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

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

doi:10.1038/s42003-019-0394-6

Cited by 15 publications

(12 citation statements)

References 46 publications

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“…Such varied patterns of 3Hyp make it challenging to pin down the specific molecular interactions involving 3Hyp. At the same time, collagens have been used as biomarkers for disease detection, species identification, and investigations of the involvement of collagen in cancer metastasis, tissue remodeling, the homeostasis of the extracellular matrix, and the mineralization process of bones, to name just a few [ 15 – 18 ]. The unpredictable nature of prolyl-3-hydroxylation has hampered the application of MS in these and other related research that rely on a precise knowledge of the genomic sequence and the PTMs of specific segments of collagen.…”

Section: Introductionmentioning

confidence: 99%

Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry

Kirchner

Deng

2021

PLoS ONE

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Collagen is the major protein in the extracellular matrix and plays vital roles in tissue development and function. Collagen is also one of the most processed proteins in its biosynthesis. The most prominent post-translational modification (PTM) of collagen is the hydroxylation of Pro residues in the Y-position of the characteristic (Gly-Xaa-Yaa) repeating amino acid sequence of a collagen triple helix. Recent studies using mass spectrometry (MS) and tandem MS sequencing (MS/MS) have revealed unexpected hydroxylation of Pro residues in the X-positions (X-Hyp). The newly identified X-Hyp residues appear to be highly heterogeneous in location and percent occupancy. In order to understand the dynamic nature of the new X-Hyps and their potential impact on applications of MS and MS/MS for collagen research, we sampled four different collagen samples using standard MS and MS/MS techniques. We found considerable variations in the degree of PTMs of the same collagen from different organisms and/or tissues. The rat tail tendon type I collagen is particularly variable in terms of both over-hydroxylation of Pro in the X-position and under-hydroxylation of Pro in the Y-position. In contrast, only a few unexpected PTMs in collagens type I and type III from human placenta were observed. Some observations are not reproducible between different sequencing efforts of the same sample, presumably due to a low population and/or the unpredictable nature of the ionization process. Additionally, despite the heterogeneous preparation and sourcing, collagen samples from commercial sources do not show elevated variations in PTMs compared to samples prepared from a single tissue and/or organism. These findings will contribute to the growing body of information regarding the PTMs of collagen by MS technology, and culminate to a more comprehensive understanding of the extent and the functional roles of the PTMs of collagen.

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Section: Introductionmentioning

confidence: 99%

Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry

Kirchner

Deng

2021

PLoS ONE

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“…Collagen, the most abundant fibrous protein, is found within hard and soft tissues, such as connective tissue [126], skin [127][128][129], tendon [130], cornea [131], and cartilage [132][133][134][135], and is a crucial constituent of the ECM [136]. In this regard, collagen derived from the bovine [137], porcine [138], fish [139], marine sponge [140], shellfish [141], and jellyfish [142] is largely explored, so as to be utilized as a biocompatible material in various fields [143].…”

Section: Collagen-based Hydrogelsmentioning

confidence: 99%

Protein-Based Hydrogels: Promising Materials for Tissue Engineering

et al. 2022

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The successful design of a hydrogel for tissue engineering requires a profound understanding of its constituents’ structural and molecular properties, as well as the proper selection of components. If the engineered processes are in line with the procedures that natural materials undergo to achieve the best network structure necessary for the formation of the hydrogel with desired properties, the failure rate of tissue engineering projects will be significantly reduced. In this review, we examine the behavior of proteins as an essential and effective component of hydrogels, and describe the factors that can enhance the protein-based hydrogels’ structure. Furthermore, we outline the fabrication route of protein-based hydrogels from protein microstructure and the selection of appropriate materials according to recent research to growth factors, crucial members of the protein family, and their delivery approaches. Finally, the unmet needs and current challenges in developing the ideal biomaterials for protein-based hydrogels are discussed, and emerging strategies in this area are highlighted.

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“…This helical conformation requires the presence of a repetitive motif in its core, namely Gly-X-Y-, in which glycine (Gly) residues are repeated at every third position while the X and Y positions are made up of proline and hydroxyproline moieties. The presence of these is critical for the stability of the collagen structure, due to the formation of intermolecular hydrogen bonds [170,171].…”

Section: Collagen-based Hydrogelsmentioning

confidence: 99%

Recent Advances of Taxol-Loaded Biocompatible Nanocarriers Embedded in Natural Polymer-Based Hydrogels

Voci

Gagliardi

Molinaro

et al. 2021

Gels

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The discovery of paclitaxel (PTX) has been a milestone in anti-cancer therapy and has promoted the development and marketing of various formulations that have revolutionized the therapeutic approach towards several malignancies. Despite its peculiar anti-cancer activity, the physico-chemical properties of PTX compromise the administration of the compound in polar media. Because of this, since the development of the first Food and Drug Administration (FDA)-approved formulation (Taxol®), consistent efforts have been made to obtain suitable delivery systems able to preserve/increase PTX efficacy and to overcome the side effects correlated to the presence of some excipients. The exploitation of natural polymers as potential materials for drug delivery purposes has favored the modulation of the bioavailability and the pharmacokinetic profiles of the drug, and in this regard, several formulations have been developed that allow the controlled release of the active compound. In this mini-review, the recent advances concerning the design and applications of natural polymer-based hydrogels containing PTX-loaded biocompatible nanocarriers are discussed. The technological features of these formulations as well as the therapeutic outcome achieved following their administration will be described, demonstrating their potential role as innovative systems to be used in anti-tumor therapy.

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

Cited by 15 publications

References 46 publications

Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry

Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry

Protein-Based Hydrogels: Promising Materials for Tissue Engineering

Recent Advances of Taxol-Loaded Biocompatible Nanocarriers Embedded in Natural Polymer-Based Hydrogels

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