG, Bereznikova AV, Esakova TV, Pettersson K, Lovgren T, Severina ME, Pulkki K, Vuopio-Pulkki LM, Gusev NB. (1997) Troponin I is released in bloodstream of patients with acute myocardial infarction not in free form but as complex. Clin. Chem. 43(8): 1379-1385.
      10. Wu AH, Feng YJ, Moore R, Apple FS, McPherson PH, Buechler KF, Bodor G. (1998) Characterization of cardiac troponin subunit release into serum after acute myocardial infarction and comparison of assays for troponin T and I. American Association for Clinical Chemistry Subcommittee on cTnI Standardization. Clin. Chem., 44(6): 1198-1208.
      11. Onuoha GN, Alpar EK, Dean B, Tidman J, Rama D, Laprade M, Pau B.(2001) Skeletal troponin-I release in orthopedic and soft tissue injuries. J Orthop Sci. 6(1): 11-15.
      12. Bertinchant JP, Robert E, Polge A, Marty-Double C, Fabbro-Peray P, Poirey S, Aya G, Juan JM, Ledermann B, de la Coussaye JE, Dauzat M. (2000) Comparison of the diagnostic value of cardiac troponin I and T determinations for detecting early myocardial damage and the relationship with histological findings after isoprenalineinduced cardiac injury in rats. Clin Chim Acta. 298(1- 2): 13-28.
      13. Katrukha AG, Bereznikova AV, Filatov VL, Esakova TV, Kolosova OV, Pettersson K, Lovgren T, Bulargina TV, Trifonov IR, Gratsiansky NA, Pulkki K, Voipio-Pulkki LM, Gusev NB. (1998) Degradation of cardiac troponin I: implication for reliable immunodetection. Clin. Chem. 44(12): 2433-2440.
      14. Jaquet K, Thieleczek R, Heilmeyer LM Jr. (1995) Pattern formation on cardiac troponin I by consecutive phosphorylation and dephosphorylation. Eur J Biochem. 231(2): 486-90.
      15. Katrukha AG. (2003) Antibody selection strategies in cardiac troponin assays. Cardiac Markers, 2nd edition, Edited by Alan HB. Wu. 173-185.
      16. Katrukha A, Bereznikova A, Filatov V, Esakova T. Biochemical factors influencing measurement of cardiac troponin I in serum. Clin Chem Lab Med. 1999;37(11-12):1091-5.
      17. Eriksson S, Halenius H, Pulkki K, Hellman J, Pettersson K. Negative interference in cardiac troponin I immunoassays by circulating troponin autoantibodies. Clin Chem. 2005, 51(5):839-47.

ProBNP, BNP and NT-proBNP

      1. Mair J, Hammerer-Lercher A, Puschendorf B: The impact of cardiac natriuretic peptide determination on the diagnosis and management of heart failure. Clin Chem Lab Med 2001;39:571-88.
      2. Cowie MR, Mendez GF: BNP and congestive heart failure. Prog Cardiovasc Dis 2002;44:293-321.
      3. Pandey KN: Biology of natriuretic peptides and their receptors. Peptides 2005;26:901-32.
      4. Wu AH, Packer M, Smith A, Bijou R, Fink D, Mair J, Wallentin L, Johnston N, Feldcamp CS, Haverstick DM, Ahnadi CE, Grant A, Despres N, Bluestein B, Ghani F: Analytical and clinical evaluation of the Bayer ADVIA Centaur automated B-type natriuretic peptide assay in patients with heart failure: a multisite study. Clin Chem 2004;50:867-73.
      5. Hess G, Runkel S, Zdunek D, Hitzler WE: N-terminal pro-brain natriuretic peptide (NT-proBNP) in healthy blood donors and in patients from general practitioners with and without a diagnosis of cardiac disease. Clin Lab 2005;51:167- 72.
      6. Heeschen C, Hamm CW, Mitrovic V, Lantelme NH, White HD: N-terminal pro-B-type natriuretic peptide levels for dynamic risk stratification of patients with acute coronary syndromes. Circulation 2004;110:3206-12.
      7. Troughton RW, Frampton CM, Yandle TG, Espiner EA, Nicholls MG, Richards AM: Treatment of heart failure guided by plasma aminoterminal brain natriuretic peptide (N-BNP) concentrations. Lancet 2000;355:1126-30.
      8. Masson S, Latini R, Anand IS, Vago T, Angelici L, Barlera S, Missov ED, Clerico A, Tognoni G, Cohn JN: Direct comparison of B-type natriuretic peptide (BNP) and amino-terminal proBNP in a large population of patients with chronic and symptomatic heart failure: the Valsartan Heart Failure (Val-HeFT) data. Clin Chem 2006;52:1528-38.
      9. Mueller T, Gegenhuber A, Poelz W, Haltmayer M: Diagnostic accuracy of B type natriuretic peptide and amino terminal proBNP in the emergency diagnosis of heart failure. Heart 2005;91:606-12.
      10. Schellenberger U, O’Rear J, Guzzetta A, Jue RA, Protter AA, Pollitt NS: The precursor to B-type natriuretic peptide is an O-linked glycoprotein. Arch Biochem Biophys 2006;451:160-6.
      11. Seferian KR, Tamm NN, Semenov AG, Mukharyamova KS, Tolstaya AA, Koshkina EV, Kara AN, Krasnoselsky MI, Apple FS, Esakova TV, Filatov VL, Katrukha AG. The brain natriuretic peptide (BNP) precursor is the major immunoreactive form of BNP in patients with heart failure. Clin Chem 2007; 53: 866-873.
      12. Ala-Kopsala M, Magga J, Peuhkurinen K, Leipala J, Ruskoaho H, Leppaluoto J, Vuolteenaho O: Molecular heterogeneity has a major impact on the measurement of circulating N-terminal fragments of A- and B-type natriuretic peptides. Clin Chem 2004;50:1576-88.

Myoglobin

      1. Kagen L, Scheidt S, Butt A. (1977) Serum myoglobin in myocardial infarction: the “staccato phenomenon.” Is acute myocardial infarction in man an intermittent event? Am J Med. 62(1): 86-92.
      2. Penttila K. et al. (2002) Myoglobin, creatine kinase MB isoforms and creatine kinase MB mass in early diagnosis of myocardial infarction in patients with acute chest pain. Clin Biochem. 35(8): 647-53.
      3. Srinivas VS. et al. (2001) Myoglobin levels at 12 hours identify patients at low risk for 30-day mortality after thrombolysis in acute myocardial infarction: a Thrombolysis in Myocardial Infarction 10B substudy. Am Heart J. 142(1): 29-36.
      4. Van Nieuwenhoven FA. Et al. (1995) Discrimination between myocardial and skeletal muscle injury by assessment of the plasma ratio of myoglobin over fatty acid-binding protein. Circulation. 92(10): 2848-54.

GAPDH

      1. Bentham M et al. Role of myristoylation and N-terminal basic residues in membrane association of the human immunodeficiency virus type 1 Nef protein. J Gen Virol 87:563-71 (2006).
      2. Lee DC et al. Enhanced cystatin C and lysosomal protease expression following 6-hydroxydopamine exposure. Neurotoxicology 27:260-76 (2006).
      3. Rouleau C et al. Protein tyrosine phosphatase PRL-3 in malignant cells and endothelial cells: expression and function. Mol Cancer Ther 5:219-29 (2006).
      4. Dove B et al. Cell cycle perturbations induced by infection with the coronavirus infectious bronchitis virus and their effect on virus replication. J Virol 80:4147-56 (2006)
      5. Fraser M et al. Regulation of p53 and suppression of apoptosis by the soluble guanylyl cyclase/cGMP pathway in human ovarian cancer cells. Oncogene 25:2203-12 (2006).
      6. Carroll RC et al. Prospective evaluation of platelet B2 bradykinin and thrombopoietin receptor levels from preeclamptic compared to non-preeclamptic pregnancy patients. Thromb Res 117:551-6 (2006).
      7. Fediuc S et al. Effect of voluntary wheel running on circadian corticosterone release and on HPA axis responsiveness to restraint stress in Sprague-Dawley rats. J Appl Physiol 100:1867-75 (2006).
      8. Grigorieva JA, Dainiak MB, Katrukha AG, Muronetz VI. Antibodies to the nonnative forms of d-glyceraldehyde-3-phosphate dehydrogenase: identification, purification, and influence on the renaturation of the enzyme. Arch Biochem Biophys. 369(2):252-60 (1999).
      9. Dainiak MB, Izumrudov VA, Muronetz VI, Galaev IY, Mattiasson B. Conjugates of monoclonal antibodies with polyelectrolyte complexes– an attempt to make an artificial chaperone. Biochim Biophys Acta. 1381(3):279-85 (1998).

Lectin-like Oxidized LDL receptor (LOX-1)

      1. Libby, P. Current concepts of the pathogenesis of acute coronary events. 2001, Circulation, 104, 365-372.
      2. Sawamura, T., et al., An endothelial receptor for oxidized low density lipoprotein. 1997. Nature, 386, 73-77.
      3. Mehta, J., et al., Lectin-like, oxidized low-density lipoprotein receptor-1 (LOX-1): A critical player in the development of atherosclerosis and related disorders. 2006, Cardiovasc.Res., 69, 36-45.
      4. Hayashida, K., Serum Soluble Lectin-Like Oxidized Low-Density Lipoprotein Receptor-1 Levels Are Elevated in Acute Coronary Syndrome: A Novel Marker for Early Diagnosis. 2005, Circulation, 112, 812-818.
      5. Tatsuguchi, M., et al., Oxidized LDL receptor gene (OLR1) is associated with the risk of myocardial infarction. 2003, Biochem. Biophys. Res. Commun. 303, 247-250.

Thyroid Peroxidase (TPO)

      1. Mariotti S., et al, J Clin Endocrinol Metab 1983; 56(3): 467-73
      2. Czarnocka B., et al; C R Acad Sci III 1985; 300(15): 577-80
      3. Grennan J., et al; Autoimmunity 1999; 30(3): 157-69
      4. Finke R.; J Clin Endocrinol Metab 1990; 71(1): 53-9
      5. Doble ND., et al; Immunology 1988; 64(1): 23-9
      6. Goodburn R., et al; Clin Chim Acta 1982; 119(3): 291-7
      7. Ohwovoriole AE.; Asian Pac J Allergy Immunol 1989; 7(2): 79-83
      8. Wietman AP.; Clin Immunol Immunopathol 1987; 43(3): 333-42
      9. Kendler DL., et al; Clin Endocrinol (Oxf) 1990; 33(6): 751-60
      10. Gardas A., et al; Biochim Biophys Acta 1999; 1433 (1-2): 229-39

Urotensin II

      1. Kwok Leung Ong, Karen S.L. Lam, and Bernard M.Y. Cheung. Urotensin II: Its Function in Health and Its Role in Disease. Cardiovasc. Drugs Ther. 2005, Jan; 19(1): 65-75.
      2. Onan, D. et.al. UrotensinII: the old kid in town. TRENDS in Endocrinology and Metabolism, 2004, Vol.15(4): 175-182.
      3. Tzanidis A. et al. Direct actions of urotensin II on the heart. Implications for cardiac fibrosis and hypertrophy. Circ. Res. 2003; 93: 246-253.
      4. Toshiaki Suguro, Takuya Watanabe et al. Increased Human Urotensin II Levels Are Correlated With Carotid Atherosclerosis in Essential Hypertension. Am. J. hypertens., 2007, Feb, Vol. 20 (2): 211-217

Myeloperoxidase (MPO)

      1. Nauseef WM et al.(1988): Biosynthesis and processing of myeloperoxidase – a marker for myeloid cell differentiation. Eur J Haematol. 40(2): 97-110.
      2. Klebanoff SJ. (2005): Myeloperoxidase: friend and foe. J Leukos Biol. 77: 598- 625.
      3. Chevrier I et al. (2003): Myeloperoxidase: new polymorphisms and relation with lung cancer risk. Pharmacogenetics. 13(12): 729-39.
      4. Reynolds WF et al. (2000): MPO and APOEepsilon4 polymorphisms interact to increase risk for AD in Finnish males. Neurology. 55(9): 1284-90.
      5. Nagra RM et al. (1997): Immunohistochemical and genetic evidence of myeloperoxidase involvement in multiple sclerosis. J Neuroimmunol. 78(1-2): 97-107.
      6. Nambi V. (2005): The use of myeloperoxidase as a risk marker for atherosclerosis. Curr Atheroscler Rep. 7(2): 127-31.
      7. Zhang R. et al. (2001): Association between myeloperoxidase levels and risk of coronary artery disease. JAMA. 286(17): 2136-42.
      8. Brennan ML et al. (2003): Prognostic value of myeloperoxidase in patients with chest pain. New Eng J Med. 349(17): 1595-1604.
      9. Baldus S. et al. (2003): Myeloperoxidase serum level predicts risk in patients with acute coronary syndromes. Circulation 10: 1440-1445.
      10. Choi HK et al. (2001): Diagnostic performance of antineutrophil cytoplasmic antibody tests for idiopathic vasculitides: meta-analysis with a focus on antimyeloperoxidase antibodies. J Rheumatol. 28(7): 1584-1590.

Serum Amyloid A (SAA)

      1. Malle E et al (1993): Serum amyloid A (SAA): an acute phase protein and apolipoprotein. Atherosclerosis, 102: 131-146.
      2. Marhaug G et al. (1982): Characterization of amyloid related protein SAA compleed with serum lipoprotein (apoSAA). Clin Exp Immunol 50: 382-389.
      3. Benson MD, Cohen AS. (1979): Serum amyloid A protein in amyloidosis, rheumatic, and enoplastic diseases. Arthritis Rheum. 22(1): 36-42.
      4. Liuzzo G et al. (1994): The prognostic value of C-reactive protein and serum amyloid A protein in severe unstable angina. N Engl J Med 331: 417-424.
      5. Ogasawara K et al (2004): A serum amyloid A and LDL complex as a new prognostic marker in stable coronary artery disease. Atherosclerosis, 174: 349-356.
      6. Ricker PM et al. (2000): C-reactive protein and other markers of inflammation in the prediction of cardiovascular disease in women. N Engl J Med 342: 836-843.
      7. Johnson BD et al (2004): Serum amyloid A as a predictor of coronary artery disease and cardiovascular Outcome in women. Circulation, 109:726-732.

Soluble CD40 ligand (sCD40L)

      1. Hollenbaugh D, Grosmaire LS, Kullas CD, Chalupny NJ, Braesch- Andersen S, Noelle RJ, Stamenkovic I, Ledbetter JA, Aruffo A. (1992) The human T cell antigen gp39, a member of the TNF gene family, is a ligand for the CD40 receptor: expression of a soluble form of gp39 with B cell co-stimulatory activity. EMBO J. 11:4313–4321.
      2. Henn V, Slupsky JR, Grafe M, Anagnostopoulos I, Forster R, Muller- Berghaus G, Kroczek RA. (1998) CD40 ligand on activated platelets triggers an inflammatory reaction of endothelial cells. Nature 391:591–594.
      3. Mach, F., Schonbeck, U., Bonnefoy, J.-Y., Pober, J. S.,Libby, P. (1997) Activation of monocyte/macrophage functions related to acute atheroma complication by ligation of CD40. Induction of collagenase, stromelysin, and tissue factor. Circulation 96:396–399.
      4. Garlichs CD, Eska. S, Raaz D, Schmidt A, Ludwig J, Herrmann M, Klinghamer L, Daniel WG, Schmeisser A. (2001) Patients with acute coronary syndromes express enhanced CD40 ligand/CD154 on platelets. Heart 86:649–655.
      5. Durie FH, Fava RA, Foy TM, Aruffo A, Ledbetter JA, Noelle RJ. (1993) Prevention of collagen-induced arthritis with an antibody to gp39, the ligand for CD40. Science 261:1328–1330.
      6. Gerritse K, Laman JD, Noelle RJ, Aruffo A, Ledbetter JA, Boersma WJ, Claassen E. (1996) CD40-CD40 ligand interactions in experimental allergic encephalomyelitis and multiple sclerosis. Proc. Natl Acad. Sci. USA 93:2499–2504.
      7. Francois Mach, Uwe Schonbeck, Galina K. Sukhova, Elizabeth Atkinson, Peter Libby. (1998) Reduction of atherosclerosis in mice by inhibition of CD40signalling. Nature. 394(9):200-203.
      8. Thor Ueland, Pal Aukrust, Arne Yndestad, Kari Otterdal, Stig S. Froland, Kenneth Dickstei4, John Kjekshus, Lars Gullestad, Jan K. Damas. (2005) Soluble CD40 ligand in acute and chronic heart failure. Eur. Heat J. 26:1101-1107.
      9. Varo N, de Lemos JA, Libby P, Morrow DA, Murphy SA, Nuzzo R, Gibson CM, Cannon CP, Braunwald E, Schonbeck U. (2003) Soluble CD40L: risk prediction after acute coronary syndromes. Circulation. 108(9):1049-52.

Cystatin C

      1. Turk B, Turk D and Salvesen GS: Regulating Cysteine Protease Activity: Essential Role of Protease Inhibitors As Guardians and Regulators. Current  pharmaceutical Design, 2002, 8, 1623-1637.
      2. Schnittger S, Rao VV, Abrahamson M, Hansmann I: Cystatin C (CST3), the candidate gene for hereditary cystatin C amyloid angiopathy (HCCAA), and other members of the cystatin gene family are clustered on chromosome 20p11.2. Genomics. 1993 Apr; 16(1):50-5.
      3. Asgeirsson B, Haebel S, Thorsteinsson L, Helgason E, Gudmundsson KO, Gudmundsson G, Roepstorff P: Hereditary cystatin C amyloid angiopathy: monitoring the presence of the Leu-68–>Gln cystatin C variant in cerebrospinal fl uids and monocyte cultures by MS. Biochem J. 1998 Feb 1; 329 (Pt 3): 497-503.
      4. Coll E, Botey A, Alvarez A, Poch E, Quinto L, Saurina A, Vera M, Piera C, Darnell A: Serum cystatin C as a new marker for noninvasive estimation of glomerular filtration rate and as a marker for early renal impairment. Am J Kidney Dis. 2000 Jul; 36(1): 29-34.
      5. Shlipak MG, Sarnak MJ, Katz R, Fried LF, Seliger SL, Newman AB, Siscovick DS, Stehman-Breen C: Cystatin C and the risk of death and cardiovascular events among elderly persons. N Engl J Med. 2005 May 19; 352(20): 2049- 60.
      6. Artunc FH, Fisher IU, Risler T, Erley CM: Improved estimation of GFR by serum cystatin C in patients undergoing cardiac catheterization. Int J Cardiol. 2005 Jul 10; 102(2):173-8.
      7. Roos JF, Doust J, Tett SE, Kirkpatrick CM: Diagnostic accuracy of cystatin C compared to serum creatinine for the estimation of renal dysfunction in adults and children-A meta-analysis. Clin Biochem. 2007 Mar; 40(5-6): 383-91.
      8. Uchida K, Gotoh A: Measurement of cystatin-C and creatinine in urine. Clin Chim Acta. 2002 Sep; 323(1-2): 121-128.
      9. Lassus J, Harjola VP, Sund R, Siirilä-Waris K, Melin J, Peuhkurinen K, Pulkki K, Nieminen MS; for the FINN-AKVA Study group: Prognostic value of cystatin C in acute heart failure in relation to other markers of renal function and NT-proBNP. Eur Heart J. 2007 Aug;28(15):1841-7. Epub 2007 Feb 8

Human Serum Albumin (HSA)

      1. Bennett PH et al. Screening and management of microalbuminuria in patients with diabetes mellitus: recommendations to the Scientific Advisory Board of the National Kidney Foundation from an ad hoc committee of the Council on Diabetes Mellitus of the National Kidney Foundation. Am J Kidney Dis. 1995, 25(1), pp.107-112.
      2. Salmasi AM et al. The degree of albuminuria is related to left ventricular hypertrophy in hypertensive diabetics and is associated with abnormal left ventricular filling: a pilot study. Angiology. 2003, 54(6), pp. 671-678.
      3. Wachtell K et al. Albuminuria and cardiovascular risk in hypertensive patients with left ventricular hypertrophy: the LIFE study. Ann Intern Med. 2003, 139(11), pp.901-906.

Pregnancy Associated Plasma Protein A (PAPP-A)

      1. Oxvig, C., Sand, O., Kristensen, T., Gleich GJ., Circulating human pregnancy associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein.// J Biol Chem 268:12243-6(1993).
      2. Overgaard, MT., Haaning, J., Boldt, HB., Olsen, IM., Laursen, LS., et al. Expression of recombinant human pregnancy-associated plasma protein-A and identifi cation of the proform of eosinophil major basic protein as its physiological inhibitor.// J Biol Chem; 275:31128-33 (2000).
      3. Kristensen T, Oxvig C, Sand O, Moller NP, Sottrup-Jensen L. Amino acid sequence of human pregnancy-associated plasma protein-A derived from cloned cDNA. Biochemistry. 1994;33:1592-8.
      4. Lawrence, J. B., Oxvig, C., Overgaard, M. T., Sottrup-Jensen, L., Gleich, G. J., Hays, L. G., et al. The insulin-like growth factor (IGF)-dependent IGF binding protein-4 protease secreted by human fi broblasts is pregnancy-associated plasma protein-A.// Proc Natl Acad Sci U S A, 96 (6), 3149-53 (1999).
      5. Wald N, Stone R, Cuckle HS, Grudzinskas JG, Barkai G, Brambati B, et al. First trimester concentrations of pregnancy associated plasma protein A and placental protein 14 in Down’s syndrome. BMJ 1992;305:28.
      6. Wapner R, Thom E, Simpson JL, Pergament E, Silver R, Filkins K, et al. Firsttrimester screening for trisomies 21 and 18. N Engl J Med 2003; 349:1405-13.
      7. Bayes-Genis, A., Conover, C. A., Overgaard, M. T., Bailey, K. R., Christiansen, M., Holmes, D. R. Jr, et al. Pregnancy-associated plasma protein A as a marker of acute coronary syndromes.// N Engl J Med, 345 (14), 1022- 9 (2001).
      8. Qin, Q.P., Laitinen, P., Majamaa-Voltti, K., Eriksson, S., Kumpula, E.K., and Petter-son, K. Release Patterns of Pregnancy Associated Plasma Protein A (PAPP-A) in Patients with Acute Coronary Syndroms.//Scand Cardiovasc J, 36(6), 358-61(2002).
      9. Heeschen C, Dimmeler S, Hamm CW, Fichtlscherer S, Simoons ML, Zeiher AM. Pregnancy-associated plasma protein-A levels in patients with acute coronary syndromes Comparison with markers of systemic inflammation, platelet activation, and myocardial necrosis. J Am Coll Cardiol 2005;45:229-37.
      10. Qin QP, Kokkala S, Lund J, Tamm N, Voipio-Pulkki LM, Pettersson K. Molecular distinction of circulating pregnancy-associated plasma protein A in myocardial infarction and pregnancy. Clin Chem 2005;51:75-83.

Procalcitonin (PCT)

      1. Le Moullec J.M., et al. The complete sequence of human procalcitonin. // FEBS Lett., 167 (1), 93-97 (1984).
      2. Assicot M, et al. High serum procalcitonin concentrations in patients with sepsis and infection. // Lancet, 341, 515-18 (1993).
      3. Meisner M., Reinhart K. Is procalcitonin really a marker of sepsis? // Int. J. Intensive Care, 8 (1), 15-25. (2001).
      4. Potapov EV., et al. Elevated donor cardiac troponin T and procalcitonin indicate two independent mechanisms of early graft failure after heart transplantation. //Int. J. Cardiol., 92 (2-3), 163-7 (2003).

D-Dimer and high molecular weight fibrin degradation products

      1. Bounameaux H, de Moerloose P, Perrier A, Reber G. Plasma measurement of D-dimer as diagnostic aid in suspected venous thromboembolism: an overview. Thromb Haemost. 1994; 71: 1-6.
      2. Rowbotham BJ, Carroll P, Whitaker AN, Bunce IH, Cobcroft RG, Elms MJ, Masci PP, Bundesen PG, Rylatt DB, Webber AJ. Measurement of crosslinked fibrin derivatives–use in the diagnosis of venous thrombosis. Thromb Haemost. 1987; 57: 59-61.

Rat C-peptide and proinsulin

      1. Davidson H.W., Rhodes C.J., Hutton J.C. Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic beta cell via two distinct site-specific endopeptidases. Nature, 1988, 333 (6168):93-6
      2. Davidson H.W., Hutton J.C. The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing. Biochem J., 1987, 245(2):575-82
      3. Rhodes CJ, Lincoln B, Shoelson SE Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase. Implication of a favored route for prohormone process ing. J Biol Chem., 1992, 267(32):22719-27.
      4. Horwitz DL, Starr JI, Mako ME, Blackard WG, Rubenstein AH. Proinsulin, insulin, and C-peptide concen trations in human portal and peripheral blood. J Clin Invest. 1975, 55(6):1278-83.
      5. Clark PM. Assays for insulin, proinsulin(s) and C-peptide. Ann Clin Biochem. 1999 ;36 ( Pt 5) :541-64.

Thrombin Activatable Fibrinolysis Inhibitor (TAFI)

      1. Van Tilburg N.H. et al. Thrombin activatable fi brinolysis inhibitor and the risk for deep vein thrombosis. Blood 2000; 95: 2855-9.
      2. Silveira A. et al. Plasma procarboxypeptidase U in men with symptomatic coronary artery disease. Thromb Haemost 2000; 84: 364-8.
      3. Schroeder V. et al. Thrombin activatable fibrinolysis inhibitor (TAFI) levels in patients with coronary artery disease investigated by angiography. Thomb. Haemost. 2002; 88(6): 1020-5.
      4. Hendriks D, Scharpe S, van Sande M, Lommaert MP. Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N. J Clin Chem Clin Biochem. 1989;27:277-85.
      5. Campbell W, Okada H. An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits. Biochem Biophys Res Commun. 1989;162(3):933-9.
      6. Eaton DL, Malloy BE, Tsai SP, Henzel W, Drayna D.Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J Biol Chem. 1991;266(32):21833-8.
      7. Gils A, Alessi MC, Brouwers E, Peeters M, Marx P, Leurs J, Bouma B, Hendriks D, Juhan-Vague I, Declerck PJ. Development of a genotype 325-specific proCPU/TAFI ELISA. Arterioscler Thromb Vasc Biol. 2003;23(6):1122-7.
      8. Chetaille P, Alessi MC, Kouassi D, Morange PE, Juhan-Vague I. Plasma TAFI antigen variations in healthy subjects. Thromb Haemost. 2000;83(6):902-5.
      9. Bajzar L, Morser J, Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J Biol Chem. 1996;271(28):16603-8.
      10. Boffa MB, Wang W, Bajzar L, Nesheim ME. Plasma and recombinant thrombin-activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties. J Biol Chem. 1998;273(4):2127-35.
      11. Mao SS, Cooper CM, Wood T, Shafer JA, Gardell SJ. Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans. J Biol Chem. 1999;274(49):35046-52.
      12. Marx PF, Dawson PE, Bouma BN, Meijers JC. Plasmin-mediated activation and inactivation of thrombin-activatable fibrinolysis inhibitor. Biochemistry. 2002;41(21):6688-96.
      13. Valnickova Z, Thogersen IB, Christensen S, Chu CT, Pizzo SV, Enghild JJ. Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein. J Biol Chem. 1996;271(22):12937-43.
      14. Marx PF, Hackeng TM, Dawson PE, Griffin JH, Meijers JC, Bouma BN. Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. J Biol Chem. 2000;275(17):12410-5.
      15. Schroeder V, Chatterjee T, Mehta H, Windecker S, Pham T, Devantay N, Meier B, Kohler HP. Thrombin activatable fibrinolysis inhibitor (TAFI) levels in patients with coronary artery disease investigated by angiography. Thromb Haemost. 2002;88(6):1020-5.
      16. Eichinger S, Schoenauer V, Weltermann A, Minar E, Bialonzcyk C, Hirschl M, Schneider B, Quehenberger P, Kyrle PA. Thrombin activatable fibrinolysis inhibitor (TAFI) and the risk of recurrent venous thromboembolism. Blood. 2004 (in press).
      17. Lau HK, Segev A, Hegele RA, Sparkes JD, Teitel JM, Chisholm RJ, Strauss BH. Thrombin-activatable fibrinolysis inhibitor (TAFI): a novel predictor of angiographic coronary restenosis. Thromb Haemost. 2003;90(6):1187-91.
      18. Colucci M, Binetti BM, Branca MG, Clerici C, Morelli A, Semeraro N, Gresele P. Deficiency of thrombin activatable fibrinolysis inhibitor in cirrhosis is associated with increased plasma fibrinolysis. Hepatology. 2003;38(1):230-7.
      19. Meijers JC, Oudijk EJ, Mosnier LO, Bos R, Bouma BN, Nieuwenhuis HK, Fijnheer R. Reduced activity of TAFI (thrombin-activatable fibrinolysis inhibitor) in acute promyelocytic leukaemia. Br J Haematol. 2000;108(3):518-23.

Fibrinogen

      1. Lowe G. et al. Blood rheology, cardiovascular risk factors, and cardiovascular disease: the West of Scotland Coronary Prevention Study. Thromb Haemost, 2000; 84:553-8.
      2. Danesh J. et al. Association of fibrinogen, C-reactive protein, albumin, or leukocyte count with coronary heart disease: meta-analyses of prospective studies. JAMA, 1998; 279:1477-82.

Fibrinopeptide A

      1. Sonel A. et al. Prospective Study Correlating Fibrinopeptide A, Troponin I, Myoglobin, and Myosin Light Chain Levels With Early and Late Ischemic Events in Consecutive Patients Presenting to the Emergency Department With Chest Pain. Circulation. 2000; 102:1107-13.
      2. Rapold H.J. et al. Fibrin formation and platelet activation in patients with myocardial infarction and normal coronary arteries. Eur Heart J. 1989; 10:323-33.

Human glycated hemoglobin (HbA1c)

      1. Sacks, D.B., et al., Guidelines and recommendations for laboratory analysis in the diagnosis and management of diabetes mellitus. 2002 Clin. Chem., 48, 436-472.
      2. Nelson, D.L. and Cox, M.M. “Leninger principles of biochemistry”, 2003, Worth Publishers, pp 210-221.
      3. Cussimanio et al., Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. 2003. Biophys.Chem., 105, 743-755.
      4. Little R.R. Recent progress in glycohemoglobin (HbA1c) testing. 2000. Diabetes Care, 23, 3, 265-266.

Adiponectin

      1. Kadowaki et al., Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome. 2006, JCI, 116, 7, 1784-1792.
      2. Matsuzawa Y., et al., Adiponectin and metabolic syndrome. 2004, Arterioscler. Tromb.Vasc.Biol., 24, 29-33.
      3. Kumada, M., et al., association of hypoadiponectinemia with coronary artery disease in men. 2003. Arterioscler Thromb Vasc Biol.,23, 85-89.
      4. Wang Y., et al., Post-translational Modifications of the Four Conserved Lysine Residues within the Collagenous Domain of Adiponectin Are Required for the Formation of Its High Molecular Weight Oligomeric Complex. 2006, JBC, 281, 24, 16391-16400.
      5. Hara, K., et al., Measurement of the High–Molecular Weight Form of Adiponectin in Plasma Is Useful for the Prediction of Insulin Resistance and Metabolic Syndrome. 2006, Diabetes Care, 29, 1357-1362.

Leptin

      1. El-Atat F et al. (2003) Obesity and hypertension. Endocrinol Metab Clin North Am. 32(4):823-854.
      2. Rahmouni K, Haynes WG. (2004) Leptin and the cardiovascular system. Recent Prog Horm Res. 59:225-244.
      3. Zhang Y. et al. (1994) Positional cloning of the mouse obese gene and its human homologue. Nature 372: 425-432.
      4. Ogawa Y. et al. (1995) Molecular cloning of rat obese cDNA and augmented gene expression in genetically obese Zucker fatty (fa/fa) rats. J Clin Invest 96:1647-1652.

Immunoglobulins

      1. Andreu-Ballester JC, Pérez-Griera J, Ballester F, Colomer-Rubio E, Ortiz-Tarín I, Oteroe CP: Secretory immunoglobulin A (sIgA) deficiency in serum of patients with GALTectomy. Clinical Immunology (2007) 123, 289–297

Influenza

      1. Koskinen JO, Vainionpää R, Meltola NJ, Soukka J, Hänninen PE, Soini AE: Rapid Method for Detection of Influenza A and B Virus Antigens by Use of a Two-Photon Excitation Assay Technique and Dry-Chemistry Reagents. J. Clin. Microbiol., Nov. 2007, p. 3581–3588

Biodefense

      1. Working group on civilian biodefense, “Anthrax as a biological weapon”, JAMA, vol. 281, N 18, 1999
      2. Working group on civilian biodefense, “Plague as a biological weapon”, JAMA, vol. 283, N 17, 2000
      3. Working group on civilian biodefense, “Tularemia as a biological weapon”, JAMA, vol. 285, N 21, 2001
      4. Working group on civilian biodefense, Botulinum toxin as a biological weapon, JAMA, vol. 285, N 8, 2001
      5. The Centers for Disease Control (CDC); The World Health Organization (WHO).

Gangliosides

    1. Kolter T., Proia RL., Sandhoff K., Combinatorial Ganglioside Biosynthesis. J Biol Chem. 2002 Jul 19;277(29):25859-62.
    2. Jeyakumar M., Butters TD., Dwek RA., Platt FM., Glycosphingolipid lysosomal storage diseases: therapy and pathogenesis. Neuropathol Appl Neurobiol. 2002 Oct;28(5):343-57.
Skip to toolbar