Cystatin superfamily

Journal of Health Care for the Poor and Underserved

Volumn 21, Issue 1 SUPPL. 1, 2010, Pages 51-70

  Ochieng, Josiah ^a   Chaudhuri, Gautam ^b  

^a MEHARRY MEDICAL COLLEGE   (United States)

^b Department of Biochemistry   (United States)

Author keywords

Cystatin; Fetuin A; Metalloproteinases; Neurodegenerative; Tumorigenesis

Indexed keywords

CYSTATIN; MATRIX METALLOPROTEINASE;

ARTICLE; CHEMISTRY; DEGENERATIVE DISEASE; GLOMERULUS FILTRATION RATE; HUMAN; IMMUNOMODULATION; ONCOGENESIS AND MALIGNANT TRANSFORMATION; PHYSIOLOGY; STRUCTURE ACTIVITY RELATION;

CYSTATINS; GLOMERULAR FILTRATION RATE; HUMANS; IMMUNOMODULATION; MATRIX METALLOPROTEINASES; NEOPLASTIC PROCESSES; NEURODEGENERATIVE DISEASES; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 77249109808     PISSN: 10492089     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (110)

1. Turk V, Bode W. Te cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 1991 Jul. 22;285(2):213-9.
2. Cornwall GA, Hsia N. A new subgroup of the family 2 cystatins. Mol Cell Endocrinol. 2003 Feb. 28;200 (1-2) :1-8.
3. Ni J, Abrahamson M, Zhang M. Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins. J Biol Chem. 1997 Apr. 18;272(16):10853-8.
4. Tompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positionspecific gap penalties and weight matrix choice. Nucleic Acids Res. 1994 Nov. 11; 22(22):4673-80.
5. Chen J, Anderson JB, DeWeese-Scott C, et al. MMDB: Entrez's 3D-structure database. Nucleic Acids Res. 2003 Jan 1;31(1):474-7.
6. Shimba N, Kariya E, Tate S, et al. Structural comparison between wild-type and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the alpha-helix conformation? J Struct Funct Genomics. 2000;1(1):26-42.
7. Brown WM, Dziegielewska KM. Friends and relations of the cystatin superfamily-new members and their evolution. Protein Sci. 1997 Jan;6(1):5-12.
8. Brown WM, Saunders NR, Mollgard K, et al. Fetuin-an old friend revisited. Bioessays. 1992 Nov;14(11):749-55.
9. Winderickx J, Hemschoote K, De Clercq N, et al. Tissue-specific expression and androgen regulation of different genes encoding rat prostatic 22-kilodalton glycoproteins homologous to human and rat cystatin. Mol Endocrinol. 1990 Apr;4(4):657-67.
10. Devos A, De Clercq N, Vercaeren I, et al. Structure of rat genes encoding androgenregulated cystatin-related proteins (CRPs) : a new member of the cystatin superfamily. Gene. 1993 Mar. 30;125(2):159-67.
11. Hu B, Coulson L, Moyer B, et al. Isolation and molecular cloning of a novel bone phosphoprotein related in sequence to the cystatin family of thiol protease inhibitors. J Biol Chem. 1995 Jan 6;270(1):431-6.
12. Ni J, Fernandez MA, Danielsson L, et al. Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor. J Biol Chem. 1998 Sep. 18;273(38):24797-804.
13. Sotiropoulou G, Anisowicz A, Sager R. Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. J Biol Chem. 1997 Jan 10;272(2):903-10.
14. Kopitar M, Ritonja A, Popovic T, et al. A new type of low-molecular mass cysteine proteinase inhibitor from pig leukocytes. Biol Chem Hoppe Seyler. 1989 Oct;370(10):1145-51.
15. Ritonja A, Kopitar M, Jerala R, et al. Primary structure of a new cysteine proteinase inhibitor from pig leucocytes. FEBS Lett. 1989 Sep. 25;255(2):211-4.
16. Cornwall GA, Orgebin-Crist MC, Hann SR. Te CRES gene: a unique testis-regulated gene related to the cystatin family is highly restricted in its expression to the proximal region of the mouse epididymis. Mol Endocrinol. 1992 Oct;6(10):1653-64.
17. Liotta LA, Rao CN, Barsky SH. Tumor invasion and the extracellular matrix. Lab Invest. 1983 Dec;49(6):636-49.
18. Mignatti P, Robbins E, Riflkin DB. Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell. 1986 Nov. 21;47(4):487-98.
19. Chambers AF, Matrisian LM. Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst. 1997 Sep. 3;89(17):1260-70.
20. Cudic M, Fields GB. Extracellular proteases as targets for drug development. Curr Protein Pept Sci. 2009 Aug;10(4):297-307.
21. Eder J, Hommel U, Cumin F, et al. Aspartic proteases in drug discovery. Curr Pharm Des. 2007;13(3):271-85.
22. Yan S, Sameni M, Sloane BF. Cathepsin B and human tumor progression. Biol Chem. 1998 Feb;379(2):113-23.
23. Koblinski JE, Ahram M, Sloane BF. Unraveling the role of proteases in cancer. Clin Chim Acta. 2000 Feb. 15;291(2):113-35.
24. Sinha AA, Gleason DF, Deleon OF, et al. Localization of a biotinylated cathepsin B oligonucleotide probe in human prostate including invasive cells and invasive edges by in situ hybridization. Anat Rec. 1993 Feb;235(2):233-40.
25. Visscher DW, Sloane BF, Sameni M, et al. Clinicopathologic significance of cathepsin B immunostaining in transitional neoplasia. Mod Pathol. 1994 Jan;7(1):76-81.
26. Smith KJ, Pacey GE. Reverse dual phase gas diffusion flow injection analysis. Talanta. 1993 Dec;40(12):1961-6.
27. Kos J, Werle B, Lah T, et al. Cysteine proteinases and their inhibitors in extracellular fluids: markers for diagnosis and prognosis in cancer. Int J Biol Markers. 2000 Jan-Mar;15(1):84-9.
28. Kos J, Krasovec M, Cimerman N, et al. Cysteine proteinase inhibitors stefin A, stefin B, and cystatin C in sera from patients with colorectal cancer: relation to prognosis. Clin Cancer Res. 2000 Feb;6(2):505-11.
29. Zore I, Krasovec M, Cimerman N, et al. Cathepsin B/cystatin C complex levels in sera from patients with lung and colorectal cancer. Biol Chem. 2001 May;382(5):805-10.
30. Kothapalli R, Bailey RD, Kusmartseva I, et al. Constitutive expression of cytotoxic proteases and down-regulation of protease inhibitors in LGL leukemia. Int J Oncol. 2003 Jan;22(1):33-9.
31. Korolenko TA, Poteryaeva ON, Falameeva OV, et al. Cystein proteinase inhibitor stefin A as an indicator of eficiency of tumor treatment in mice. Bull Exp Biol Med. 2003 Jul;136(1):46-8.
32. Sokol J P, Schiemann W P. Cystatin C antagonizes transforming growth factor beta signaling in normal and cancer cells. Mol Cancer Res. 2004 Mar;2(3):183-95.
33. Blobe GC, Schiemann W P, Lodish HF. Role of transforming growth factor beta in human disease. N Engl J Med. 2000 May 4;342(18):1350-8.
34. Massague J, Blain S W, Lo RS. TGFbeta signaling in growth control, cancer, and heritable disorders. Cell. 2000 Oct. 13;103(2):295-309.
35. Swallow CJ, Partridge EA, Macmillan JC, et al. Alpha2HS-glycoprotein, an antagonist of transforming growth factor beta in vivo, inhibits intestinal tumor progression. Cancer Res. 2004 Sep. 15;64(18):6402-9.
36. Zhang J, Shridhar R, Dai Q, et al. Cystatin M: a novel candidate tumor suppressor gene for breast cancer. Cancer Res. 2004 Oct. 1;64(19):6957-64.
37. Hsu SJ, Nagase H, Balmain A. Identification of Fetuin-B as a member of a cystatinlike gene family on mouse chromosome 16 with tumor suppressor activity. Genome. 2004 Oct;47(5):931-46.
38. Kos J, Stabuc B, Schweiger A, et al. Cathepsins B, H, and L and their inhibitors stefin A and cystatin C in sera of melanoma patients. Clin Cancer Res. 1997 Oct; 3(10):1815-22.
39. Huh CG, Hakansson K, Nathanson CM, et al. Decreased metastatic spread in mice homozygous for a null allele of the cystatin C protease inhibitor gene. Mol Pathol. 1999 Dec;52(6):332-40.
40. Kundranda MN, Henderson M, Carter KJ, et al. Te serum glycoprotein fetuin-A promotes Lewis lung carcinoma tumorigenesis via adhesive-dependent and adhesive independent mechanisms. Cancer Res. 2005 Jan 15;65(2):499-506.
41. Nie Z. Fetuin: its enigmatic property of growth promotion. Am J Physiol. 1992 Sep; 263(3 Pt 1):C551-62.
42. Matrisian LM. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet. 1990 Apr;6(4):121-5.
43. Coussens LM, Werb Z. Matrix metalloproteinases and the development of cancer. Chem Biol. 1996 Nov;3(11):895-904.
44. Rudolph-Owen LA, Chan R, Muller WJ, et al. Te matrix metalloproteinase matrilysin influences early-stage mammary tumorigenesis. Cancer Res. 1998 Dec. 1;58(23):5500-6.
45. Walakovits LA, Moore VL, Bhardwaj N, et al. Detection of stromelysin and collagenase in synovial fluid from patients with rheumatoid arthritis and posttraumatic knee injury. Arthritis Rheum. 1992 Jan;35(1):35-42.
46. Dollery CM, McEwan JR, Henney AM. Matrix metalloproteinases and cardiovascular disease. Circ Res. 1995 Nov;77(5):863-8.
47. Grant GA, Goldberg GI, Wilhelm SM, et al. Activation of extracellular matrix metalloproteases by proteases and organomercurials. Matrix Suppl. 1992;1:217-23.
48. Fridman R, Toth M, Pena D, et al. Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2). Cancer Res. 1995 Jun. 15;55(12):2548-55.
49. Ellerbroek SM, Wu YI, Stack MS. Type I collagen stabilization of matrix metalloproteinase-2. Arch Biochem Biophys. 2001 Jun. 1;390(1):51-6.
50. Ray S, Lukyanov P, Ochieng J. Members of the cystatin superfamily interact with MMP-9 and protect it from autolytic degradation without affecting its gelatinolytic activities. Biochim Biophys Acta. 2003 Dec. 1;1652(2):91-102.
51. Yan L, Borregaard N, Kjeldsen L, et al. Te high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). Modulation of MMP-9 activity by NGAL. J Biol Chem. 2001 Oct. 5;276(40):37258-65. Epub 2001 Aug. 2.
52. Ochieng J, Fridman R, Nangia-Makker P, et al. Galectin-3 is a novel substrate for human matrix metalloproteinases-2 and-9. Biochemistry. 1994 Nov. 29;33(47):14109-14.
53. Mai J, Waisman DM, Sloane BF. Cell surface complex of cathepsin B/annexin II tetramer in malignant progression. Biochim Biophys Acta. 2000 Mar. 7;1477 (1-2) :215-30.
54. Hajjar KA, Jacovina AT, Chacko J. An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II. J Biol Chem. 1994 Aug. 19; 269(33):21191-7.
55. Chung CY, Erickson H P. Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J Cell Biol. 1994 Jul;126(2):539-48.
56. Kojima K, Yamamoto K, Irimura T, et al. Characterization of carbohydrate-binding protein p33/41: relation with annexin I V, molecular basis of the doublet forms (p33 and p41), and modulation of the carbohydrate binding activity by phospholipids. J Biol Chem. 1996 Mar. 29;271(13):7679-85.
57. Kundranda MN, Ray S, Saria M, et al. Annexins expressed on the cell surface serve as receptors for adhesion to immobilized fetuin-A. Biochim Biophys Acta. 2004 Aug. 23;1693(2):111-23.
58. Ochieng J, Warfield P, Green B. Interactions of gelatinases with soluble and immobilized fetuin-A and asialofetuin. Arch Biochem Biophys. 1995 Sep. 10;322(1):250-5.
59. Ochieng J, Green B. Te interactions of alpha 2HS glycoprotein with metalloproteinases. Biochem Mol Biol Int. 1996 Sep;40(10):13-20.
60. Tajirian T, Dennis JW, Swallow CJ. Regulation of human monocyte proMMP-9 production by fetuin, an endogenous TGF-beta antagonist. J Cell Physiol. 2000 Nov;185(2):174-83.
61. Massey D. Commentary: clinical diagnostic use of cystatin C. J Clin Lab Anal. 2004; 18(1):55-60.
62. Perrone RD, Madias NE, Levey AS. Serum creatinine as an index of renal function: new insights into old concepts. Clin Chem. 1992 Oct;38(10):1933-53.
63. Simonsen O, Grubb A, Tysell H. Te blood serum concentration of cystatin C (gamma-trace) as a measure of the glomerular filtration rate. Scand J Clin Lab Invest. 1985 Apr;45(2):97-101.
64. Abrahamson M, Barrett AJ, Salvesen G, et al. Isolation of six cysteine proteinase inhibitors from human urine. Teir physicochemical and enzyme kinetic properties and concentrations in biological fluids. J Biol Chem. 1986 Aug. 25;261(24):11282-9.
65. Reed CH. Diagnostic applications of cystatin C. Br J Biomed Sci. 2000;57(4):323-9.
66. van Oss CJ, Bronson PM, Border JR. Changes in the serum alpha glycoprotein distribution in trauma patients. J Trauma. 1975 May;15(5):451-5.
67. Lebreton J P, Joisel F, Raoult J P, et al. Serum concentration of human alpha 2 HS glycoprotein during the inflammatory process: evidence that alpha 2 HS glycoprotein is a negative acute-phase reactant. J Clin Invest. 1979 Oct;64(4):1118-29.
68. van Oss CJ, Gillman CF, Bronson PM, et al. Opsonic properties of human serum alpha-2 HS glycoprotein. Immunol Commun. 1974;3(4):329-35.
69. Lewis JG, Andre CM. Enhancement of human monocyte phagocytic function by alpha 2HS glycoprotein. Immunology. 1981 Mar;42(3):481-7.
70. Lewis JG, Andre CM. Effect of human alpha 2HS glycoprotein on mouse macrophage function. Immunology. 1980 Mar;39(3):317-22.
71. Wang H, Zhang M, Soda K, et al. Fetuin protects the fetus from TNF. Lancet. 1997 Sep. 20;350(9081):861-2.
72. Zhang M, Caragine T, Wang H, et al. Spermine inhibits proinflammatory cytokine synthesis in human mononuclear cells: a counterregulatory mechanism that restrains the immune response. J Exp Med. 1997 May 19;185(10):1759-68.
73. Wang H, Zhang M, Bianchi M, et al. Fetuin (alpha2-HS-glycoprotein) opsonizes cationic macrophagedeactivating molecules. Proc Natl Acad Sci U S A. 1998 Nov. 24;95(24):14429-34.
74. Chapman HA Jr, Reilly JJ Jr, Yee R, et al. Identification of cystatin C, a cysteine proteinase inhibitor, as a major secretory product of human alveolar macrophages in vitro. Am Rev Respir Dis. 1990 Mar;141(3):698-705.
75. Pierre P, Mellman I. Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells. Cell. 1998 Jun. 26;93(7):1135-45.
76. Riese RJ, Wolf PR, Bromme D, et al. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity. 1996 Apr; 4(4):357-66.
77. Nakagawa T, Roth W, Wong P, et al. Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Science. 1998 Apr;280(5362):450-3.
78. Nakagawa TY, Rudensky AY. Te role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation. Immunol Rev. 1999 Dec;172:121-9.
79. Schonemeyer A, Lucius R, Sonnenburg B, et al. Modulation of human T cell responses and macrophage functions by onchocystatin, a secreted protein of the filarial nematode Onchocerca volvulus. J Immunol. 2001 Sep. 15;167(6):3207-15.
80. Verdot L, Lalmanach G, Vercruysse V, et al. Cystatins up-regulate nitric oxide release from interferon-gamma-activated mouse peritoneal macrophages. J Biol Chem. 1996 Nov. 8;271(45):28077-81.
81. Hartmann S, Schonemeyer A, Sonnenburg B, et al. Cystatins of filarial nematodes up-regulate the nitric oxide production of interferon-gamma-activated murine macrophages. Parasite Immunol. 2002 May;24(5):253-62.
82. Marletta MA. Nitric oxide synthase structure and mechanism. J Biol Chem. 1993 Jun. 15;268(17):12231-4.
83. Kolb H, Kolb-Bachofen V. Nitric oxide: a pathogenetic factor in autoimmunity. Immunol Today. 1992 May;13(5):157-60.
84. Das L, Datta N, Bandyopadhyay S, et al. Successful therapy of lethal murine visceral leishmaniasis with cystatin involves up-regulation of nitric oxide and a favorable T cell response. J Immunol. 2001 Mar. 15;166(6):4020-8.
85. Denham S, Rowland IJ. Inhibition of the reactive proliferation of lymphocytes by activated macrophages: the role of nitric oxide. Clin Exp Immunol. 1992 Jan;87(1):157-62.
86. Kawabe T, Isobe KI, Hasegawa Y, et al. Immunosuppressive activity induced by nitric oxide in culture supernatant of activated rat alveolar macrophages. Immunology. 1992 May;76(1):72-8.
87. Yamada M. Cerebral amyloid angiopathy: an overview. Neuropathology. 2000 Mar; 20(1):8-22.
88. Revesz T, Ghiso J, Lashley T, et al. Cerebral amyloid angiopathies: a pathologic, biochemical, and genetic view. J Neuropathol Exp Neurol. 2003 Sep;62(9):885-98.
89. Fujihara S, Shimode K, Nakamura M, et al. Cerebral amyloid angiopathy with the deposition of cystatin C (gamma-trace) and beta-protein. Prog Clin Biol Res. 1989;317:939-44.
90. Maruyama K, Ikeda S, Ishihara T, et al. Immunohistochemical characterization of cerebrovascular amyloid in 46 autopsied cases using antibodies to beta protein and cystatin C. Stroke. 1990 Mar;21(3):397-403.
91. Vattemi G, Engel WK, McFerrin J, et al. Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis muscles. J Neurochem. 2003 Jun;85(6):1539-46.
92. Mitchell TI, Jefrey JJ, Palmiter RD, et al. Te acute phase reactant serum amyloid A (SAA3) is a novel substrate for degradation by the metalloproteinases collagenase and stromelysin. Biochim Biophys Acta. 1993 Mar. 21;1156(3):245-54.
93. Stix B, Kahne T, Sletten K, et al. Proteolysis of AA amyloid fbril proteins by matrix metalloproteinases-1,-2, and-3. Am J Pathol. 2001 Aug;159(2):561-70.
94. Backstrom JR, Lim G P, Cullen MJ, et al. Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1-40). J Neurosci. 1996 Dec. 15;16(24):7910-9.
95. Sousa MM, do Amaral JB, Guimaraes A, et al. Up-regulation of the extracellular matrix remodeling genes, biglycan, neutrophil gelatinase- associated lipocalin and matrix metal loproteinase-9 in familial amyloid polyneuropathy. Faseb J. 2005 Jan;19(1):124-6.
96. Kjeldsen L, Johnsen AH, Sengelov H, et al. Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. J Biol Chem. 1993 May 15;268(14):10425-32.
97. Jensson O, Gudmundsson G, Arnason A, et al. Hereditary cystatin C (gamma-trace) amyloid angiopathy of the CNS causing cerebral hemorrhage. Acta Neurol Scand. 1987 Aug;76(2):102-14.
98. Levy E, Lopez-Otin C, Ghiso J, et al. Stroke in Icelandic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteases. J Exp Med. 1989 May 1;169(5):1771-8.
99. Carrell RW, Gooptu B. Conformational changes and disease-serpins, prions and Alzheimer's. Curr Opin Struct Biol. 1998 Dec;8(6):799-809.
100. Kelly J W. Te alternative conformations of amyloidogenic proteins and their multistep assembly pathways. Curr Opin Struct Biol. 1998 Feb;8(1):101-6.
101. Staniforth RA, Giannini S, Higgins LD, et al. Tree-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. Embo J. 2001 Sep. 3;20(17):4774-81.
102. Janowski R, Kozak M, Jankowska E, et al. Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. Nat Struct Biol. 2001 Apr;8(4):316-20.
103. Ekiel I, Abrahamson M. Folding-related dimerization of human cystatin C. J Biol Chem. 1996 Jan 19;271(3):1314-21.
104. Jerala R, Zerovnik E. Accessing the global minimum conformation of stefin A dimer by annealing under partially denaturing conditions. J Mol Biol. 1999 Sep; 291(5):1079-89.
105. Zerovnik E, Jerala R, Kroon-Zitko L, et al. Characterization of the equilibrium intermediates in acid denaturation of human stefin B. Eur J Biochem. 1997 Apr. 15; 245(2):364-72.
106. Ekiel I, Abrahamson M, Fulton DB, et al. NMR structural studies of human cystatin C dimers and monomers. J Mol Biol. 1997 Aug;271(2):266-77.
107. Bollengier F. Cystatin C, alias post-gamma-globulin: a marker for multiple sclerosis? J Clin Chem Clin Biochem. 1987 Dec;25(9):589-93.
108. Nagai A, Murakawa Y, Terashima M, et al. Cystatin C and cathepsin B in CSF from patients with inflammatory neurologic diseases. Neurology. 2000;55:1828-32.
109. Rinne R, Saukko P, Jarvinen M, et al. Reduced cystatin B activity correlates with enhanced cathepsin activity in progressive myoclonus epilepsy. Ann Med. 2002;34(5):380-5.
110. Shannon P, Pennacchio LA, Houseweart MK, et al. Neuropathological changes in a mouse model of progressive myoclonus epilepsy: cystatin B deficiency and Unverricht-Lundborg disease. J Neuropathol Exp Neurol. 2002 Dec;61(12):1085-91.