Collagen procollagen mRNA

Figure 3.4 Factors affecting foreign body reaction and potential points of intervention at the level of the myofibroblast (1) inhibit synthesis or release of TGF-P (2) block stimulation by TGF-P of its membrane receptors on the activated fibroblast (3) inhibit the Smad proteins, which transfer the TGF-P effect to the nucleus (4) inhibit transcription of procollagen mRNA (5) inhibit translation of the message to form procollagen (6) inhibit prolyl-4-hydroxylase, which creates hydroxyproline and facilitates helix formation (7) inhibit lysyl oxidase, which cross-links the collagen (8) enhance the function of MMPs, which degrade collagen, or inhibit TIMPs, which degrade MMPs.

Tajima, S., and Pinnell, S. R., 1982, Regulation of collagen synthesis by ascorbic acid. Ascorbic acid increases type I procollagen mRNA, Biochem. Biophys. Res. Commun. 106 632-637. 

The procollagen peptidase is sometimes lacking. In other cases a person synthesizes an abnormal pro-o2 chain that is resistant to cleavage by the peptidase because of deletion of the normal cleavage site. In others collagen is formed in only small amounts or is degraded rapidly. Some individuals lack lysyl hydroxylase and others have a defect in mRNA splicing which causes loss of an exon from the mRNA and synthesis of shortened pro-o2 chains. ... 

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