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Literature DB >> 636956

Naturally occurring low molecular weight inhibitors of neutral proteinases from PMN-granulocytes and of kallikreins.

H Fritz, H Schiessler, R Gieger, K Ohlsson, K Hochstrasser.

Abstract

Human mucous secretions contain low molecular weight (Mr approximately 11,000) acid-stable inhibitors directed against elastase and cathepsin G from PMN-granulocytes. Important biochemical properties of these inhibitors are presented and their possible biological function is discussed. An inhibitor of glandular and plasma kallikreins preventing kinin-liberation from kininogen but not ester hydrolysis was obtained from rat kidney tubules. A molecular weight of about 4700 was estimated for this kallikrein-specific inhibitor (trypsin-induced kinin-liberation is not prevented).

Entities: Chemical Gene Species

Mesh：

Substances：

Year: 1978 PMID： 636956 DOI： 10.1007/bf01972403

Source DB: PubMed Journal: Agents Actions ISSN： 0065-4299

16 in total

1. A kallikrein-specific inhibitor in rat kidney tubules.

Authors: R Geiger; K Mann
Journal: Hoppe Seylers Z Physiol Chem Date: 1976-04

2. The structure of elastatinal, an elastase inhibitor of microbial origin.

Authors: A Okura; H Morishima; T Takita; T Aoyagi; T Takeuchi; H Umezawa
Journal: J Antibiot (Tokyo) Date: 1975-04 Impact factor: 2.649

3. Effect of elastase-like and chymotrypsin-like neutral proteases from human granulocytes on isolated clotting factors.

Authors: W Schmidt; R Egbring; K Havemann
Journal: Thromb Res Date: 1975-04 Impact factor: 3.944

4. The cleavage of a methionyl-lysyl-bradykinin-like peptide from kininogen by a protease of human neutrophil leukocyte lysosomes.

Authors: H Z Movat; F M Habal; D R Macmorine
Journal: Adv Exp Med Biol Date: 1976 Impact factor: 2.622

5. Isolation and partial characterization of a low molecular weight acid stable protease inhibitor from human bronchial secretion.

Authors: K Ohlsson; H Tegner; U Akesson
Journal: Hoppe Seylers Z Physiol Chem Date: 1977-05

6. Attemps to isolate a kallikrein inhibitor from rat salivary gland.

Authors: G Siqueira; W T Beraldo
Journal: Agents Actions Date: 1973-12

7. Elastases from human and canine granulocytes, II. Interaction with protease inhibitors of animal, plant, and microbial origin.

Authors: H Schiessler; K Ohlsson; I Olsson; M Arnhold; Y Birk; H Fritz
Journal: Hoppe Seylers Z Physiol Chem Date: 1977-01

Naturally occurring low molecular weight inhibitors of neutral proteinases from PMN-granulocytes and of kallikreins.

1. A kallikrein-specific inhibitor in rat kidney tubules.

2. The structure of elastatinal, an elastase inhibitor of microbial origin.

3. Effect of elastase-like and chymotrypsin-like neutral proteases from human granulocytes on isolated clotting factors.

4. The cleavage of a methionyl-lysyl-bradykinin-like peptide from kininogen by a protease of human neutrophil leukocyte lysosomes.

5. Isolation and partial characterization of a low molecular weight acid stable protease inhibitor from human bronchial secretion.

6. Attemps to isolate a kallikrein inhibitor from rat salivary gland.

7. Elastases from human and canine granulocytes, II. Interaction with protease inhibitors of animal, plant, and microbial origin.

8. Cationic proteins of human granulocytes. V. Interaction with plasma protease inhibitors.

9. Inhibitors of acrosin and granulocyte proteinases from human genital tract secretions.

10. alpha1-Antichymotrypsin interaction with cationic proteins from granulocytes.

Review 1. Lysosomal enzymes of phagocytes and the mechanism of their release.

2. Periodontal pathogens affect the level of protease inhibitors in gingival crevicular fluid.

3. Subcellular localization and further characterization of a new elastase inhibitor from pneumococci.