Proteinase-activated receptors: Structural requirements for activity, receptor cross-reactivity, and receptor selectivity of receptor-activating peptides

Canadian Journal of Physiology and Pharmacology

Volumn 75, Issue 7, 1997, Pages 832-841

  Hollenberg, Morley D ^a   Saifeddine, Mahmoud ^a   Al Ani, Bahjat ^a   Kawabata, Atsufumi ^a,b  

^a UNIVERSITY OF CALGARY   (Canada)

^b KINKI UNIVERSITY   (Japan)

Author keywords

Aorta; Calcium; Kidney cells (HEK293); Proteases; Stomach; Thrombin; Trypsin

Indexed keywords

CELL RECEPTOR; PEPTIDE; PROTEINASE; SERINE PROTEINASE; THROMBIN; THROMBIN RECEPTOR; TRYPSIN;

ANIMAL CELL; AORTA; ARTICLE; CALCIUM CELL LEVEL; CONCENTRATION RESPONSE; DRUG ACTIVITY; KIDNEY CELL; NONHUMAN; PRIORITY JOURNAL; RAT; REGULATORY MECHANISM; STOMACH; STRUCTURE ACTIVITY RELATION;

EID: 0030823980     PISSN: 00084212     EISSN: None     Source Type: Journal    
DOI: 10.1139/y97-110     Document Type: Article

References (3)

1. 2, in rat vascular and gastric smooth muscle. Can. J. Physiol. Pharmacol. 73: 1203-1207.
2. Blackhart, B.D., Teng, W., Naughton, M.A., Nystedt, S., Emilsson, K., Sundelin, J., and Scarborough, R.M. 1995. Cross-reactivity of thrombin receptor and PAR-2 agonist peptides. Is there a simple explanation for alleged thrombin receptor subtypes? Thromb. Haemostasis, 73: 928.
3. Blackhart, B.D., Emilsson, K., Nguyen, D., Teng, W., Martelli, A.J., Nystedt, S., Sundelin, J., and Scarborough, R.M. 1996. Ligand cross-reactivity within the protease-activated receptor family. J. Biol. Chem. 271: 16 466 - 16 471.