Tachykinins

Holzer, Peter

doi:10.1016/b978-0-12-385095-9.00181-0

Cited by 1 publication

(2 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The processing of Substance P, VIP and the unmasking of the TL-sequence of the PAR2-based peptide were not different between control, acute or post-colitis animals. It has been shown that substance P is involved in gastrointestinal inflammation and mucosal injury, but we did not observe significant differences in the processing of this peptide between colonic samples from control, acute colitis and post-colitis animals [ 28 ].…”

Section: Discussionmentioning

confidence: 57%

“…Therefore, we first aimed to obtain cleavage patterns of naturally occurring substrates with a set of purified trypsin-like and elastase-like proteases present in the human colon (trypsin-1, -2, -3, tryptase, thrombin, cathepsin G, neutrophil elastase and pancreatic elastase). We focused on -endorphin, vasoactive intestinal peptide (VIP), neurotensin, enkephalins, substance P and bradykinin because these peptides are linked to pain sensitization or inflammation and, as such, are relevant in the pathophysiology of colitis [ 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 ]. Since a role for protease-activated receptors (PARs) in colitis and post-colitis has been described, the ability of the proteases to ‘unmask’ or ‘disarm’ PARs was assessed as well [ 31 , 32 , 33 , 34 ].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Proteolytic Cleavage of Bioactive Peptides and Protease-Activated Receptors in Acute and Post-Colitis

bruyn

Ceuleers

Hanning

et al. 2021

IJMS

View full text Add to dashboard Cite

The protease activity in inflammatory bowel disease (IBD) and irritable bowel syndrome has been studied extensively using synthetic fluorogenic substrates targeting specific sets of proteases. We explored activities in colonic tissue from a 2,4,6-trinitrobenzenesulfonic acid (TNBS)-induced colitis rat model by investigating the cleavage of bioactive peptides. Pure trypsin- and elastase-like proteases on the one hand and colonic tissue from rats with TNBS-induced colitis in the acute or post-inflammatory phase on the other, were incubated with relevant peptides to identify their cleavage pattern by mass spectrometry. An increased cleavage of several peptides was observed in the colon from acute colitis rats. The tethered ligand (TL) sequences of peptides mimicking the N-terminus of protease-activated receptors (PAR) 1 and 4 were significantly unmasked by acute colitis samples and these cleavages were positively correlated with thrombin activity. Increased cleavage of β-endorphin and disarming of the TL-sequence of the PAR3-based peptide were observed in acute colitis and linked to chymotrypsin-like activity. Increased processing of the enkephalins points to the involvement of proteases with specificities different from trypsin- or chymotrypsin-like enzymes. In conclusion, our results suggest thrombin, chymotrypsin-like proteases and a set of proteases with different specificities as potential therapeutic targets in IBD.

show abstract

Section: Discussionmentioning

confidence: 57%