Distinct Expression Pattern of Two Related Human Proteins Containing Multiple Types of Protease-Inhibitory Modules
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Mária Trexler
Abstract
We have recently identified a gene (the WFIKKN gene) on human chromosome 16 (16p13.3) that encodes a secreted protein containing WAPtype, Follistatin/ Kazal type, Kunitztype and NTRtype proteaseinhibitory modules and an Immunoglobulin domain [Trexler et al., Proc. Natl. Acad. Sci. USA 98 (2001), 3705 3709]. In the present work we show that a gene on chromosome 17 encodes a WFIKKNrelated protein (WFIKKNRP) that has the same domain organization as the WFIKKN protein. The exonintron structure of the two genes is also similar as both genes have a single phase 0 intron that splits their WAP domains in equivalent positions. In view of the presence of several protease inhibitory modules in these proteins it seems likely that they serve to control the action of multiple types of proteases. The tissue expression pattern of the two proteins, however, is markedly different suggesting that they have distinct biological roles. Whereas the WFIKKN gene is expressed primarily in adult pancreas, liver and thymus but not in brain and ovary, significant expression of the WFIKKNRP gene is observed in ovary, testis and brain, but not in liver. Pronounced differences could also be seen in the case of fetal tissues: expression of the WFIKKN gene was highest in the lung, skeletal muscle and liver, whereas the WFIKKNRP gene was expressed primarily in brain, skeletal muscle, thymus and kidney.
Copyright © 2002 by Walter de Gruyter GmbH & Co. KG
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Artikel in diesem Heft
- Non-Enzymatic Activities of Proteases: From Scepticism to Reality
- The Urokinase Plasminogen Activator Receptor in the Regulation of the Actin Cytoskeleton and Cell Motility
- The Molecular Basis for Anti-Proteolytic and Non-Proteolytic Functions of Plasminogen Activator Inhibitor Type-1: Roles of the Reactive Centre Loop, the Shutter Region, the Flexible Joint Region and the Small Serpin Fragment
- Nervous System Pathology: The Fibrin Perspective
- Post-Transcriptional Regulation of Gene Expression in the Plasminogen Activation System
- Role of Myofibroblasts at the Invasion Front
- Transmodulation of Cell Surface Regulatory Molecules via Ectodomain Shedding
- The Plasminogen Activating System in Periodontal Health and Disease
- Apolipoprotein(a): Structure-Function Relationship at the Lysine-Binding Site and Plasminogen Activator Cleavage Site
- Anti-Invasive Effects of Green Tea Polyphenol EpiGalloCatechin-3-Gallate (EGCG), a Natural Inhibitor of Metallo and Serine Proteases
- Inhibition of Receptor-Dependent Urokinase Signaling by Specific Ser to Glu Substitutions
- Activation of p38 MAP-Kinase and Caldesmon Phosphorylation Are Essential for Urokinase-Induced Human Smooth Muscle Cell Migration
- Growth Factor-Dependent Proliferation and Invasion of Muscle Satellite Cells Require the Cell-Associated Fibrinolytic System
- The Col-1 Module of Human Matrix Metalloproteinase-2 (MMP-2): Structural/Functional Relatedness between Gelatin-Binding Fibronectin Type II Modules and Lysine-Binding Kringle Domains
- Random Peptide Bacteriophage Display as a Probe for Urokinase Receptor Ligands
- Plasmin Produces an E-Cadherin Fragment That Stimulates Cancer Cell Invasion
- The Role of Proteases in Fibronectin Matrix Remodeling in Thyroid Epithelial Cell Monolayer Cultures
- Induction of Fibronectin mRNA by Urokinase- and Tissue-Type Plasminogen Activator in Human Skin Fibroblasts: Differential Role of u-PA and t-PA at the Fibronectin Protein Level
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- UVA Light Stimulates the Production of Cathepsin G and Elastase-Like Enzymes by Dermal Fibroblasts: A Possible Contribution to the Remodeling of Elastotic Areas in Sun-Damaged Skin
- uPA-Silica-Particles (SP-uPA): A Novel Analytical System to Investigate uPA-uPAR Interaction and to Test Synthetic uPAR Antagonists as Potential Cancer Therapeutics
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