Occurrence of Glycylhydroxypyrolyl Sequences in Earthworm Cuticle Collagen

Goldstein, A.; Adams, Elijah

doi:10.1016/s0021-9258(18)93346-6

Cited by 31 publications

(8 citation statements)

References 22 publications

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“…21 The results for earthworm are consistent with previous data that 4Hyp was detected at the Xaa position at an approximately 2-fold higher rate than at the Yaa position. 21 In addition, our data also agree with a 50-year-old prediction (approximately 100 residues/1000 residues of Xaa position 4Hyp), which was calculated based on the low thermal stability of earthworm cuticle collagen (melting temperature = 22 °C). 34 4Hyp largely present at the Xaa position appears to be unrelated with the thermal stability of collagen.…”

Section: ■ Results and Discussionsupporting

confidence: 91%

“…Collagen present in earthworm cuticles is reported to contain a much larger amount of 4Hyp at the Xaa position than at the Yaa position. 21,22 This finding was obtained by N-terminal amino acid sequence analysis of collagenase-released Gly-Xaa-Yaa tripeptides, but the method could not confidently determine the positional distribution of 4Hyp due to carryover from preceding cycles. 21,22 We extracted collagen from earthworm cuticles using acetic acid and performed amino acid analysis (Table S3).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Collagen present in earthworm cuticles is reported to contain a much larger amount of 4Hyp at the Xaa position than at the Yaa position. , This finding was obtained by N-terminal amino acid sequence analysis of collagenase-released Gly-Xaa-Yaa tripeptides, but the method could not confidently determine the positional distribution of 4Hyp due to carryover from preceding cycles. , We extracted collagen from earthworm cuticles using acetic acid and performed amino acid analysis (Table S3). The amino acid composition was consistent with the published data .…”

Section: Resultsmentioning

confidence: 99%

“…The estimation by our method was based on the assumption that earthworm collagen entirely consists of uninterrupted Gly-Xaa-Yaa repeating sequences. Although the amino acid sequence has not been determined, sequence analysis of the collagenase digest of earthworm collagen indicated that most portions are collagenous sequences …”

Section: Resultsmentioning

confidence: 99%

“…We validated the efficiency of peptide generation by partial acid hydrolysis using model peptides and optimized the LC conditions for separating APDS-derivatized dipeptides. We analyzed bovine fibrillar collagens, including type I, III, and V collagens, as well as earthworm cuticle collagen in which Pro residues at the Xaa position are reported to be substantially 4-hydroxylated. , The quantitative accuracy of our method was verified by Edman sequencing followed by LC–MS detection of released phenylthiohydantoin (PTH) derivatizes of Pro, 4Hyp, and 3Hyp.…”

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confidence: 99%

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Quantitative Analysis of the Positional Distribution of Hydroxyproline in Collagenous Gly-Xaa-Yaa Sequences by LC–MS with Partial Acid Hydrolysis and Precolumn Derivatization

2020

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Collagen is extensively modified by various enzymes, including prolyl hydroxylases. Pro residues at the Yaa position of repeating Gly-Xaa-Yaa amino acid sequences are mostly hydroxylated to 4-hydroxyproline (4Hyp), which is essential for the thermal stability of collagen triple helix. In contrast, Pro residues at the Xaa position are rarely modified to 3Hyp and 4Hyp, the biological function of which is poorly understood. Overall estimation of prolyl hydroxylation with discrimination of the position (Xaa or Yaa) and hydroxylation type (4Hyp or 3Hyp) has been difficult to perform using traditional methods. In the present study, we developed a novel position-specific analytical method featuring LC−MS detection of collagenous Gly-containing dipeptides, including Gly-Pro, Pro-Gly, Gly-4Hyp, Gly-3Hyp, and 4Hyp-Gly, after partial acid hydrolysis and precolumn derivatization using 3-aminopyridyl-Nhydroxysuccinimidyl carbamate (APDS). We performed acid hydrolysis at 55 °C with HCl/trifluoroacetic acid/water (2:1:1, v/v) to avoid peptide inversion and imbalanced peptide generation observed for collagenous model peptides. The positional distribution of Pro, 4Hyp, and 3Hyp can be calculated from the relative concentrations of the APDS-derivatized dipeptides, and in combination with amino acid analysis, we can determine their absolute contents at the Xaa and Yaa positions. Bovine type I, III, and V collagens were analyzed by the established method, and the amount of 4Hyp was higher than that of 3Hyp at the Xaa position in type I and III collagens. In addition, we clearly showed that collagen extracted from earthworm cuticles has an extremely high content of Xaa position 4Hyp, reaching over 10% of the total amino acids.

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Section: ■ Results and Discussionsupporting

confidence: 91%

Section: ■ Results and Discussionmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Quantitative Analysis of the Positional Distribution of Hydroxyproline in Collagenous Gly-Xaa-Yaa Sequences by LC–MS with Partial Acid Hydrolysis and Precolumn Derivatization

2020

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New analysis of the phylogenetic change of collagen thermostability

Burjanadze

2000

Biopolymers

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Recent data concerning the thermostability and the primary structure of type IV collagens, some invertebrate collagens, and for the stability of synthetic collagen‐like polypeptides, show that our earlier analysis of the phylogenetic change of thermostability has some shortcomings. The results of the analysis were corrected and it has been shown that the dependence of denaturation temperature Td on 4‐hydroxyproline content is hyperbolic and the total Gly‐Pro‐Hyp sequence content is a main, but not exclusive, factor influencing the change of collagen thermostability. It appears possible that the same mechanism underlies the thermostability of fibril‐forming collagens of all animal life, ranging from Antarctic ice fish to at least one annelid (Alvinella pompejana) living at very high temperatures at the bottom of the ocean near thermal vents. © 2000 John Wiley & Sons, Inc. Biopoly 53: 523–528, 2000

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Collagenolytic Enzymes

Nordwig¹

1971

Advances in Enzymology - And Related Areas of Molecular Biology

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Occurrence of Glycylhydroxypyrolyl Sequences in Earthworm Cuticle Collagen

Cited by 31 publications

References 22 publications

Quantitative Analysis of the Positional Distribution of Hydroxyproline in Collagenous Gly-Xaa-Yaa Sequences by LC–MS with Partial Acid Hydrolysis and Precolumn Derivatization

Quantitative Analysis of the Positional Distribution of Hydroxyproline in Collagenous Gly-Xaa-Yaa Sequences by LC–MS with Partial Acid Hydrolysis and Precolumn Derivatization

New analysis of the phylogenetic change of collagen thermostability

Collagenolytic Enzymes

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