The appearance of free hydroxyproline as the major product of degradation of newly synthesized collagen in cell culture

doi:10.1016/0304-4165(82)90236-7

Biochimica et Biophysica Acta (BBA) - General Subjects

Volume 719, Issue 3, 17 December 1982, Pages 480-487

https://doi.org/10.1016/0304-4165(82)90236-7 Get rights and content

Abstract

Embryonic lung fibroblasts and rabbit vascular smooth muscle cells have the ability to degrade newly synthesized collagen. Analysis of 24-h pulse media from cultures given [¹⁴C]proline demonstrates that greater than 90% of the degraded collagen is represented by free hydroxyproline rather than the peptide-bound imino acid. The addition of cycloheximide or α-α-dipyridyl to the culture medium during the pulse period severely diminished the formation of the free hydroxyproline demonstrating its enzymatic and protein (collagen) origin. It is proposed that assessment of free hydroxyproline formation may allow us to distinguish between intracellular and extracellular collagen degradation.

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Collagen is the key structural component of collagenous tissues (Tornberg, 2005). Collagen with a triple helix structure is almost water-insoluble while it becomes water-soluble via degradation (Imberman et al., 1982). Thus, the contents of soluble collagen, dissolution rate of Hyp and GAG were determined to estimate changes in collagenous tissue proteins in abalone muscles during heat treatment.
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Collagen is the main structural component of the connective tissues (Tornberg, 2005). Generally, collagen with a triple helix structure is almost water-insoluble, however, it becomes water-soluble when degraded into collagen polypeptides (Imberman, Oppenheim, & Franzblau, 1982). Therefore, the release of water-soluble Hyp indicates the degradation of collagens.
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Among which, the combination of TP and OA showed the best inhibitory effects, followed by OA and TP. Collagen with a complete triple helix structure is almost completely water-insoluble, however it becomes water-soluble when degraded into collagen polypeptides (Imberman, Oppenheim, & Franzblau, 1982). Therefore, the release of water-soluble Hyp, the characteristic amino acid of collagen, is a marker for the degradation of monomeric collagen.
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Citation Excerpt :
Collagen is a major component of the body wall of sea cucumbers, and it accounts for about 70% of the total protein in the body wall (Saito, Kunisaki, Urano, & Kimura, 2002). The degree of collagen degradation in sea cucumbers can be represented by free hydroxyproline content (Imberman, Oppenheim, & Franzblau, 1982; Sakamoto et al., 2015). The free hydroxyproline concentration of samples with different moisture content increased significantly during the entire storage period, as shown in Table 2 (p < 0.05), which indicates that collagen decomposed in all the samples to different degrees.
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The appearance of free hydroxyproline as the major product of degradation of newly synthesized collagen in cell culture

Abstract

J. Biol. Chem.

Int. Rev. Connect. Tissue Res.

Biochim. Biophys. Acta

Anal. Biochem.

J. Biol. Chem.

Biochim. Biophys. Acta

FEBS Lett.

Nature