Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles: a role for Hsp47 and cyclophilin B in the export of …
T Smith, LR Ferreira, C Hebert, K Norris… - Journal of Biological …, 1995 - ASBMB
Hsp47 and cyclophilin B (CyPB) are residents of the endoplasmic reticulum (ER). Both of
these proteins are closely associated with polysome-associated α1 (I) procollagen chains.
Hsp47 possesses chaperone properties early during the translation of procollagen while the
cis/trans-isomerase properties of CyPB facilitate procollagen folding. In this report, we further
investigate the interaction of these proteins with procollagen I during export from the ER. To
inhibit vesicular budding and retain procollagen within the ER, cells were treated with the …
these proteins are closely associated with polysome-associated α1 (I) procollagen chains.
Hsp47 possesses chaperone properties early during the translation of procollagen while the
cis/trans-isomerase properties of CyPB facilitate procollagen folding. In this report, we further
investigate the interaction of these proteins with procollagen I during export from the ER. To
inhibit vesicular budding and retain procollagen within the ER, cells were treated with the …
