Identification and purification from the plasma of Type 1 diabetic subjects of a proteolytically active Grp94: Evidence that Grp94 is entirely responsible for plasma proteolytic activity

Diabetologia

Volumn 46, Issue 7, 2003, Pages 996-1006

  Pagetta, A ^a   Folda, A ^a   Brunati, A M ^a   Finotti, P ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

Blood proteins; Diabetes mellitus; Heat shock proteins; Insulin dependent; Peptide hydrolase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALPHA 1 ANTITRYPSIN; CASEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; IMMUNOGLOBULIN G; PEPTIDE HYDROLASE; PHENYLACETIC ACID DERIVATIVE; PLASMA PROTEIN; POLYCLONAL ANTIBODY;

ADULT; AFFINITY CHROMATOGRAPHY; ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; FAST PROTEIN LIQUID CHROMATOGRAPHY; FEMALE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; IMMUNOBLOTTING; IMMUNOPRECIPITATION; INSULIN DEPENDENT DIABETES MELLITUS; ION EXCHANGE; MALE; MASS SPECTROMETRY; PLASMA; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN PURIFICATION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;

ADULT; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DIABETES MELLITUS, TYPE 1; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FEMALE; HSP70 HEAT-SHOCK PROTEINS; HUMANS; KINETICS; MALE; MEMBRANE PROTEINS; MIDDLE AGED; MOLECULAR CHAPERONES; REFERENCE VALUES;

EID: 0042071558     PISSN: 0012186X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00125-003-1133-5     Document Type: Article

References (44)

1. Donnelly R, Emslie-Smith AM, Gardner D, Morris AD (2000) Vascular complications of diabetes. Br Med J 320:1062-1066
2. Yamashita T (1995) Increased transendothelial permeation of albumin by high glucose concentration. Metabolism 44:739-744
3. Microalbuminuria Collaborative Study Group, UK (1995) Intensive therapy and progression to clinical albuminuria in patients with insulin dependent diabetes mellitus and microalbuminuria. Br Med J 311:973-977
4. Marre M (1999) Genetics and the prediction of complications in type 1 diabetes. Diabetes Care S2:B53-B58
5. Rogus JJ, Warram JH, Krolewski AS (2002) Genetic studies of late diabetic complications. The overlooked importance of diabetes duration before complication onset. Diabetes 51:1655-1662
6. Atkinson M, Eisenbarth GS (2001) Type 1 diabetes: new perspectives on disease pathogenesis and treatment. Lancet 358:221-229
7. Du XL, Sui GZ, Stockklauser-Färber K et al. (1998) Induction of apoptosis by high proinsulin and glucose in cultured human umbelical vein endothelial cells is mediated by reactive oxygen species. Diabetologia 41:249-256
8. Fornoni A, Striker LJ, Zheng F, Striker GE (2002) Reversibility of glucose-induced changes in mesangial cell extracellular matrix depends on the genetic background. Diabetes 51:499-505
9. Finotti P, Piccoli A, Carraro P (1992) Alteration of plasma proteinase-antiproteinase system in type 1 diabetic patients. Influence of sex and relationship with metabolic control. Diabets Res Clin Pract 18:35-42
10. Raghotama C, Rao P (1996) Degradation of glycated hemoglobin by erythrocytic proteolytic enzymes. Clin Chim Acta 245:201-208
11. Yamamoto H, Maake C, Murphy LJ (1999) Enhanced proteolytic activity directed against the N-terminal of IGF-I in diabetic rats. J Endocrinol 162:243-250
12. Shinada M, Akdeniz A, Panagiotopoulos S, Jerums G, Bach LA (2000) Proteolysis of insulin-like growth factor-binding protein-3 is increased in urine from patients with diabetic nephropathy. J Clin Endocrinol 85:1163-1169
13. Carmassi F, Morale M, Puccetti R et al. (1992) Coagulation and fibrinolytic system impairment in insulin dependent diabetes mellitus. Thromb Res 67:643-654
14. 2-macroglobulin in diabetes. Clin Chim Acta 154:85-101
15. Carr ME (2001) Diabetes mellitus. A hypercoagulable state. J Diabetes Complications 15:44-54
16. +-ATPase stimulating substance from plasma of insulin-dependent diabetics and its identification as α1-antitrypsin. Biochim Biophys Acta 1139: 122-132
17. Sandler M, Stewart RI, Gemperly BM, Hanekom C, Kühn H (1987) Serum alpha-1-protease inhibitor activity and pulmonary function in young insulin-dependent diabetic subjects. Respiration 52: 281-289
18. Hu SI, Carozza M, Klein M, Nantermet P, Luk D, Crow RM (1998) Human HtrA, an evolutionarily conserved serine protease identified as a differentially expressed gene product in osteoarthritic cartilage. J Biol Chem 273:34406-34412
19. Erlanger BF, Kokowsky N, Cohen W (1961) The preparation and properties of two new chromogenic substrates of trypsin. Arch Biochem Biophys 95:271-278
20. Watanabe H, Tanase S, Nakajou K, Maruyama T, Kragh-Hansen U, Otagiri M (2000) Role of Arg-410 and Tyr-411 in human serum albumin for ligand binding and esterase-like activity. Biochem J 349:813-819
21. Finotti P, Pagetta A, Ashton T (2001) The oxidative mechanism of heparin interferes with radical production by glucose and reduces the degree of glycooxidative modifications on human serum albumin. Eur J Biochem 268:2193-2200
22. Pinna LA, Donella A, Clari G, Moret V (1976) Preferential dephosphorylation of protein bound phosphorylthreonine and phosphorylserine residues by cytosol and mitochondrial "casein phosphatases". Biochem Biophys Res Commun 70:1308-1312
23. Li Z, Srivastava PK (1993) Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation. EMBO J 12:3143-3151
24. Rosser MFN, Nicchitta CV (2000) Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, Grp94. I. Evidence for allosteric regulation of ligand binding. J Biol Chem 275:22798-22805
25. Wallin RPA, Lundqvist A, Moré SH, Bonin A von, Kiessling R, Ljunggren H-J (2002) Heat shoch proteins as activators of the innate immune system. Trends Immunol 23:130-135
26. Nicchitta CV (1998) Biochemical, cell biological and immunological issues surrounding the endoplasmatic reticulum chaperone GRP94/gp96. Curr Opin Immunol 10:103-109
27. Suzue K, Zhou X, Eisen HN, Young RA (1997) Heat shock fusion proteins as vehicles for antigen delivery into the major histocompatibility complex class I presentation pathway. Proc Natl Acad Sci USA 94:13146-13151
28. Binder RJ, Blachere NE, Srivastava PK (2001) Heat shock protein-chaperoned peptides but not free peptides introduced into the cytosol are presented efficiently by major histocompatibility complex I molecules. J Biol Chem 276:17163-17171
29. Linderoth NA, Popowicz A, Sastry S (2000) Identification of the peptide-binding site in the heat shock chaperone/tumor rejection antigen gp96 (Grp94). J Biol Chem 275:5472-5477
30. Li Z, Menoret A, Srivastava P (2002) Role of heat-shock proteins in antigen presentation and cross-presentation. Curr Opin Immunol 14:45-51
31. Asea A, Rehli M, Kabingu E, et al. (2002) Novel signal transduction pathway utilized by extracellular Hsp70. J Biol Chem 277:15028-15034
32. Lee AS (2001) The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem Sci 26:504-510
33. Elias D, Markovits D, Reshef T, Van Der Zee R, Cohen IR (1990) Induction and therapy of autoimmune diabetes in the non-obese diabetic (NOD/Lt) mouse by a 65-kDa heat shock protein. Proc Natl Acad Sci USA 87:1576-1580
34. Burkart V, Liu H, Bellmann K et al. (2000) Natural resistance of human beta cells toward nitric oxide is mediated by heat shock protein 70. J Biol Chem 275:19521-19528
35. Faccio L, Fusco C, Chen A, Martinotti S, Bonventre JV, Zervos AS (2000) Characterization of a novel serine protease that has extensive homology to bacterial heat shoch endoprotease HtrA and is regulated by kidney ischemia. J Biol Chem 275:2581-2588
36. Ménoret A, Li ZL, Niswongers ML, Altmeyer A, Srivastava PK (2001) An endoplasmic reticulum protein implicated in chaperoning peptides to major histocompatibility of class I is an aminopeptidase. J Biol Chem 276:33313-33318
37. Wassenberg JJ, Reed RC, Nicchitta CV (2000) Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, Grp94. II. Ligand-mediated activation of Grp94 molecular chaperone and peptide-binding activity. J Biol Chem 275:22806-22814
38. Sastry S, Linderoth N (1999) Molecular mechanism of peptide loading by the tumor rejection antigen/heat shock chaperone grp96 (GRP94). J Biol Chem 274:12023-12035
39. Wearsh PA, Nicchitta CV (1996) Endoplasmic reticulum chaperone Grp94 subunit assembly is regulated through a defined oligomerization domain. Biochemistry 35:16760-16769
40. Smýkal P, Hrdý, I, Pechan PM (2000) high molecular-mass complexes formed in vivo contain smHSPs and HSP70 and display chaperone-like activity. Eur J Biochem 267:2195-2207
41. Brunati AM, Contri A, Muenchbach M, James P, Marin O, Pinna LA (2000) GRP94 (endoplasmin) co-purifies with and is phosphorylated by Golgi apparatus casein kinase. FEBS Lett 471:151-1554
42. Berwin B, Reed RC, Nicchitta CV (2001) Virally induced lyric cell death elicits the release of immunogenic GRP94/gp96. J Biol Chem 276:21083-21068
43. Melnick J, Aviel S, Argon Y (1992) The endoplasmatic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J Biol Chem 267:21303-21306
44. Singh-Jasuja H (2000) Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptor-mediated endocytosis. J Exp Med 191:1965-1974