Affiliation:
1. INSERM Unité 295-Faculté de Médecine-Pharmacie de Rouen, Avenue de l'Université, 76800 Saint-Etienne-du-Rouvray, France.
2. INSERM Unité 78-543 chemin de la Brèteque, 76230 Bois-Guillaume, France.
Abstract
In hepatoma HepG2 cells, human inter-alpha-trypsin inhibitor (ITI) was synthesized as three heavy chains, H-1 (100 kDa), H-2 (110 kDa) and H-3 (113 kDa), and light hybrid chain (49.5 kDa) composed of alpha 1-microglobulin and HI-30 (ITI derivative, human inhibitor of 30 kDa). The association of at least two heavy chains, H-1 and H-3, with the HI-30 part of the light chain gave rise to a molecule similar to serum ITI. A composite protein (approximately 250 kDa) including heavy and light chains was also secreted, while alpha 1-microglobulin and ITI H-2 protein were released as separate entities. Light chain synthesis could be the limiting factor for ITI maturation.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
34 articles.
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