Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, VIII. Characterization of the Bovine Inhibitor as Double-Headed Tiypsin-Elastase Inhibitor

Hochstrasser, K; Albrecht, Gerd J.; Schönberger, Öyvind L.; Wächter, Elmar

doi:10.1515/bchm2.1983.364.2.1689

Cited by 15 publications

(10 citation statements)

References 9 publications

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“…reactive sites in the Kunitz-type domains in the inhibitory sites of UTI are Gly-Pro-Cys-Met--Gly-Met-Thr for elastase inhibition and Gly--Pro-Cys-Arg-Ala-Phe-Ile for trypsin and plasmin inhibition, respectively [1]. The inhibitory property of HI-14,-the active 14 kDa fragment released from human ITI, was examined by Albrecht et al [7].…”

Section: Discussionmentioning

confidence: 99%

“…Hochstrasser et al [1] were the first authors to describe a physiological UTI (HI-30) with an apparent molecular mass of 34 kDa as estimated by gel chromatography.…”

Section: Introductionmentioning

confidence: 99%

“…The amino acid sequences surrounding the reactive sites of the Kunitz-type domains in the inhibitory sites of UTI have been reported [1,7]. Human ITI and its fragments, HI-30 and HI-14, which are released by limited proteolysis with trypsin from ITI, have the same inhibitory effect on several proteinases [7].…”

Section: Introductionmentioning

confidence: 99%

“…More indications regarding the relationship between ITI, UTI, and other polypeptides derived from them have been given elsewhere [3]. The structure of these molecules, their polypeptidic chains, their proteoglycan moiety, the location of proteinase inhibitory sites, as well as the molecular weights are described elsewhere [1][2][3][4]7].…”

Section: Introductionmentioning

confidence: 99%

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Urinary trypsin inhibitor (UTI) and fragments derived from UTI by limited proteolysis efficiently inhibit tumor cell invasion

et al. 1994

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We investigated the effects of purified human urinary trypsin inhibitor (UTI) and fragments derived from UTI by proteolysis on the invasive potential of ovarian cancer cells (HOC-I) and gestational choriocarcinoma cells (SMT-ccl) using an in vitro reconstituted basement membrane invasion assay. These cells express cell-associated plasmin and functional uPA receptors that are partially occupied by ligands. SMT-ccl cells, which express threefold higher levels of cell-associated plasmin activity than HOC-I cells, showed approximately twofold increase in their invasive potential. For the invasion assay, HOC-I cells were primed with exogenous plasminogen, but SMT-ccl cells were not. Human leukocyte elastase (HLE)-digested UTI (22 kDa fragment; UTI-22) inhibited plasmin practically with the same strength as native UTI. Trypsin-digested UTI (20 kDa fragment; UTI-20), however, did not inhibit plasmin significantly. Treatment of cells with UTI or UTI-22 reduced the incidence of tumor cell invasive capacity, whereas the inhibitory effect of UTI-20 was not remarkable. The inhibitory effect on tumor cell invasion was dose-dependent and non-toxic; moreover, it was not mediated by inhibition of the tumor cell chemotactic response or of cell attachment to matrigel. These results indicate that inhibition of the proteolytic enzyme plasmin specifically reduced the invasive capacity of tumor cells in vitro.

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Section: Discussionmentioning

confidence: 99%

“…Hochstrasser et al [1] were the first authors to describe a physiological UTI (HI-30) with an apparent molecular mass of 34 kDa as estimated by gel chromatography.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Urinary trypsin inhibitor (UTI) and fragments derived from UTI by limited proteolysis efficiently inhibit tumor cell invasion

et al. 1994

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“…1 is the precursor of urinary trypsin inhibitor (UTI), which is one of the Kunitz-type protease inhibitors present in human serum and urine (1)(2)(3)(4). ITI was found to act as a stabilizer of pericellular matrix.…”

Section: Inter-␣-trypsin Inhibitor (Iti)mentioning

confidence: 99%

Inter-α-trypsin Inhibitor Bound to Tumor Cells Is Cleaved into the Heavy Chains and the Light Chain on the Cell Surface

Kobayashi

Gotoh

Hirashima

et al. 1996

Journal of Biological Chemistry

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Biological functions of serine proteases in mast cells in allergic inflammation

Katunuma¹,

Kido²

1988

J of Cellular Biochemistry

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Serine proteases in mast cell granules, such as chymase, atypical chymase, and tryptase, which are major proteins in the granules, may play important roles in the process of immunoglobulin E (IgE)-mediated degranulation and in pathobiological alterations in tissues. Indeed, inhibitors of chymase, substrate analogs, and antichymase F(ab')2, but not inhibitors of tryptase, markedly inhibited histamine release induced by IgE-receptor bridging but not that induced by Ca ionophore. In contrast, inhibitors of metalloprotease inhibited histamine release induced not only by IgE-receptor bridging but also by Ca ionophore. These results suggest that chymase and metalloprotease are involved at different steps in the process of degranulation. The extents of inhibition of histamine release were closely correlated with the amounts of the inhibitors of chymase accumulated in the granules. After degranulation, the released proteases may in part contribute to pathobiological alterations in allergic disorders through generations of C3a anaphylatoxin and thrombin by human and rat tryptase, respectively, and those of angiotensin II and a chemotactic factor of neutrophils by human and rat chymase, respectively. Moreover, chymase and atypical chymase from rat were shown to destroy type IV collagen, and human tryptase was found to hydrolyze various plasma proteins, such as fibrinogen and high-molecular-weight kininogen. The biological activities of tryptase and chymase from rat may be regulated by their dissociation from and association with trypstatin, an endogenous inhibitor of these proteases.

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Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, VIII. Characterization of the Bovine Inhibitor as Double-Headed Tiypsin-Elastase Inhibitor

Cited by 15 publications

References 9 publications

Urinary trypsin inhibitor (UTI) and fragments derived from UTI by limited proteolysis efficiently inhibit tumor cell invasion

Urinary trypsin inhibitor (UTI) and fragments derived from UTI by limited proteolysis efficiently inhibit tumor cell invasion

Inter-α-trypsin Inhibitor Bound to Tumor Cells Is Cleaved into the Heavy Chains and the Light Chain on the Cell Surface

Biological functions of serine proteases in mast cells in allergic inflammation

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