Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Identification of collagen marker peptides for animal source identification of crocodilian leather

ABSTRACT: For species discrimination of crocodilian leather, we performed LC-MS/MS identification of type I collagen-derived marker peptides using leathers made from crocodile, alligator, caiman, and lizard skins.

ORGANISM(S): Caiman Crocodilus Fuscus Varanus Salvator Alligator Mississippiensis Crocodylus Siamensis

SUBMITTER: Yuki Taga

PROVIDER: PXD011575 | JPOST Repository | Fri Jan 04 00:00:00 GMT 2019

REPOSITORIES: jPOST

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	Alligator%20(American%20alligator)-1.baf	Other
	Alligator%20(American%20alligator)-1.mgf	Mgf
	Alligator%20(American%20alligator)-2.baf	Other
	Alligator%20(American%20alligator)-2.mgf	Mgf
	Alligator%20(American%20alligator)-3.baf	Other

Items per page:

1 - 5 of 20

Publications

Semi-Nondestructive Certification of Crocodilian Leather by LC-MS Detection of Collagen Marker Peptides.

Kumazawa Yuki Y Hattori Shunji S Taga Yuki Y

Analytical chemistry 20190114 3

Leather produced from crocodile, alligator, and caiman skin is widely used in the fashion industry. Crocodilian leather is generally more expensive than mammalian leather, and the value greatly differs even between the crocodilian species. However, inappropriate labeling of the animal source on leather products sometimes arises from accidental or fraudulent substitution, which is difficult to unambiguously detect by existing methods. In the present study, animal source identification of crocodil ...[more]

PMID: 30599131

Similar Datasets

Identification of collagen marker peptides for species identification of glue

Project description:To establish an LC-MS method for identification of the animal source of glue, we performed MS/MS identification of type I collagen-derived marker peptides using authentic collagen, glue, and leather samples after trypsin digestion.

2018-07-18 | PXD009059 | JPOST Repository

Species identification of early colonial bone artefacts excavated from Pyrmont, Australia, by mass spectrometric identification of collagen peptides

Project description:Zooarchaeology by Mass Spectrometry (ZooMS) is a rapidly developing and increasingly utilised peptide mass fingerprinting (PMF) technique that analyses Collagen 1A1 and 1A2 marker peptides for the genus- or species-level identification of fragmentary bones in the archaeological record. Traditionally, this analysis is performed using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-ToF-MS) to identify characteristic m/z values of known marker peptides. Here we present data on the application of a modified ZooMS approach, using nanoflow liquid chromatography – tandem mass spectrometry proteomics, to the analysis of a collection of six early colonial Australian (early to mid-19th Century CE) bone artefacts excavated from a site in Pyrmont, Sydney, Australia in 2017. We were successfully able to identify characteristic marker peptides for bovine COL1A1 and COL1A2 in all six artefacts.

2023-11-29 | PXD032926 | Pride

Cathepsin K Contributes to Cavitation and Collagen Turnover in Pulmonary Tuberculosis

Project description:Cavitation in tuberculosis (TB) enables highly efficient person-to-person aerosol transmission. Currently, a number of hypotheses exist regarding the mechanisms underlying this process. To explore this process, we undertook an unbiased next-generation transcriptional analysis of samples from cavity walls, grossly normal tissue from the same lung, and uninfected control lungs. Of 17,318 mapped host transcripts, only 199 showed a significant >2-fold change in cavity wall versus normal infected and uninfected samples. Amongst 22 upregulated proteases, 5 type I collagenases were over-represented; these included cathepsin K (CTSK), mast cell chymase-1 (CMA1), matrix metalloproteinase (MMP)-1, MMP-13, and MMP-14. To determine if cavitation was associated with changes in collagen turnover, we assayed serum and urinary markers of collagen metabolism in rabbits with cavitary TB versus infected controls. Serum collagen type 1 C-terminal propeptide (CICP, a marker of collagen synthesis and degradation) and urinary deoxypyridinoline (DPD, a marker of degradation) were increased by 10- (p = 0.019) and 4-fold (p = 0.068), respectively; while urinary helical peptide (a marker of degradation) was decreased 3-fold (p=0.015). This indicates that cavitation in TB is associated with significant increases of both destruction and synthesis of collagen and that cleavage of type I collagen occurs outside the known cleavage sites of MMP-1, -13 and -14. Rabbit gene expression analysis in lung tissue from M. tuberculosis infected animals. Cavitary tissue, non cavitary tissue and lung tissue from non-infected animals are compared.

2015-11-03 | E-GEOD-68206 | biostudies-arrayexpress

Cathepsin K Contributes to Cavitation and Collagen Turnover in Pulmonary Tuberculosis

2015-11-03 | GSE68206 | GEO

Bone collagen from American Avian species identification using Zooarchaeology by Mass Spectrometry (ZooMS)

Project description:The dataset is for identification of MALDI markers for peptide mass fingerprinting of bone collagen for species identification using ZooMS. Corresponding MALDI data can be found through Zenodo at 10.5281/zenodo.6363113. This dataset contatins: - raw files - peak list files - results files final confirmation biomarker searches - databases for the whole proteome, de novo marker development, and confirmation biomarker searches - csv file with information about the sample numbers

2022-06-15 | MSV000089660 | MassIVE

Palaeoproteomic data for domesticated equids (horse and donkey) collagen for Zooarchaeology by Mass Spectrometry (ZooMS)

Project description:The dataset is for identification of MALDI markers for peptide mass fingerprinting of bone collagen for species identification using ZooMS for horse and donkey using chymotrypsin. Corresponding MALDI data can be found through Zenodo at 10.5281/zenodo.6878868. This dataset contains: - raw files - peak list files - results files for the proteome search and for collagen marker identification - database for the collagen marker identification - csv file with information about the sample numbers. More information about the extraction and digestion can be found at the linked manuscript.

2022-07-21 | MSV000089943 | MassIVE

Bone collagen from South African rodent species identification using Zooarchaeology by Mass Spectrometry (ZooMS)

Project description:The dataset is for identification of MALDI markers for peptide mass fingerprinting of bone collagen for species identification using ZooMS. Corresponding MALDI data can be found through Zenodo at [ADD]. This dataset contatins: - raw files - peak list files - results files final confirmation biomarker searches - databases for the whole proteome, de novo marker development, and confirmation biomarker searches - csv file with information about the sample number

2023-02-15 | MSV000091290 | MassIVE

Effects of O2 concentration on endeometrial organoids within collagen-based gel (70% type I collagen and 30% matrigel)

Project description:We investgated effect of O2 concentration on gene expression of EMO within collagen-based gel (70% type I collagen and 30% matrigel).

2023-11-12 | GSE247420 | GEO

Bone collagen from African Bovids for species identification using Zooarchaeology by Mass Spectrometry (ZooMS)

Project description:The dataset is for identification of MALDI markers for peptide mass fingerprinting of bone collagen for species identification using ZooMS The dataset contatins: - raw files - peak list files - results files for searches against BOVIN proteome and bovine collagen sequences - database for the bovine collagen sequences - MALDI data for each sample - csv file with information about the sample numbers

2020-08-09 | MSV000085936 | MassIVE

Collagen induced arthritis in dba/1j mice associates with oxylipin changes in plasma

Project description:Oxylipins play important roles in various biological processes and are considered as mediators of inflammation for a wide range of diseases such as rheumatoid arthritis (RA). The purpose of this research was to study differences in oxylipin levels between a widely used collagen-induced arthritis (CIA) mice model and healthy control (Ctrl) mice. DBA/1J male mice (age: 6-7 weeks) were selected and randomly divided into two groups, viz. a CIA- and a Ctrl group. The CIA mice were injected intraperitoneal (i.p.) with the joint cartilage component collagen type II (CII) and an adjuvant injection of lipopolysaccharide (LPS). Oxylipin metabolites were extracted from plasma for each individual sample using solid phase extraction (SPE) and were detected with high performance liquid chromatography/tandem mass spectrometry (HPLC-ESI-MS/MS), using dynamic multiple reaction monitoring (dMRM). Both univariate and multivariate statistical analysis was applied. The results in univariate student's t-test revealed 10 significantly up- or down-regulated oxylipins in CIA mice, which were supplemented by another 6 additional oxylipins, contributing to group clustering upon multivariate analysis. The dysregulation of these oxylipins revealed the presence of ROS-generated oxylipins and an increase of inflammation in CIA mice. The results also suggested that the Collagen-induced arthritis might associate with dysregulation of apoptosis, possibly inhibited by activated NF- κ B because of insufficient PPAR-γ ligands.

2015-11-04 | MTBLS243 | MetaboLights

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data