Hysteretic behavior of proprotein convertase 1/3 (PC1/3)

PLoS ONE

Volumn 6, Issue 9, 2011, Pages

  Icimoto, Marcelo Y ^a   Barros, Nilana M ^a   Ferreira, Juliana C ^a   Marcondes, Marcelo F ^a   Andrade, Douglas ^a   Machado, Mauricio F ^a   Juliano, Maria A ^a   Júdice, Wagner A ^b   Juliano, Luiz ^a   Oliveira, Vitor ^a  

^a FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

^b UNIVERSIDADE DE MOGI DAS CRUZES   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; HISTATIN; HORMONE PRECURSOR; INSULIN; PEPTIDASE; PROINSULIN; PROPROTEIN CONVERTASE 1; PROPROTEIN CONVERTASE 3; SERINE PROTEINASE; UNCLASSIFIED DRUG; HTN3 PROTEIN, HUMAN;

ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; CONTROLLED STUDY; EUKARYOTE; GEL ELECTROPHORESIS; HYDROLYSIS; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN EXPRESSION; PROTEIN PROCESSING; ANIMAL; CHO CELL; HAMSTER; METABOLISM;

ANIMALS; CALCIUM; CHO CELLS; CRICETINAE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HISTATINS; HYDROGEN-ION CONCENTRATION; MICE; PROPROTEIN CONVERTASE 1;

EID: 80052831946     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0024545     Document Type: Article

References (33)

1. Van de Ven W, Roebroek A, (1993) Structure and function of eukaryotic proprotein processing enzymes of subtilisin family of serine proteases. Crit Rev Oncog 4: 115-136.
2. Seidah NG, Chrétien M, (1999) Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res 848: 45-62.
3. Steiner DF, (1998) The proprotein convertases. Curr Opin Chem Biol 2: 31-39.
4. Seidah NG, (2011) What lies ahead for the proprotein convertases? Ann N Y Acad Sci 1220: 149-161.
5. Dikeakos JD, Mercure C, Lacombe MJ, Seidah NG, Reudelhuber TL, et al. (2007) PC1/3, PC2 and PC5/6A are targeted to dense core secretory granules by a common mechanism. FEBS J 274: 4094-4102.
6. Benjannet S, Rondeau N, Day R, Chrétien M, Seidah NG, et al. (1991) PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues. Proc Natl Acad Sci U S A 88: 3564-3568.
7. Zhou Y, Rovere C, Kitabgi P, Lindberg I, (1995) Mutational analysis of PC1 (SPC3) in PC12 cells. 66-kDa PC1 is fully functional. J Biol Chem 270: 24702-24706.
8. Goodman LJ, Gorman CM, (1994) Autoproteolytic activation of the mouse prohormone convertase mPC1. Biochem Biophys Res Commun 201: 795-804.
9. Benjannet S, Rondeau N, Paquet L, Boudreault A, Lazure C, et al. (1993) Comparative biosynthesis, covalent post-translational modifications and efficiency of prosegment cleavage of the prohormone convertases PC1 and PC2: glycosylation, sulphation and identification of the intracellular site of prosegment cleavage of PC1 and PC2. Biochem J 294: 735-743.
10. Zhou A, Mains RE, (1994) Endoproteolytic processing of proopiomelanocortin and prohormone convertases 1 and 2 in neuroendocrine cells overexpressing prohormone convertases 1 or 2. J Biol Chem 269: 17440-17447.
11. Zhou Y, Lindberg I, (1993) Purification and characterization of the prohormone convertase PC1(PC3). J Biol Chem 268: 5615-5623.
12. Demaurex N, (2002) pH Homeostasis of cellular organelles. News Physiol Sci 17: 1-5.
13. Mitchell KJ, Pinton P, Varadi A, Tacchetti C, Ainscow EK, et al. (2001) Dense core secretory vesicles revealed as a dynamic Ca(2+) store in neuroendocrine cells with a vesicle-associated membrane protein aequorin chimaera. J Cell Biol 155: 41-51.
14. Davidson HW, (2004) (Pro)Insulin processing: a historical perspective. Cell Biochem Biophys 40: 143-158.
15. Jean F, Basak A, Rondeau N, Benjannet S, Hendy GN, et al. (1993) Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells. Biochem J 292: 891-900.
16. Izidoro MA, Gouvea IE, Santos JAN, Assis DM, Oliveira V, et al. (2009) A study of human furin specificity using synthetic peptides derived from natural substrates, and effects of potassium ions. Arch Biochem Biophys 487: 105-114.
17. Basak A, Ernst B, Brewer D, Seidah NG, Munzer JS, et al. (1997) Histidine-rich human salivary peptides are inhibitors of proprotein convertases furin and PC7 but act as substrates for PC1. J Pept Res 49: 596-603.
18. Lindberg I, Zhou Y, Orlando F, (1995) Overexpression of neuropeptide precursors and processing enzymes. Peptidases and neuropeptide processing, Vol. 23 Methods in Neuroscience San Diego Academic Press pp. 94-108.
19. Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
20. Hirata I, Cesari M, Nakaie C, Boschov P, Ito A, et al. (1994) Internally quenched fluorogenic protease substrates: solid-phase synthesis and fluorescence spectroscopy of peptides containing orth-aminobenzoyl/dinitrophenyl groups as donor acceptor pairs. Lett Pept Sci 27: 299-301.
21. Korkmaz B, Attucci S, Juliano MA, Kalupov T, Jourdan ML, et al. (2008) Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates. Nat Protoc 3: 991-1000.
22. Neet KE, Ainslie GR, (1980) Hysteretic enzymes. Methods Enzymol 64: 192-226.
23. Araujo MC, Melo RL, Cesari MH, Juliano MA, Juliano L, et al. (2000) Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I-converting enzyme. Biochemistry 39: 8519-8525.
24. Hoshino A, Kowalska D, Jean F, Lazure C, Lindberg I, et al. (2011) Modulation of PC1/3 Activity by Self-Interaction and Substrate Binding. Endocrinology 152: 1402-1411.
25. Zhang D, Kovach IM, (2005) Full and partial deuterium solvent isotope effect studies of alpha-thrombin-catalyzed reactions of natural substrates. J Am Chem Soc 127: 3760-3766.
26. Izidoro MA, Assis DM, Oliveira V, Santos JAN, Juliano MA, et al. (2010) Effects of magnesium ions on recombinant human furin: selective activation of hydrolytic activity upon substrates derived from virus envelope glycoprotein. Biol Chem 391: 1105-1112.
27. Madan G, Rao M, (1996) Physiological and clinical importance of nitric oxide. Indian J Med Sci 50: 318-324.
28. Frieden C, (1979) Slow transitions and hysteretic behavior in enzymes. Annu Rev Biochem 48: 471-489.
29. Frieden C, (1970) Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept. J Biol Chem 245: 5788-5799.
30. Masson P, Goldstein BN, Debouzy JC, Froment MT, Lockridge O, et al. (2004) Damped oscillatory hysteretic behaviour of butyrylcholinesterase with benzoylcholine as substrate. Eur J Biochem 271: 220-234.
31. Kurganov BI, Dorozhko AK, Kagan ZS, Yakovlev VA, (1976) The theoretical analysis of kinetic behaviour of kinetic behaviour of "hysteretic" allosteric enzymes. III. Dissociating and associating enzyme systems in which the rate of installation of equilibrium between the oligomeric forms in comparable to that of enzymatic reaction. J Theor Biol 60: 287-299.
32. Masson P, Lockridge O, (2010) Butyrylcholinesterase for protection from organophosphorus poisons: catalytic complexities and hysteretic behavior. Arch Biochem Biophys 494: 107-120.
33. Scamuffa N, Calvo F, Chrétien M, Seidah NG, Khatib AM, et al. (2006) Proprotein convertases: lessons from knockouts. FASEB J 20: 1954-1963.