Novel approach to study the initial events in the folding and assembly of procollagen

Seminars in Cell and Developmental Biology

Volumn 7, Issue 5, 1996, Pages 667-672

  Bulleid, Neil J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Collagen; Disulphide bond formation; Procollagen; Protein folding; Selection

Indexed keywords

EID: 0001157739     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1996.0081     Document Type: Article

References (29)

1. Prockop DJ, Kivirikko KI (1995) Collagens: molecular biology, diseases, and potential for therapy. Annu Rev Biochem 64:403-434
2. Kivirikko KI, Myllylä R, Pihlajaniemi T (1992) Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins, in Post-translational Modification of Proteins (Harding JJ, Crabbe MJC, eds) pp 1-52. CRC press, Boca Raton, Florida
3. Doege KJ, Fessler JH (1986) Folding of carboxyl domain and assembly of procollagen I. J Biol Chem 261:8924-8935
4. Schofield DJ, Uitto J, Prockop DJ (1974) Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cells. Biochemistry 13:1801-1806
5. Olsen BR, Hoffman H-P, Prockop DJ (1976) Interchain disulfide bonds at the COOH-terminal end of procollagen synthesized by matrix-free cells from chick embryonic tendon and cartilage. Arch Biochem Biophys 175:341-350
6. Brucker P, Bächinger H-P, Timpl R, Engel J (1978) Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix to coil transition. Eur J Biochem 90:595-603
7. Berg RA, Prockop DJ (1973) The thermal transition of a nonhydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilising the triple helix of collagen. Biochem Biophys Res Commun 52:115-120
8. 14C] protocollagen and its hydroxylation by prolyl-hydroxylase. Biochemistry 12:3395-3401
9. Fessler LI, Timpl R, Fessler JH (1981) Assembly and processing of procollagen type III in chick embryo blood vessels. J Biol Chem 256:2531-2537
10. Nakai A, Satoh M, Hirayoshi K, Nagata K (1992) Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum. J Cell Biol 117:903-914
11. Smith T, Ferreira LR, Hebert C, Norris K, Sauk JJ (1995) Hsp47 and cyclophylin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. J Biol Chem 270:18323-18328
12. Prockop DJ, Constantinou CD, Dombrowski KE, Hojima Y, Kadler KE, Kuvaniemi H, Tromp G, Vogel BE (1989) Type I procollagen: the gene-protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissue. Am J Med Gen 34:60-67
13. Byers PH (1989) Inherited disorders of collagen gene structure and expression. Am J Med Gen 34:72-80
14. Williams CJ, Prockop DJ (1983) Synthesis and processing of a type I procollagen containing shortened proα1(I) chains by fibroblasts from a patient with osteogenesis imperfecta. J Biol Chem 258:5915-5921
15. Superti-Furga A, Steinmann B (1988) Impaired secretion of type III procollagen in Ehlers-Danlos syndrome type IV fibroblasts: correction of the defect by incubation at reduced temperature and demonstration of subtle alterations in the triple-helical region of the molecule. Biochem Biophys Res Commun 150:140-147
16. Byers PH (1993) Osteogenesis imperfecta, in Connective Tissues and its Heritable Disorders (Royce PM, Steinmann B, ed.) pp 317-350. Wiley-Liss, New York
17. Wilson R, Oliver J, Brookman JL, High S, Bulleid NJ (1995) Development of a semi-permeabilised cell system to study the translocation, folding, assembly and transport of secretory proteins. Biochem J 307:679-687
18. Pihlajaniemi T, Myllyla R, Alitalo K, Vaheri A, Kivirikko KI (1981) Post-translational modifications in the biosynthesis of type IV collagen by a human tumor cell-line. Biochemistry 20:7409-7415
19. Bulleid NJ, Wilson R, Lees JF (1996) Type III procollagen assembly in semi-intact cells: chain association, nucleation and triple helix folding do not require formation of inter-chain disulfide bonds but triple helix nucleation does require hydroxylation. Biochem J, 317:195-202
20. Bruckner P, Prockop DJ (1981) Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Analyt Biochem 110:360-368
21. Fessler LI, Fessler JH (1979) Characterization of type III procollagen from chick embryo blood vessels. J Biol Chem 254:233-239
22. Chessler SD, Byers PH (1993) BiP binds type I procollagen proα chains with mutations in the carboxy-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J Biol Chem 268:18226-18233
23. Chessler SD, Byers PH (1992) Defective folding and stable association with protein disulfide isomerase/ prolyl hydroxylase of type I procollagen with a deletion in the proα2(I) chain that preserves the gly-X-Y repeat pattern. J Biol Chem 267:7751-7757
24. Lamandé SR, Bateman JF (1995) The type I collagen proα1(I) COOH-terminal propeptide N-linked oligosaccharide: functional analysis by site-directed mutagenesis. J Biol Chem 270:17858-17865
25. Koivu J, Myllylä R (1987) Interchain disulfide bond formation in types I and II procollagen: evidence for a protein disulfide isomerase catalysing bond formation. J Biol Chem 262:6159-6164
26. Lees JF, Bulleid NJ (1994) The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and III procollagen. J Biol Chem 269:24354-24360
27. Hammond C, Braakman I, Helenius A (1994) Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci 91:913-917
28. Peterson JR, Ora A, Van PN, Helenius A (1995) Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol Biol Cell 6:1173-1184
29. Satoh M, Hirayoshi K, Yokota S, Hosokawa N, Nagata K (1996) Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen. J Cell Biol 133:469-483