Back to Search
Start Over
Prolyl hydroxylation in elastin is not random
- Source :
- Biochimica et Biophysica Acta (BBA) - General Subjects. 1860:2169-2177
- Publication Year :
- 2016
- Publisher :
- Elsevier BV, 2016.
-
Abstract
- Background This study aimed to investigate the prolyl and lysine hydroxylation in elastin from different species and tissues. Methods Enzymatic digests of elastin samples from human, cattle, pig and chicken were analyzed using mass spectrometry and bioinformatics tools. Results It was confirmed at the protein level that elastin does not contain hydroxylated lysine residues regardless of the species. In contrast, prolyl hydroxylation sites were identified in all elastin samples. Moreover, the analysis of the residues adjacent to prolines allowed the determination of the substrate site preferences of prolyl 4-hydroxylase. It was found that elastins from all analyzed species contain hydroxyproline and that at least 20%–24% of all proline residues were partially hydroxylated. Determination of the hydroxylation degrees of specific proline residues revealed that prolyl hydroxylation depends on both the species and the tissue, however, is independent of age. The fact that the highest hydroxylation degrees of proline residues were found for elastin from the intervertebral disc and knowledge of elastin arrangement in this tissue suggest that hydroxylation plays a biomechanical role. Interestingly, a proline-rich domain of tropoelastin (domain 24), which contains several repeats of bioactive motifs, does not show any hydroxyproline residues in the mammals studied. Conclusions The results show that prolyl hydroxylation is not a coincidental feature and may contribute to the adaptation of the properties of elastin to meet the functional requirements of different tissues. General significance The study for the first time shows that prolyl hydroxylation is highly regulated in elastin.
- Subjects :
- 0301 basic medicine
Proline
Swine
Lysine
Biophysics
Hydroxylation
Biochemistry
Prolyl Hydroxylases
03 medical and health sciences
Hydroxyproline
chemistry.chemical_compound
medicine
Animals
Humans
Molecular Biology
030102 biochemistry & molecular biology
biology
Tropoelastin
Elastin
Hydroxylysine
030104 developmental biology
medicine.anatomical_structure
chemistry
Organ Specificity
biology.protein
Cattle
Collagen
Chickens
Protein Processing, Post-Translational
Elastic fiber
Subjects
Details
- ISSN :
- 03044165
- Volume :
- 1860
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Accession number :
- edsair.doi.dedup.....f5b5f6a0383fa80e38f5d5b0dcec486f