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• W2205840347 abstract "ABSTRACT The three major components on a weight basis of rat serosal and human pulmonary mast cell secretory granules are histamine, heparin proteoglycan and neutral proteases. Neutral proteases appear to account for more than 50% of the total secretory granule protein and at least 20% of the total cell protein. Rat mast cells contain chymase, a chymotryptic endopeptidase of 28,000 MW, and carboxypeptidase A, a C-terminal exopeptidase of about 38,000 mw. Human mast cells have neither of these enzymes, but instead contain tryptase, a tryptic endopeptidase of 144,000 mw. Under physiologic conditions, mast cell neutral proteases bind tightly to heparin; secretion of the proteases and heparin as a complex may serve to limit the diffusion of each individual component from their site of release and to modulate subsequent enzyme-substrate interactions. Histamine is free to diffuse away from its connective tissue site of secretion. Due to its ability to augment vasopermeability, histamine should allow diffusion of soluble substances into the area where mast cell proteases were released and immobilized. For example, the cleavage of human C3 to C3a and other peptides by tryptase that occurs in vitro may also occur in vivo and be acilitated by the histamne-dependent diffusion of C3 From serum into connective tissue. The nrolonged presence of active neutral proteases at sites of mast cell activation may influence the growth and repair of connective tissue and the chronicity of immediate hypersensitivity reactions." @default.
• W2205840347 created "2016-06-24" @default.
• W2205840347 creator A5037098194 @default.
• W2205840347 date "1983-01-01" @default.
• W2205840347 modified "2023-09-27" @default.
• W2205840347 title "Mast Cell Neutral Proteases" @default.
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• W2205840347 doi "https://doi.org/10.1016/b978-0-08-029775-0.50088-2" @default.
• W2205840347 hasPublicationYear "1983" @default.
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