Correlation of serpin–protease expression by comparative analysis of real-time PCR profiling data
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 pathologi...
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| Published in: | Genomics (San Diego, Calif.) Vol. 88; no. 2; pp. 173 - 184 |
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| ISSN: | 0888-7543, 1089-8646 |
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| Abstract | 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. |
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| AbstractList | 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. 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.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. |
| Author | Badola, Sunita Robison, Keith Fedyk, Eric R. Strayle, Jochen Silverman, Gary A. Spurling, Heidi Kapeller, Rosana Tsu, Christopher A. |
| Author_xml | – sequence: 1 givenname: Sunita surname: Badola fullname: Badola, Sunita organization: Millennium Pharmaceuticals, Inc., 40 Landsdowne Street, Cambridge, MA 02139, USA – sequence: 2 givenname: Heidi surname: Spurling fullname: Spurling, Heidi organization: Millennium Pharmaceuticals, Inc., 40 Landsdowne Street, Cambridge, MA 02139, USA – sequence: 3 givenname: Keith surname: Robison fullname: Robison, Keith organization: Millennium Pharmaceuticals, Inc., 40 Landsdowne Street, Cambridge, MA 02139, USA – sequence: 4 givenname: Eric R. surname: Fedyk fullname: Fedyk, Eric R. organization: Millennium Pharmaceuticals, Inc., 40 Landsdowne Street, Cambridge, MA 02139, USA – sequence: 5 givenname: Gary A. surname: Silverman fullname: Silverman, Gary A. organization: Department of Pediatrics, University of Pittsburgh School of Medicine, Magee-Women’s Hospital, 300 Halket Street, Pittsburgh, PA 15213, USA – sequence: 6 givenname: Jochen surname: Strayle fullname: Strayle, Jochen organization: Bayer HealthCare AG, 42096 Wuppertal, Germany – sequence: 7 givenname: Rosana surname: Kapeller fullname: Kapeller, Rosana organization: Millennium Pharmaceuticals, Inc., 40 Landsdowne Street, Cambridge, MA 02139, USA – sequence: 8 givenname: Christopher A. surname: Tsu fullname: Tsu, Christopher A. email: tsu@mpi.com organization: Millennium Pharmaceuticals, Inc., 40 Landsdowne Street, Cambridge, MA 02139, USA |
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| Keywords | CHF Expression profiling UUI SMC RSL IBD siRNA PBMC BM-MNC Imbalance Protease serpin DRG Gene correlation BPH B2M PCR COPD Cancer Correlation Enzyme Genomics Time Malignant tumor Gene expression Polymerase chain reaction Peptidases Serpin Gene Analysis Hydrolases |
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| SubjectTerms | Amino Acid Sequence Biological and medical sciences Cancer Cell Line Cell Line, Transformed Cysteine Endopeptidases - genetics Cysteine Endopeptidases - metabolism Disease Progression Expression profiling Female Fundamental and applied biological sciences. Psychology Gene correlation Gene Expression Profiling - methods Gene Expression Regulation Gene Expression Regulation, Enzymologic Genes. Genome Genetics of eukaryotes. Biological and molecular evolution Humans Imbalance Male Molecular and cellular biology Molecular genetics Molecular Sequence Data Neoplasms - genetics Neoplasms - metabolism PCR Polymerase Chain Reaction - methods Protease Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Serpin Serpins - genetics Serpins - metabolism Species Specificity |
| Title | Correlation of serpin–protease expression by comparative analysis of real-time PCR profiling data |
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