scholarly journals Collagen survival and its use for species identification in Holocene-lower Pleistocene bone fragments from British archaeological and paleontological sites

Antiqua ◽  
2011 ◽  
Vol 1 (1) ◽  
pp. 1 ◽  
Author(s):  
Mike Buckley ◽  
Matthew James Collins
Keyword(s):  
Species Identification ◽  
Collagen Type I ◽  
Systematic Investigation ◽  
Type I ◽  
Structural Protein ◽  
Collagen Peptides ◽  
Collagen Peptide ◽  
Peptide Mass ◽  
Lower Pleistocene ◽  
Bone Fragments

Proteins have long been known to persist in Quaternary bone fossils and are often targeted as a source of carbon used in radiocarbon dating and stable isotope analyses for determining provenance and obtaining dietary information. We have previously reported a technique using the dominant structural protein collagen (type I) as a source of genetic information for species identification in modern and relatively young (Holocene) archaeological samples. We report a systematic investigation of amino acid composition and collagen peptide mass fingerprints (PMF), for a range of samples dating back approximately 1.5 million years. Extrapolation from high temperature experimental decomposition rates predict that at a constant 10°C (the approximate mean annual air temperature in Britain today) it will take between 0.2 and 0.7 Ma for levels of collagen to fall to 1% of their original concentration in an optimal burial environment. Even when the glacial intervals of the British Quaternary are factored into the temperature calculations, the more conservative of these two estimates extends the range for collagen sequencing to the Lower Pleistocene as confirmed by the presence of collagen peptides in bones from the Weybourne Crag (~1.5 Ma). Collagen fingerprinting can extend the range of identifiable taxa present at sites with large assemblages of fragmentary bone material such as that encountered at the ~900 Ka site at Happisburgh (Norfolk, UK) recently identified as showing signs of the earliest humans in Britain.

scholarly journals Collagenolytic Serine-Carboxyl Proteinase from Alicyclobacillus sendaiensis Strain NTAP-1: Purification, Characterization, Gene Cloning, and Heterologous Expression

2003 ◽  
Vol 69 (1) ◽  
pp. 162-169 ◽  
Author(s):  
Naoki Tsuruoka ◽  
Toru Nakayama ◽  
Masako Ashida ◽  
Hisashi Hemmi ◽  
Masahiro Nakao ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Molecular Mass ◽  
Gene Cloning ◽  
Collagen Type I ◽  
Protein Sequencing ◽  
Collagenolytic Activity ◽  
Efficient Production ◽  
Type I ◽  
Calculated Molecular Mass ◽  
Collagen Peptides

ABSTRACT Enzymatic degradation of collagen produces peptides, the collagen peptides, which show a variety of bioactivities of industrial interest. Alicyclobacillus sendaiensis strain NTAP-1, a slightly thermophilic, acidophilic bacterium, extracellularly produces a novel thermostable collagenolytic activity, which exhibits its optimum at the acidic region (pH 3.9) and is potentially applicable to the efficient production of such peptides. Here, we describe the purification to homogeneity, characterization, gene cloning, and heterologous expression of this enzyme, which we call ScpA. Purified ScpA is a monomeric, pepstatin-insensitive carboxyl proteinase with a molecular mass of 37 kDa which exhibited the highest reactivity toward collagen (type I, from a bovine Achilles tendon) among the macromolecular substrates examined. On the basis of the sequences of the peptides obtained by digestion of collagen with ScpA, the following synthetic peptides were designed as substrates for ScpA and kinetically analyzed: Phe-Gly-Pro-Ala*Gly-Pro-Ile-Gly (k cat, 5.41 s−1; Km , 32 μM) and Met-Gly-Pro-Arg*Gly-Phe-Pro-Gly-Ser (k cat, 351 s−1; Km , 214 μM), where the asterisks denote the scissile bonds. The cloned scpA gene encoded a protein of 553 amino acids with a calculated molecular mass of 57,167 Da. Heterologous expression of the scpA gene in the Escherichia coli cells yielded a mature 37-kDa species after a two-step proteolytic cleavage of the precursor protein. Sequencing of the scpA gene revealed that ScpA was a collagenolytic member of the serine-carboxyl proteinase family (the S53 family according to the MEROPS database), which is a recently identified proteinase family on the basis of crystallography results. Unexpectedly, ScpA was highly similar to a member of this family, kumamolysin, whose specificity toward macromolecular substrates has not been defined.

scholarly journals AP Collagen Peptides Prevent Cortisol-Induced Decrease of Collagen Type I in Human Dermal Fibroblasts

2021 ◽  
Vol 22 (9) ◽  
pp. 4788
Author(s):  
Minjung Chae ◽  
Il-Hong Bae ◽  
Sung Hwan Lim ◽  
Kyoungmi Jung ◽  
Jonghwa Roh ◽  
...  
Keyword(s):  
Stress Responses ◽  
Collagen Type ◽  
Transforming Growth Factor ◽  
Collagen Type I ◽  
Dermal Fibroblasts ◽  
Type I ◽  
Human Dermal Fibroblasts ◽  
Collagen Peptides ◽  
Wide Range ◽  
Dependent Inhibition

Cortisol is an endogenous glucocorticoid (GC) and primary stress hormone that regulates a wide range of stress responses in humans. The adverse effects of cortisol on the skin have been extensively documented but the underlying mechanism of cortisol-induced signaling is still unclear. In the present study, we investigate the effect of cortisol on collagen type I expression and the effect of AP collagen peptides, collagen tripeptide-rich hydrolysates containing 3% glycine-proline- hydroxyproline (Gly-Pro-Hyp, GPH) from the fish skin, on the cortisol-mediated inhibition of collagen type I and the cortisol-induced signaling that regulates collagen type I production in human dermal fibroblasts (HDFs). We determine that cortisol downregulates the expression of collagen type I. AP collagen peptides or GC receptor (GR) inhibitors recover the cortisol-mediated inhibition of collagen type I and GR activation. AP collagen peptides or GR inhibitors also prevent the cortisol-dependent inhibition of transforming growth factor (TGF)-β signaling. AP collagen peptides or GR inhibitors are effective in the prevention of collagen type I inhibition mediated by cortisol in senescent HDFs and reconstituted human skin models. Taken together, GR signaling might be responsible for the cortisol-mediated inhibition of TGF-β. AP collagen peptides act as GR-mediated signaling blockers, preventing the cortisol-dependent inhibition of collagen type I. Therefore, AP collagen peptides have the potential to improve skin health.

scholarly journals Self-Assembly Study of Type I Collagen Extracted from Male Wistar Hannover Rat Tail Tendons

2020 ◽  
Author(s):  
Jeimmy C. González-Masís ◽  
Jorge M. Cubero-Sesin ◽  
Yendry Regina Corrales-Ureña ◽  
Simón Guerrero ◽  
Sara González-Camacho ◽  
...  
Keyword(s):  
Self Assembly ◽  
Type I Collagen ◽  
Collagen Type I ◽  
The Body ◽  
Titration Calorimetry ◽  
Type I ◽  
Structural Protein ◽  
Calorimetric Analysis ◽  
Main Component ◽  
Rat Tail

Abstract Background: Collagen is the main structural protein in the extracellular matrix in the numerous connective tissues in the body. As the main component of connective tissue, it is the most abundant protein in mammals. Method: Collagen Type I from Wistar Hannover rat tail was obtained and it allowed to describe the thermodynamic profile during self-assembly by isothermal titration calorimetry (Nano ITC) as a novel technique. Results: The enthalpy of self-assembly of the 0,01035 moles of collagen was 33,89 mJ; relevant data in tissue engineering and 3D collagen fibrils bio-impressions organs, with a periodicity of 65 nm were obtained and characterized. Conclusions: Calorimetric analysis shows higher energy release event at the isoelectric point of the protein, suggesting an overall exothermic process due to self-assembly of the collagen and an endothermic process due to aggregation of denatured collagen.

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