Collagen fibrils formation

Mineral dust-induced ROMs contributes to pulmonary fibrosis, malignancy, hypersensitivity and emphysema (Doelman etctl., 1990 Kamp etui., 1992). The involvement of ROMs in pulmonary fibrotic reactions is indicated by the participation of PMN oxidants in the autoactivation of latent coUagenase (Weiss et al., 1985). Prolyl hydroxylase, a key enzyme in collagen fibril formation, has been shown to be dependent on the reaction of superoxide with prolyl residues (Myllyla et al., 1979). 

Morimoto K, Kawabata K, Kunii S, Hamano K, Saito T, Tonomura B (2009) Characterization of type I collagen fibril formation using thioflavin T fluorescent dye. J Biochem 145(5) 677... 

Haston, J. L., FitzGerald, O., Kane, D., and Smith, K. D. (2002). Preliminary observations on the influence of rheumatoid alpha-l-acid glycoprotein on collagen fibril formation. Biomed. Chromatogr. 16, 332-342. 

MacBeath, J. R., Shackleton, D. R., and Hulmes, D. J. S. (1993). Tyrosine-rich acidic matrix protein (TRAMP) accelerates collagen fibril formation in vitro. J. Biol. Chem. 268, 19826-19832. 

Kadler KE, Holmes DF, Trotter JA, Chapman JA. Collagen fibril formation, Biochem J. 1996 316 1-11. 

A procollagen triple helix is assembled in the endoplasmic reticulum helix formation is aided by disulfide bonds between N- and C-terminal propeptides, which align the polypeptide chains. Post-translational modification of procollagen is crucial in allowing for collagen fibril formation. For example, in cells deprived of ascorbate, as in the disease scurvy, the procollagen chains are not hydroxylated sufficiently to form stable triple helices at normal body temperature (hydrox-ylation is through the activity of prolyl hydroxylase, which requires the cofactor ascorbic acid). 

L13. Lien, Y.-H., Stern, R., Fu, J. G. G., and Siegel, R. G., Inhibition of collagen fibril formation in vitro and subsequent cross-linking by glucose. Science 225, 1489-1491... 

Lumican was originally discovered in the cornea (34), and later named for its putative role in controlling corneal transparency (10,35). Fibromodulin was first extracted from articular cartilage and named for its effects on collagen fibril formation in vitro (11). Both lumican and fibromodulin are only minor components of skin but are important to its structure, as attested to by the changes seen in the skins of null mice (36). 

Comper, W.D. and Veis, A. 1977. Characterization of nuclei in vitro collagen fibril formation. Biopolymers... 

Lowther, D. A, and Natarjan, M. The influence of glycoprotein on collagen fibril formation in the presence of chondroltin sulphate pro- 231. teoglycan. Biochem. J., 127 607-608,1972. 

Gehiian, R.A. and Piez, K.A. (1980) Collagen fibril formation in v itro. A quasielastic light-scattering study of early stages. /. Biol. Chem., 255, 8098-8102. 

---