Isolation and mass spectrometry based hydroxyproline mapping of type II collagen derived from Capra hircus ear cartilage

Priti Prasanna Maity, Debabrata Dutta, Sayan Ganguly, Kausik Kapat, Krishna Dixit, Amit Roy Chowdhury, Ramapati Samanta, Narayan Chandra Das, Pallab Datta, Amit Kumar Das, Santanu Dhara

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11 Scopus citations

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.

Original languageEnglish
Article number146
JournalCommunications Biology
Volume2
Issue number1
DOIs
StatePublished - 1 Dec 2019
Externally publishedYes

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Publisher Copyright:
© 2019, The Author(s).

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