Identification of a tissue kallikrein in human polymorphonuclear leucocytes

Figueroa, Carlos D.; MacIver, A. G.; Bhoola, K. D.

doi:10.1111/j.1365-2141.1989.tb07711.x

Cited by 81 publications

(39 citation statements)

References 31 publications

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“…In addition, plasma-derived serine proteases such as kallikrein, plasmin, and thrombin can bind to neutrophils, and their proteolytic activity can be detected on the cell surface (42)(43)(44). Thus, there are several serine esterases that potentially could cleave the plasma membrane DBP binding site.…”

Section: Resultsmentioning

confidence: 99%

Elastase Controls the Binding of the Vitamin D-Binding Protein (Gc-Globulin) to Neutrophils: A Potential Role in the Regulation of C5a Co-Chemotactic Activity

DiMartino

Shah

Trujillo

et al. 2001

The Journal of Immunology

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The vitamin D-binding protein (DBP) binds to the plasma membranes of numerous cell types and mediates a diverse array of cellular functions. DBP bound to the surface of leukocytes serves as a co-chemotactic factor for C5a, significantly enhancing the chemotactic activity of pM concentrations of C5a. This study investigated the regulation of DBP binding to neutrophils as a possible key step in the process of chemotaxis enhancement to C5a. Using radioiodinated DBP as a probe, neutrophils released 70% of previously bound DBP into the extracellular media during a 60-min incubation at 37°C. This was suppressed by serine protease inhibitors (PMSF, Pefabloc SC), but not by metallo- or thiol-protease inhibitors. DBP shed from neutrophils had no detectable alteration in its m.w., suggesting that a serine protease probably cleaves the DBP binding site, releasing DBP in an unaltered form. Cells treated with PMSF accumulate DBP vs time with over 90% of the protein localized to the plasma membrane. Purified neutrophil plasma membranes were used to screen a panel of protease inhibitors for their ability to suppress shedding of the DBP binding site. Only inhibitors to neutrophil elastase prevented the loss of membrane DBP-binding capacity. Moreover, treatment of intact neutrophils with elastase inhibitors prevented the generation of C5a co-chemotactic activity from DBP. These results indicate that steady state binding of DBP is essential for co-chemotactic activity, and further suggest that neutrophil elastase may play a critical role in the C5a co-chemotactic mechanism.

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Section: Resultsmentioning

confidence: 99%

Elastase Controls the Binding of the Vitamin D-Binding Protein (Gc-Globulin) to Neutrophils: A Potential Role in the Regulation of C5a Co-Chemotactic Activity

DiMartino

Shah

Trujillo

et al. 2001

The Journal of Immunology

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“…Tissue kallikrein has been localized to neutrophils 13 and has been postulated to be involved in neutrophil extravasation through the vascular endothelium and into tissues. Kinin activation of endothelial B 2 receptors has been shown to cause increased intracellular calcium and subsequent endothelial retraction, 14 a critical step in diapedesis.…”

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confidence: 99%

A Synthetic Tissue Kallikrein Inhibitor Suppresses Cancer Cell Invasiveness

Wolf

Evans

Chao

et al. 2001

The American Journal of Pathology

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Serine proteinases modulate the interaction of tumor cells with extracellular matrix components during extravasation and metastasis. The serine proteinase tissue kallikrein has been previously demonstrated in several human adenocarcinomas, and we presently report the localization of immunoreactive kallikrein and its mRNA in pancreatic adenocarcinoma. In addition, a synthetic peptide-based inhibitor specific for tissue kallikrein (FE999024) was used in our studies to explore a possible role for kallikrein in cancer cell invasiveness. Matrigel invasion assays were performed with a human breast-cancer cell line, MDA-MB-231, which expresses tissue kallikrein in culture. In the presence of FE999024 invasion through Matrigel was inhibited in a dose-dependent manner to a maximum of 39%. We also developed a novel ex vivo assay in which breast cancer cells are infused into the pulmonary circulation of artificially ventilated explanted rat lungs. At intervals up to 6 hours after infusion pulmonary invasion was quantified by bronchial alveolar lavage to recover human cancer cells from the airspace. Invading cells in the lung interstitium were also quantified after immunohistochemistry with a monoclonal antibody specific for human cytokeratin 18. The synthetic kallikrein inhibitor attenuates breast cancer cell invasion into the airspace by 33% when quantified by lavage recovery and up to 34% as quantified in the lung interstitium by cytokeratin 18 immunostaining. Cancer cells exploit serine proteinases to influence the local blood supply, extravasate into and out of vessels, and to migrate through tissue matrix during metastasis. The serine proteinase tissue kallikrein has been localized in human adenocarcinomas and related cell lines from a number of organs including prostate, breast, pituitary, colon, ovary, endometrium, kidney, and esophagus.

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“…Cell-binding experiments with different components of the kallikrein-kinin system have been performed in situ by immunolocalization [5, or in vitro by binding assays with radiolabeled ligands [6,11]. This study introduces an e~mati~ assay based upon the selective tissue kallikrein substrate H-Pro-Phe-Arg-AMC [lo] to monitor the amidolytic activity of unbound kallikrein using sensitive fluorescence measurements.…”

Section: Resultsmentioning

confidence: 99%

The binding of tissue prokallikrein to isolated human neutrophils

Anders

Kemme

1994

FEBS Letters

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We have investigated the binding of human tissue kallikrein and the corresponding proenzyme to isolated human lymphocytes and neutrophils, respectively, by the means of steady-state binding assays. It was demonstrated that only prokallikrein bound to washed neutrophils in a timedependent, specific and saturable manner, whereas in vitro binding of activated kallikrein to neutrophils or lymphocytes could be excluded. Our data provide strong evidence for the specific interaction of prokallikrein with intact human neutrophils and indicate a neutrophil surface binding site for the tissue kallikrein precursor which could be involved in kallikrein endocytosis and selective prokallikrein-to-kallikrein conversion.

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Identification of a tissue kallikrein in human polymorphonuclear leucocytes

Cited by 81 publications

References 31 publications

Elastase Controls the Binding of the Vitamin D-Binding Protein (Gc-Globulin) to Neutrophils: A Potential Role in the Regulation of C5a Co-Chemotactic Activity

Elastase Controls the Binding of the Vitamin D-Binding Protein (Gc-Globulin) to Neutrophils: A Potential Role in the Regulation of C5a Co-Chemotactic Activity

A Synthetic Tissue Kallikrein Inhibitor Suppresses Cancer Cell Invasiveness

The binding of tissue prokallikrein to isolated human neutrophils

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