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- Title
Isolation and mass spectrometry based hydroxyproline mapping of type II collagen derived from Capra hircus ear cartilage.
- Authors
Maity, Priti Prasanna; Dutta, Debabrata; Ganguly, Sayan; Kapat, Kausik; Dixit, Krishna; Chowdhury, Amit Roy; Samanta, Ramapati; Das, Narayan Chandra; Datta, Pallab; Das, Amit Kumar; Dhara, Santanu
- Abstract
Collagen II (COLII), the most abundant protein in vertebrates, helps maintain the structural and functional integrity of cartilage. Delivery of COLII from animal sources could improve cartilage regeneration therapies. Here we show that COLII can be purified from the Capra ear cartilage, a commonly available bio-waste product, with a high yield. MALDI-MS/MS analysis evidenced post-translational modifications of the signature triplet, Glycine-Proline-Hydroxyproline (G-P-Hyp), in alpha chain of isolated COLII (COLIIA1). Additionally, thirty-two peptides containing 59 Hyp residues and a few G-X-Y triplets with positional alterations of Hyp in COLIIA1 are also identified. Furthermore, we show that an injectable hydrogel formulation containing the isolated COLII facilitates chondrogenic differentiation towards cartilage regeneration. These findings show that COLII can be isolated from Capra ear cartilage and that positional alteration of Hyp in its structural motif, as detected by newly developed mass spectrometric method, might be an early marker of cartilage disorder. Priti Prasanna Maity et al. develop a method for high-yield isolation of type II collagen from the Capra hircus ear cartilage, a commonly available biowaste product. Using mass spectrometry they mapped the positions of hydroxyproline within the collagen II alpha chain; this methodology facilitates isolation and characterization of this biomedical resource.
- Subjects
COLLAGEN; MASS spectrometry; HYDROXYPROLINE; GOATS; CARTILAGE
- Publication
Communications Biology, 2019, Vol 2, Issue 1, pN.PAG
- ISSN
2399-3642
- Publication type
Article
- DOI
10.1038/s42003-019-0394-6