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Human Tissue Kallikreins: A New Enzymatic Cascade Pathway?
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G. M. Yousef
Published/Copyright:
June 1, 2005
Abstract
Serine proteases are proteolytic enzymes with an active serine residue in their catalytic site. Kallikreins are a subgroup of the serine protease family which is known to have diverse physiological functions. The human kallikrein gene family has now been fully characterized and includes 15 members tandemly located on chromosome 19q13.4. Here we discuss the common structural features of kallikreins at the DNA, mRNA and protein levels and summarize their tissue expression and hormonal regulation patterns. Kallikreins are expressed in many tissues including the salivary gland, endocrine tissues such as testis, prostate, breast and endometrium, and in the central nervous system. Most genes appear to be under steroid hormone regulation. The occurrence of several splice variants is common among kallikreins, and some of the splice variants seem to be tissuespecific and might be related to certain pathological conditions. Kallikreins are secreted in an inactive zymogen form which is activated by cleavage of an Nterminal peptide. Some kalikreins can undergo autoactivation while others may be activated by other kallikreins or other proteases. Most kallikreins are predicted to have trypsinlike enzymatic activity except three which are probably chymotrypsinlike. New, but mainly circumstantial evidence, suggests that at least some kallikreins may be part of a novel enzymatic cascade pathway which is turnedon in aggressive forms of ovarian and probably other cancers.
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Published Online: 2005-06-01
Published in Print: 2002-08-27
Copyright © 2002 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- The International Proteolysis Society (IPS): A Society for Proteolysis, Proteases and Protease Inhibitors
- Proteases and Their Inhibitors: Traditional Research Subjects in the Munich Area
- Apoptotic Pathways: Involvement of Lysosomal Proteases
- Human Tissue Kallikreins: A New Enzymatic Cascade Pathway?
- Discovery of Chemokine Substrates for Matrix Metalloproteinases by Exosite Scanning: A New Tool for Degradomics
- Novel Secretory Vesicle Serpins, Endopin 1 and Endopin 2: Endogenous Protease Inhibitors with Distinct Target Protease Specificities
- Extracellular Proteases of Staphylococcus spp.
- Secreted Aspartic Proteases as Virulence Factors of Candida Species
- Triple-Helical Peptide Analysis of Collagenolytic Protease Activity
- Phage Display Substrate: A Blind Method for Determining Protease Specificity
- Evolution of Placental Proteases
- Factor VII Activating Protease (FSAP): A Novel Protease in Hemostasis
- Cold-Adapted and Mesophilic Brachyurins
- The Role of Dipeptidyl Peptidase IV (DP IV) Enzymatic Activity in T Cell Activation and Autoimmunity
- Biochemical Features, Molecular Biology and Clinical Relevance of the Human 15-Domain Serine Proteinase Inhibitor LEKTI
- Interaction of Plasminogen Activator Inhibitor Type-1 (PAI-1) with Vitronectin (Vn): Mapping the Binding Sites on PAI-1 and Vn
- Structure-Function Relationship of Bromelain Isoinhibitors from Pineapple Stem
- Structural Basis for the Processive Protein Degradation by Tricorn Protease
- Zinc Ligands in an Astacin Family Metalloprotease Meprin A
- Probing the Active Sites and Mechanisms of Rat Metalloproteases Meprin A and B
- (R)-3-Amidinophenylalanine-Derived Inhibitors of Factor Xa with a Novel Active-Site Binding Mode
- Inhibition of Arginine Gingipains (RgpB and HRgpA) with Benzamidine Inhibitors: Zinc Increases Inhibitory Potency
- Cathepsin B Stability, But Not Activity, Is Affected in Cysteine:Cystine Redox Buffers
- Inhibition of Mammalian Legumain by Michael Acceptors and AzaAsn-Halomethylketones
- Role of the Prosegment of Fasciola hepatica Cathepsin L1 in Folding of the Catalytic Domain
- Roles for Arg- and Lys-Gingipains in the Disruption of Cytokine Responses and Loss of Viability of Human Endothelial Cells by Porphyromonas gingivalis Infection
- Aberrant Expression of Serpin Squamous Cell Carcinoma Antigen 2 in Human Tumor Tissues and Cell Lines: Evidence of Protection from Tumor Necrosis Factor-Mediated Apoptosis
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- Determination of Cathepsin B Expression May Offer Additional Prognostic Information for Ovarian Cancer Patients
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- Trypsin Mutants for Structure-Based Drug Design: Expression, Refolding and Crystallisation
