Protein disulphide isomerase

Page, A.P. (1997) Cyclophilin and protein disulphide isomerase genes are co-transcribed in a functionally related manner in Caenorhabditis elegans. DNA and CellBiology 16, 1335-1343. 

Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllyla, R., Huhtal, M.-L., Koivu, J.K. and Kivirikko, K.I. (1987) Molecular cloning of the 3-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBOJournals, 643-649. 

Veijola, J., Annunen, P., Koivunen, P., Page, A.P., Philajaniemi, T. and Kivirikko, K.I. (1996) Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterisation of prolyl 4-hydroxylases containing one of these polypeptides as their B subunit. BiochemicalJournal 317, 721—729. 

D. V., Characterization of protein disulphide isomerase released from activated platelets, Br. J. Haematology 90 (1995), p. 425-431... 

In vivo, formation of the disulphide bridges in cyclotides might be facilitated by a protein disulphide isomerase (PDI) recently isolated from O. affinis,129 whereas backbone cyclisation is mediated by an asparaginyl endopepti-dase.130,131 Support for the latter proposal comes from the fact that a C-terminal Asn residue is essential for cyclisation of the peptide backbone. Violacin... 

The p(25-35) interacts with the native protein, destroys its native conformation, and forms pathological aggregates. Its action is exactly opposite to that of a chaperone, which helps proteins fold correctly. Hence, p(25-35) is termed as an antichaperone, protein disulphide isomerase (PDI), a folding catalyst and chaperone, under certain conditions, can facilitate the... 

Sidekari, V. Gilbert, H.F. Mechanism of the antichaperone activity of protein disulphide isomerase facilitated assembly of large, insoluble aggregates of denatured lysozyme and PDF Biochemistry 2000, 39, 1180-1188. 

Another modification to the ricin precursor which occurs during or immediately after synthesis is disulphide bond formation [124]. In mature ricin, the B chain contains four intrachain disulphide bonds and it is joined to the A chain by a single interchain bond. These disulphide bonds are formed enzymically by ER protein disulphide isomerase [134, 135] which introduces five intrachain disulphide bonds into nascent proricin, the bond destined to become the interchain disulphide bond joining the A and B chains of mature ricin being formed between cysteine residues present in the A- and B-chain sequences in the proricin. 

Ferrari DM, Soling HD (1999) The protein disulphide-isomerase family unravelling a string of folds. Biochem J 339 1-10... 

Prolyl 4-hydroxylase (EC 1.14.11.2) is a key enzyme required for the posttranslational hydroxylation of proline residues in collagen. The enzyme consists of a tetramer composed of two pairs of nonidentical subimits (a.2 of 60 kDa each (Berg et al. 1979). Peptide mapping has demonstrated that the a and P subimits are products of different genes (Berg et al. 1979). The P subunit has been shown (Pihlaja-NiEMi et al. 1987) to be virtually identical with the enzyme protein disulphide isomerase (EC 5.3.4.1). 

Kasper et al. (1994) reported the selective im-munohistological localisation of protein disulphide isomerase in human type II alveolar and bronchial epithelial cells. The detection of the hidden antigen with the monoclonal antibody 5B5 usually failed in paraffin sections but succeeded after microwave pre-treatment of tissue slices. 

Signal peptidase Prolyl 4-hydroxylase Prolyl 3-hydroxylase Lysyl hydroxylase Hydroxylysyl galactosyl-transferase Hydroxylysyl glucosyMransferase Oligosaccharyl transferase Protein disulphide isomerase Prolyl-peptidyl cis/trans isomerase BiP... 

Bassuk, J. A., and Berg, R. A., 1989, Protein disulphide isomerase, a multifunctional endoplasmic reticulum protein. Matrix 9 244-258. 

J. S.Weissman and P. S. Kim, Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365, 185-188 (1993). 

Uehara T, Nakamura T, Yao D et al. (2006) S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 441, 513-517. 

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