Linkage between blood coagulation and inflammation: Stimulation of neutrophil tissue kallikrein by thrombin

Cohen, William; Wu, Haifeng; Featherstone, Gerald L.; Jenzano, Joyce W.; Lundblad, Roger L.

doi:10.1016/0006-291x(91)90926-x

Cited by 36 publications

(22 citation statements)

References 23 publications

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“…3b). This molecular structure is consistent with other investigations [7,24], Analysis of 35S-methioninelabeled proteins secreted by M4 cells ( fig. 2.…”

Section: Discussionsupporting

confidence: 80%

“…The gel was then elcctroblottcd onto Immobilon-P (BioRad) for 48 min at 400 mA and followed by fixation with 0.5% of glutaraldehyde in phosphate-buffered saline (pH 7.3) [I8J. After washing and subsequent blocking with 3% gelatin, rabbit polyclonal anti-human TK antibody [7] and goat anti-rabbit IgG antibody con jugated with alkaline phosphatase (BioRad) were utilized to analyze the blot. An equal volume of conditioned medium was included as a control in the Western blot analysis.…”

Section: Western Blot Analysismentioning

confidence: 99%

“…Human pancreas [3], kidney [4], salivary glands [5], prostate gland [6] and poly morphonuclear leukocytes [7] have been shown to synthe size and secrete TKs. Although TK has been studied in a number of laboratories, a precise understanding of its physiological importance is yet to be determined.…”

Section: Introductionmentioning

confidence: 99%

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Expression of Tissue Kallikrein in Normal and SV40-Transfected Human Endometrial Stromal Cells

Xu²,

Jenzano

et al. 1993

Pathobiology

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The polymerase chain reaction with specific tissue kallikrein primers was utilized to demonstrate the presence of tissue kallikrein mRNA in human endometrial stromal cells. Enzymatic analysis measured with a specific tripeptide nitroanilide substrate demonstrated the presence of tissue kallikrein in the conditioned medium obtained from both normal stromal cells and stromal cells transfected with an origin-defective temperature-sensitive SV40 large T antigen. The transfected stromal cell supernatant exhibited approximately twice as much tissue kallikrein activity as normal stromal cells at 60-100% of cell confluence. The release of tisseu kallikrein from transfected stromal cells was confirmed by Western blot analysis and [³⁵S]-methionine incorporation into a 35-kD protein which retains tissue kallikrein activity. These results demonstrate for the first time the expression and secretion of tissue kallikrein in human endometrial stromal cells and provide evidence of possible involvement of tissue kallikrein in cell transformation.

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“…3b). This molecular structure is consistent with other investigations [7,24], Analysis of 35S-methioninelabeled proteins secreted by M4 cells ( fig. 2.…”

Section: Discussionsupporting

confidence: 80%

Section: Western Blot Analysismentioning

confidence: 99%

See 1 more Smart Citation

Expression of Tissue Kallikrein in Normal and SV40-Transfected Human Endometrial Stromal Cells

Xu²,

Jenzano

et al. 1993

Pathobiology

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“…It contains the highly conserved residues of the serine protease catalytic triad but lacks the trypsin specific lysine-aspartic acid pair in the carboxyl-terminal region (3). The short activation peptide (3) and significant levels of amino acid identity brings G13 closer to the mammalian serine protease families known to be involved in immune response such as kallikreins (28,29), mast cell proteases (33), and plasminogens (34), rather than to the previously reported An. gambiae gutspecific trypsins and chymotrypsins (3).…”

Section: Fig 2 Mrna Expression Analysis Of Differentially Amplifiedmentioning

confidence: 99%

“…U56423), An. gambiae trypsin 7 (line b) (3), mouse mast cell protease 7 (line c) (28), and mouse tissue kallikrein (line d) (29). The residues (H, D, S) of the catalytic triad of serine proteases are underlined.…”

Section: Fig 2 Mrna Expression Analysis Of Differentially Amplifiedmentioning

confidence: 99%

Identification and characterization of differentially expressed cDNAs of the vector mosquito, Anopheles gambiae

Dimopoulos

Richman²,

Torre

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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The isolation and study of Anopheles gambiae genes that are differentially expressed in development, notably in tissues associated with the maturation and transmission of the malaria parasite, is important for the elucidation of basic molecular mechanisms underlying vector-parasite interactions. We have used the differential display technique to screen for mRNAs specifically expressed in adult males, females, and midgut tissues of blood-fed and unfed females. We also screened for mRNAs specifically induced upon bacterial infection of larval stage mosquitoes. We have characterized 19 distinct cDNAs, most of which show developmentally regulated expression specificity during the mosquito life cycle. The most interesting are six new sequences that are midgut-specific in the adult, three of which are also modulated by blood-feeding. The gut-specific sequences encode a maltase, a V-ATPase subunit, a GTP binding protein, two different lectins, and a nontrypsin serine protease. The latter sequence is also induced in larvae subjected to bacterial challenge. With the exception of a mitochondrial DNA fragment, the other 18 sequences constitute expressed genomic sequence tags, 4 of which have been mapped cytogenetically.

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Relative role of chloramines, hypochlorous acid, and proteases in the activation of human polymorphonuclear leukocyte collagenase

Claesson

Karlsson

Zhang

et al. 1996

Journal of Leukocyte Biology

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The activation of collagenase released by polymorphonuclear leukocytes (PMNs) has been extensively studied in vitro, but the activation of the enzyme in vivo is not fully understood. For further evaluation of the relative role of oxidative and proteolytic mechanisms in the activation of collagenase, PMNs were stimulated by serum-opsonized zymosan under both aerobic and anaerobic conditions. The results showed that similar amounts of collagenase were released by the PMNs under aerobic and anaerobic conditions, but the activity of the released collagenase was twice as high under aerobic conditions as under anaerobic conditions. Under aerobic conditions the enzyme was rapidly activated by hypochlorous acid and chloramines, which are products of the myeloperoxidase-H2O2-chloride system of the PMNs. There was also a slow proteolytic activation of the enzyme, which could be ascribed to cathepsin G and possibly to some other serine proteases of PMNs. When extrapolating these findings to in vivo conditions, it seems probable that the oxidative activation of collagenase will proceed mainly by chloramines, which are more long-lived in the tissue than hypochlorous acid. In poorly oxygenated tissues, collagenase may be mainly activated by proteolytic mechanisms.

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Linkage between blood coagulation and inflammation: Stimulation of neutrophil tissue kallikrein by thrombin

Cited by 36 publications

References 23 publications

Expression of Tissue Kallikrein in Normal and SV40-Transfected Human Endometrial Stromal Cells

Expression of Tissue Kallikrein in Normal and SV40-Transfected Human Endometrial Stromal Cells

Identification and characterization of differentially expressed cDNAs of the vector mosquito, Anopheles gambiae

Relative role of chloramines, hypochlorous acid, and proteases in the activation of human polymorphonuclear leukocyte collagenase

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