Tissue and plasma elastase and anti-protease (α1 protease inhibitor-α2 macroglobulin) levels in malignancies of head and neck

1993 ◽  
Vol 21 (3) ◽  
pp. 307S-307S ◽  
Author(s):  
GÜLDAL KIRKALI ◽  
YASEMIN BASKIN ◽  
GÜL GÜNER ◽  
TARIK ŞSLENGÖR ◽  
KERIM CERYAN
Keyword(s):  
Protease Inhibitor ◽  
Head And Neck ◽  
Α2 Macroglobulin

scholarly journals α2-Macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester

2020 ◽  
Vol 295 (49) ◽  
pp. 16732-16742 ◽  
Author(s):  
Seandean Lykke Harwood ◽  
Nadia Sukusu Nielsen ◽  
Kathrine Tejlgård Jensen ◽  
Peter Kresten Nielsen ◽  
Ida B. Thøgersen ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Primary Amines ◽  
Hydroxyl Groups ◽  
Histidine Residue ◽  
Protease Inhibition ◽  
Complement Components ◽  
Proteolytic Activation ◽  
Thiol Ester ◽  
Thiol Esters ◽  
Α2 Macroglobulin

Proteins in the α-macroglobulin (αM) superfamily use thiol esters to form covalent conjugation products upon their proteolytic activation. αM protease inhibitors use theirs to conjugate proteases and preferentially react with primary amines (e.g. on lysine side chains), whereas those of αM complement components C3 and C4B have an increased hydroxyl reactivity that is conveyed by a conserved histidine residue and allows conjugation to cell surface glycans. Human α2-macroglobulin–like protein 1 (A2ML1) is a monomeric protease inhibitor but has the hydroxyl reactivity–conveying histidine residue. Here, we have investigated the role of hydroxyl reactivity in a protease inhibitor by comparing recombinant WT A2ML1 and the A2ML1 H1084N mutant in which this histidine is removed. Both of A2ML1s' thiol esters were reactive toward the amine substrate glycine, but only WT A2ML1 reacted with the hydroxyl substrate glycerol, demonstrating that His-1084 increases the hydroxyl reactivity of A2ML1's thiol ester. Although both A2ML1s conjugated and inhibited thermolysin, His-1084 was required for the conjugation and inhibition of acetylated thermolysin, which lacks primary amines. Using MS, we identified an ester bond formed between a thermolysin serine residue and the A2ML1 thiol ester. These results demonstrate that a histidine-enhanced hydroxyl reactivity can contribute to protease inhibition by an αM protein. His-1084 did not improve A2ML1's protease inhibition at pH 5, indicating that A2ML1's hydroxyl reactivity is not an adaption to its acidic epidermal environment.

scholarly journals A Novel Protease Inhibitor of the α2-Macroglobulin Family Expressed in the Human Epidermis

2005 ◽  
Vol 281 (9) ◽  
pp. 5780-5789 ◽  
Author(s):  
Marie-Florence Galliano ◽  
Eve Toulza ◽  
Hélène Gallinaro ◽  
Nathalie Jonca ◽  
Akemi Ishida-Yamamoto ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Human Epidermis ◽  
Α2 Macroglobulin

scholarly journals Human papillomavirus infection in head and neck cancer: The role of the secretory leukocyte protease inhibitor

2013 ◽  
Vol 29 (5) ◽  
pp. 1962-1968 ◽  
Author(s):  
MARKUS HOFFMANN ◽  
ELGAR S. QUABIUS ◽  
SILKE TRIBIUS ◽  
LENA HEBEBRAND ◽  
TIBOR GÖRÖGH ◽  
...  
Keyword(s):  
Head And Neck Cancer ◽  
Human Papillomavirus ◽  
Protease Inhibitor ◽  
Head And Neck ◽  
Neck Cancer ◽  
Secretory Leukocyte Protease Inhibitor ◽  
Human Papillomavirus Infection ◽  
Papillomavirus Infection

Natural anti-proteases in rainbow trout, Oncorhynchus mykiss and brook charr, Salvelinus fontinalis and the in vitro neutralization of fish α2-macroglobulin by the metalloprotease from the pathogenic haemoflagellate, Cryptobia salmositica

Parasitology ◽  
1997 ◽  
Vol 114 (4) ◽  
pp. 375-382 ◽  
Author(s):  
X. ZUO ◽  
P. T. K. WOO
Keyword(s):  
Rainbow Trout ◽  
Protease Inhibitor ◽  
Oncorhynchus Mykiss ◽  
Proteolytic Activity ◽  
Blood Cells ◽  
Salvelinus Fontinalis ◽  
Brook Charr ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Α2 Macroglobulin

Natural anti-proteases (α1-protease inhibitor (α1-PI; α1-antitrypsin) and α2-macroglobulin (α2-M)) were found in the blood of rainbow trout, Oncorhynchus mykiss and brook charr, Salvelinus fontinalis. The α2-M inhibited Cryptobia salmositica proteases and was significantly higher in brook charr than in rainbow trout. Under in vitro conditions it took longer for the same number of parasites to neutralize the α2-M in charr than in trout blood. The haemolysis which occurred when C. salmositica was incubated in the blood of rainbow trout was due to neutralization of α2-M. This in vitro study also showed that it was the metalloprotease of C. salmositica that lysed red blood cells and the plasma of the two species of fishes initially prevented haemolysis by inhibiting the proteolytic activity. We suggest that the natural plasma α2-M plays an important role in defence against cryptobiosis in fishes.

scholarly journals Salivary secretory leukocyte protease inhibitor (SLPI) and head and neck cancer: The Cancer Prevention Study II Nutrition Cohort

Oral Oncology ◽  
2016 ◽  
Vol 55 ◽  
pp. 1-5 ◽  
Author(s):  
Christine M. Pierce Campbell ◽  
Anna R. Giuliano ◽  
B. Nelson Torres ◽  
Michael T. O’Keefe ◽  
Donna J. Ingles ◽  
...  
Keyword(s):  
Head And Neck Cancer ◽  
Protease Inhibitor ◽  
Cancer Prevention ◽  
Head And Neck ◽  
Neck Cancer ◽  
Secretory Leukocyte Protease Inhibitor ◽  
Prevention Study

scholarly journals A derivative of the plasma protease inhibitor α2-macroglobulin regulates the response to peripheral nerve injury

2007 ◽  
Vol 103 (2) ◽  
pp. 694-705 ◽  
Author(s):  
Sanja Arandjelovic ◽  
Nikola Dragojlovic ◽  
Xiaoqing Li ◽  
Robert R. Myers ◽  
W. Marie Campana ◽  
...  
Keyword(s):  
Peripheral Nerve ◽  
Protease Inhibitor ◽  
Nerve Injury ◽  
Peripheral Nerve Injury ◽  
Α2 Macroglobulin

scholarly journals Secretory leukocyte protease inhibitor and its role in virus induced head and neck cancers

2019 ◽  
Vol 35 (79) ◽  
pp. 1936-1944
Author(s):  
Vidya Ajila ◽  
Veena Shetty ◽  
Babu Subhas ◽  
Shruthi Hegde
Keyword(s):  
Protease Inhibitor ◽  
Head And Neck ◽  
Secretory Leukocyte Protease Inhibitor ◽  
Head And Neck Cancers

scholarly journals Activity of kallikrein-kinin system in children in norm and at some pathological states

2009 ◽  
Vol 8 (4(2)) ◽  
pp. 61-69
Author(s):  
Ye. I. Kondratiyeva ◽  
T. Ye. Tropova ◽  
G. A. Sukhanova ◽  
A. A. Terentiyeva ◽  
T. S. Krivonogova ◽  
...  
Keyword(s):  
Metabolic Syndrome ◽  
Protease Inhibitor ◽  
Blood Plasma ◽  
Inflammatory Diseases ◽  
Healthy Children ◽  
Urinary System ◽  
Kinin System ◽  
Α2 Macroglobulin ◽  
Kallikrein Kinin System ◽  
Ischemic Encephalopathy

Proteolytic systems of tissue and blood plasma take part in the processes of adaptation and protection of an organism, as well as in development of pathological reactions. We have studied the activity of kallikrein, kallikreinogen, angiotensine transforming enzyme, α1-protease inhibitor, and α2-macroglobulin in healthy children in different age periods, in newborns with hypoxic-ischemic encephalopathy, in children with infectious-inflammatory diseases of the urinary system, obesity, and metabolic syndrome.The activity of the kallikrein-kinin system was increased in all the groups against the background of the decreased inhibitory activity of blood plasma of different intensity, which can be used for the prediction of the course of diseases.

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