Interaction of human mast cell tryptase and chymase with low-molecular-mass serine proteinase inhibitors from the human respiratory tract

1993 ◽  
Vol 249 (8) ◽  
Author(s):  
K. Hochstrasser ◽  
W. Gebhard ◽  
G. Albrecht ◽  
G. Rasp ◽  
E. Kastenbauer
Keyword(s):  
Mast Cell ◽  
Respiratory Tract ◽  
Molecular Mass ◽  
Proteinase Inhibitors ◽  
Serine Proteinase ◽  
Human Mast Cell ◽  
Mast Cell Tryptase ◽  
Human Respiratory Tract ◽  
Serine Proteinase Inhibitors

scholarly journals Human mast cell tryptase isoforms: separation and examination of substrate-specificity differences

1995 ◽  
Vol 307 (2) ◽  
pp. 341-346 ◽  
Author(s):  
S S Little ◽  
D A Johnson
Keyword(s):  
Mast Cell ◽  
Molecular Mass ◽  
Peptide Mapping ◽  
Proteinase Inhibitors ◽  
High Molecular Mass ◽  
Mass Separation ◽  
Human Mast Cell ◽  
Mast Cell Tryptase ◽  
Sds Page ◽  
Mass Form

Tryptases are trypsin-like enzymes found in mast cell granules that appear to exist as tetramers. These enzymes are not controlled by blood plasma proteinase inhibitors and only cleave a few physiological substrates in vitro, including high-molecular-mass kininogen (HMMK) and vasoactive intestinal peptide (VIP). Purified human lung mast cell tryptase (HLT) contained two bands of approx. molecular mass 29 and 33 kDa on SDS/PAGE. These two forms of HLT have been separated by chromatography on a cellulose phosphate column, with the high-molecular-mass form (high-HLT) being eluted with 10 microM heparin and the low-molecular-mass form (low-HLT) subsequently eluted with 1 M NaCl. Removal of asparagine-linked carbohydrate caused both isoforms to run as single sharp bands on SDS/PAGE, differing slightly in molecular mass. Separation of these two isoforms of tryptase shows that tetramers consist of four homologous subunits rather than mixtures of the two isoforms. Using HMMK and VIP as substrates, these two forms of HLT were found to differ with regard to specificity and rate of cleavage. High-HLT initially cleaved HMMK at Arg-431 within the C-terminal anionic binding region of the molecule, whereas low-HLT cleaved HMMK simultaneously at multiple sites within the C-terminal portion of the molecule. On the basis of HPLC peptide mapping, each isoform also cleaved VIP at different sites. Comparison of cleavage rates based on the active-site concentrations of titrated isoforms showed that low-HLT cleaved HMMK more rapidly than did high-HLT. These two isoforms may represent different gene products or they may result from post-translational modification.

Purification of two low-molecular-mass serine proteinase inhibitors from chicken liver

1999 ◽  
Vol 852 (1) ◽  
pp. 207-216 ◽  
Author(s):  
Agnieszka Łopuska ◽  
Jolanta Polanowska ◽  
Tadeusz Wilusz ◽  
Antoni Polanowski
Keyword(s):  
Molecular Mass ◽  
Proteinase Inhibitors ◽  
Serine Proteinase ◽  
Chicken Liver ◽  
Serine Proteinase Inhibitors
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