Correlation of serpin-protease expression by comparative analysis of real-time PCR profiling data

被引:16
作者
Badola, Sunita
Spurling, Heidi
Robison, Keith
Fedyk, Eric R.
Silverman, Gary A.
Strayle, Jochen
Kapeller, Rosana
Tsu, Christopher A.
机构
[1] Millennium Pharmaceut Inc, Cambridge, MA 02139 USA
[2] Univ Pittsburgh, Magee Womens Hosp, Sch Med, Dept Pediat, Pittsburgh, PA 15213 USA
[3] Bayer HealthCare, D-42096 Wuppertal, Germany
关键词
protease; serpin; cancer; imbalance; expression profiling; gene correlation; PCR;
D O I
10.1016/j.ygeno.2006.03.017
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Imbalanced protease activity has long been recognized in the progression of disease states such as cancer and inflammation. Serpins, the largest family of endogenous protease inhibitors, target a wide variety of serine and cysteine proteases and play a role in a number of physiological and pathological states. The expression profiles of 20 serpins and 105 serine and cysteine proteases were determined across a panel of normal and diseased human tissues. In general, expression of serpins was, highly restricted in both normal and diseased tissues, suggesting defined physiological roles for these protease inhibitors. A high correlation in expression for a particular serpin-protease pair in healthy tissues was often predictive of a biological interaction. The most striking finding was the dramatic change observed in the regulation of expression between proteases and their cognate inhibitors in diseased tissues. The loss of regulated serpin-protease matched expression may underlie the imbalanced protease activity observed in pathological states. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:173 / 184
页数:12
相关论文
共 58 条
  • [11] Identification of the substrates for plasma hyaluronan binding protein
    Choi-Miura, NH
    Yoda, M
    Saito, K
    Takahashi, K
    Tomita, M
    [J]. BIOLOGICAL & PHARMACEUTICAL BULLETIN, 2001, 24 (02) : 140 - 143
  • [12] ChoiMiura NH, 1996, J BIOCHEM, V119, P1157
  • [13] α1-antitrypsin deficiency:: Biological answers to clinical questions
    Coakley, RJ
    Taggart, C
    O'Neill, S
    McElvaney, NG
    [J]. AMERICAN JOURNAL OF THE MEDICAL SCIENCES, 2001, 321 (01) : 33 - 41
  • [14] The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites
    Cooley, J
    Takayama, TK
    Shapiro, SD
    Schechter, NM
    Remold-O'Donnell, E
    [J]. BIOCHEMISTRY, 2001, 40 (51) : 15762 - 15770
  • [15] Expression, purification and inhibitory properties of human proteinase inhibitor 8
    Dahlen, JR
    Foster, DC
    Kisiel, W
    [J]. BIOCHEMISTRY, 1997, 36 (48) : 14874 - 14882
  • [16] Inhibition of soluble recombinant furin by human proteinase inhibitor 8
    Dahlen, JR
    Jean, F
    Thomas, G
    Foster, DC
    Kisiel, W
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (04) : 1851 - 1854
  • [17] Eddy S R, 1995, J Comput Biol, V2, P9, DOI 10.1089/cmb.1995.2.9
  • [18] Base-calling of automated sequencer traces using phred.: II.: Error probabilities
    Ewing, B
    Green, P
    [J]. GENOME RESEARCH, 1998, 8 (03): : 186 - 194
  • [19] Functional discovery via a compendium of expression profiles
    Hughes, TR
    Marton, MJ
    Jones, AR
    Roberts, CJ
    Stoughton, R
    Armour, CD
    Bennett, HA
    Coffey, E
    Dai, HY
    He, YDD
    Kidd, MJ
    King, AM
    Meyer, MR
    Slade, D
    Lum, PY
    Stepaniants, SB
    Shoemaker, DD
    Gachotte, D
    Chakraburtty, K
    Simon, J
    Bard, M
    Friend, SH
    [J]. CELL, 2000, 102 (01) : 109 - 126
  • [20] Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation
    Huntington, JA
    Kjellberg, M
    Stenflo, J
    [J]. STRUCTURE, 2003, 11 (02) : 205 - 215