Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen
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Luciano Puzer
Abstract
Cathepsin V is a lysosomal cysteine peptidase highly expressed in corneal epithelium; however, its function in the eye is still unknown. Here, we describe the capability of cathepsin V to hydrolyze plasminogen, which is also expressed in human cornea at levels high enough to produce physiologically relevant amounts of angiostatin-related molecules. The co-localization of these two proteins suggests an important role for the enzyme in the maintenance of corneal avascularity, essential for optimal visual performance. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of plasminogen digestion by cathepsin V revealed the generation of three major products of 60, 50 and 40 kDa, which were electrotransferred to polyvinylidene difluoride membranes and excised for characterization. NH2-terminal amino acid sequencing of these fragments revealed the sequences EKKVYL, TEQLAP and LLPNVE, respectively. These data are compatible with cleavage sites at plasminogen F94–E95, S358–T359 and V468–L469 peptide bonds generating fragments of the five-kringle domains. In contrast, we did not detect any plasminogen degradation by cathepsins B, K and L. Using a Matrigel assay, we confirmed the angiogenesis inhibition activity on endothelial cells caused by plasminogen processing by cathepsin V. Our results suggest a novel physiological role for cathepsin V related to the control of neovascularization in cornea.
©2008 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function
- Transcriptional responses of Plasmodium falciparum to α-difluoromethylornithine-induced polyamine depletion
- Secondary structures and functional requirements for thiM riboswitches from Desulfovibrio vulgaris, Erwinia carotovora and Rhodobacter spheroides
- Secreted human apolipoprotein(a) kringle IV-10 and kringle V inhibit angiogenesis and xenografted tumor growth
- Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue
- Evaluation of the ‘side door’ in carboxylesterase-mediated catalysis and inhibition
- Functional tyrosine residue in the active center of human dipeptidyl peptidase III
- Development of a human adipocyte model derived from human mesenchymal stem cells (hMSC) as a tool for toxicological studies on the action of TCDD
- HNF4α orchestrates a set of 14 genes to down-regulate cell proliferation in kidney cells
- Effects of gastric inhibitory polypeptide (GIP) and related analogues on glucagon release at normo- and hyperglycaemia in Wistar rats and isolated islets
- Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen
