High impact information on TXNL5

• However, TRP-14-induced PMN adhesion was transient, and TRP-14 did not cause ICAM-1 expression [1].
• The initial P-selectin expression and PMN adhesion responses were reproduced by the 14-amino peptide (SFLLRNPNDKYEPF) (thrombin-receptor activity peptide; TRP-14) which comprised the NH2 terminus created by thrombin's proteolytic action on its receptors [1].
• Human umbilical vein endothelial cells (HUVECs) challenged with TRP-14 (10(-4) to 10(-5) M) produced concentration-dependent increases in endothelial adhesivity to PMN [2].
• We examined the effects of TRP-14 in inducing endothelial cell hyperadhesivity and neutrophil (PMN) adhesion to endothelial cell monolayers [2].
• Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways [3].

Biological context of TXNL5

• The surface of TRP14 in the vicinity of the active site includes an extended loop and an additional alpha-helix, and the distribution of charged residues in the surface is different from Trx1 [4].
• Deficiency of TRP14 or Trx1 enhanced TNF-alpha-induced activation of caspases and subsequent apoptosis by a similar extent [3].
• The observed absence of energy transfer between Tyr1 and Trp14 of dynorphin indicates that the two fluorophores are at least 20 A apart and rules out a close proximity between the N- and C-terminal segments of the peptide [5].
• TRP-14 (> 1 microM) increased the concentration of intracellular calcium ([Ca2+]i) in endothelial cells with kinetics similar to the increase in [Ca2+]i triggered by alpha-thrombin [6].

Anatomical context of TXNL5

• The complex was detected in HeLa cells treated with H(2)O(2) or TNF-alpha but not in untreated cells, suggesting that LC8 cytoplasmic dynein light chain is a possible substrate of TRP14 [3].
• TRP-14-induced release of P-selectin from intracellular stores may be a critical determinant of the response since treatment of endothelial cells with anti-P-selectin monoclonal antibody (mAb) G1 prevented the increase in PMN adhesion [2].
• The 125I-labeled TRP-14 also interacted with bovine pulmonary microvessel endothelial cells, human umbilical vein endothelial cells, and porcine pulmonary artery smooth muscle cells [6].
• The model of the Maxi-K channel reveals a narrower and more structurally restrained outer vestibule in which the aromatic residues Phe266 and Tyr294 may stabilize binding of IbTX and ChTX by pi-pi stacking with the aromatic residues Trp14 and Tyr36 of the peptides [7].

Associations of TXNL5 with chemical compounds

• In an effort to identify target proteins of TRP14, a mutant of TRP14, in which the active site cysteine (Cys(46)) was substituted with serine, was shown to form a disulfide-linked complex with LC8 cytoplasmic dynein light chain [3].
• Based on tryptophan fluorescence spectra and computer modeling from x-ray structures of native globins, steric constraint between Trp14 and Tyr125 would be induced in the chimeric alphaalphabeta-subunit, which would perturb the packing of the A- and H-helices and destabilize the globule structure [8].
• It is shown that a different distance from Trp14 to haem iron in the three proteins might be the structural basis for the different yield of the peroxyl radical and the different efficiency of incorporation of molecular oxygen into styrene [9].

Other interactions of TXNL5

• TRP-14 was also a pulmonary vasodilator with a t1/2R value of 0.8 +/- 0.09 min at a concentration of 10(-7) M; both TRP-14 and TRP-7 were approximately 3-log less potent than equimolar alpha-thrombin.(ABSTRACT TRUNCATED AT 250 WORDS)[10]

References