The Importance of Serine Proteinases as Aeroallergens Associated with Asthma

1999 ◽  
Vol 119 (4) ◽  
pp. 259-264 ◽  
Author(s):  
Horng-Der Shen ◽  
Ming F. Tam ◽  
Hong Chou ◽  
Shou-Hwa Han
Keyword(s):  
Serine Proteinases

Serine proteinases in human cutaneous mastocytosis

1986 ◽  
Vol 278 (5) ◽  
pp. 363-366 ◽  
Author(s):  
J. E. Fr�ki ◽  
N. M. Schechter ◽  
G. S. Lazarus
Keyword(s):  
Serine Proteinases ◽  
Cutaneous Mastocytosis

Distribution of the granulocyte serine proteinases proteinase 3 and elastase in human glomerulonephritis

1995 ◽  
Vol 25 (2) ◽  
pp. 253-261 ◽  
Author(s):  
Christian Mrowka ◽  
Elena Csernok ◽  
Wolfgang L. Gross ◽  
Helmut E. Feucht ◽  
Ulrike Bechtel ◽  
...  
Keyword(s):  
Proteinase 3 ◽  
Serine Proteinases

scholarly journals Mouse macrophage elastase. Purification and characterization as a metalloproteinase

1981 ◽  
Vol 193 (2) ◽  
pp. 589-605 ◽  
Author(s):  
M J Banda ◽  
Z Werb
Keyword(s):  
Culture Medium ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Serine Proteinase ◽  
Peritoneal Macrophages ◽  
Serine Proteinases ◽  
Endogenous Inhibitor ◽  
Purification And Characterization ◽  
Predominant Form ◽  
Mouse Peritoneal Macrophages

Macrophage elastase was purified from tissue-culture medium conditioned by inflammatory mouse peritoneal macrophages. Characterized as a secreted neutral metalloproteinase, this enzyme was shown to be catalytically and immunochemically distinct from the mouse pancreatic and mouse granulocyte elastases, both of which are serine proteinases. Inhibition profiles, production of nascent N-terminal leucine residues and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of degraded elastin indicated that macrophage elastase is an endopeptidase, with properties of a metalloproteinase, rather than a serine proteinase. Macrophage elastase was inhibited by alpha 2-macroglobulin, but not by alpha 1-proteinase inhibitor. Macrophage elastase was resolved into three chromatographically distinct forms. The predominant form had mol.wt. 22 000 and was purified 4100-fold. Purification of biosynthetically radiolabelled elastase indicated that this form represented less than 0.5% of the secreted protein of macrophages. Approx. 800% of the starting activity was recovered after purification. Evidence was obtained for an excess of an endogenous inhibitor masking more than 80% of the secreted activity.

Serine Proteinases from Cold-Adapted Organisms

1997 ◽  
pp. 27-46 ◽  
Author(s):  
Magnús M. Kristjánsson ◽  
Bjarni Ásgeirsson ◽  
Jón B. Bjarnason
Keyword(s):  
Serine Proteinases ◽  
Cold Adapted

scholarly journals The Mouse Testis Is the Source of Various Serine Proteases and Serine Proteinase Inhibitors (SERPINs): Serine Proteases and SERPINs Identified in Leydig Cells Are under Gonadotropin Regulation

Endocrinology ◽  
2006 ◽  
Vol 147 (9) ◽  
pp. 4374-4383 ◽  
Author(s):  
Fanny Odet ◽  
Adélie Verot ◽  
Brigitte Le Magueresse-Battistoni
Keyword(s):  
Extracellular Matrix ◽  
Plasminogen Activator ◽  
Serine Proteases ◽  
Leydig Cells ◽  
Proteinase Inhibitors ◽  
Primary Cultures ◽  
Serine Proteinases ◽  
Rt Pcr ◽  
Positive Effects ◽  
Extracellular Matrix Components

The occurrence of various serine proteinases and serine proteinases inhibitors (SERPINs) was investigated by RT-PCR in whole testes of 1-, 3-, and 8-wk-old mice in crude and enriched germ cell fractions, mouse Leydig tumor cells (mLTC-1), and primary cultures of 3- and 8-wk-old enriched fractions of Leydig cells and 3-wk-old Sertoli cells. New members were identified in the testis protease repertoire. Within the Leydig repertoire, a PCR product was found for plasminogen activators urokinase plasminogen activator (uPA) and tissue plasminogen activator (8-wk-old cells), matriptase-2 (mLTC-1), kallikrein-21, SERPINA5, SERPINB2 (primary cultures), and serine peptidase inhibitor Kunitz type 2 (SPINT2). The gonadotropin regulation was explored by semiquantitative RT-PCR, using steroidogenic acute regulatory protein (StAR) as a positive control. Matriptase-2, kallikrein-21, SPINT2, and SERPINA5 were down-regulated, whereas uPA and its receptor were up-regulated by human chorionic gonadotropin (hCG) via cAMP in the mLTC-1 cells. Positive effects were observed transiently after 1–8 h of hCG exposure, and negative effects, first evidenced after 6 h, lasted 48 h. The hCG-induced effects were confirmed in primary cultures. In addition, SERPINB2 was augmented by hCG in primary cultures. Addition of either trypsin or protease inhibitors did not alter the hCG-induced surge of StAR. Because hCG regulated proteases and SERPINs (whereas testosterone did not), it could alter the proteolytic balance of Leydig cells and consequently the metabolism of extracellular matrix components. Therefore, even though a direct interplay between the early hCG-induced surge of uPA and StAR is unlikely, our data together with the literature suggest that extracellular matrix proteins alter Leydig cell steroidogenesis.

Sign in / Sign up

Export Citation Format

Share Document