collagen molecule
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2022 ◽  
pp. 29-54
Author(s):  
Béla Suki
Keyword(s):  

Polymers ◽  
2021 ◽  
Vol 13 (23) ◽  
pp. 4134
Author(s):  
Yuliya Nashchekina ◽  
Pavel Nikonov ◽  
Nataliya Mikhailova ◽  
Alexey Nashchekin

Collagen in the body is exposed to a range of influences, including free radicals, which can lead to a significant change in its structure. Modeling such an effect on collagen fibrils will allow one to get a native structure in vitro, which is important for modern tissue engineering. The aim of this work is to study the effect of free radicals on a solution of hydrogen peroxide with a concentration of 0.006–0.15% on the structure of collagen fibrils in vitro, and the response of cells to such treatment. SEM measurements show a decrease in the diameter of the collagen fibrils with an increase in the concentration of hydrogen peroxide. Such treatment also leads to an increase in the wetting angle of the collagen surface. Fourier transform infrared spectroscopy demonstrates a decrease in the signal with wave number 1084 cm−1 due to the detachment of glucose and galactose linked to hydroxylysine, connected to the collagen molecule through the -C-O-C- group. During the first day of cultivating ASCs, MG-63, and A-431 cells, an increase in cell adhesion on collagen fibrils treated with H2O2 (0.015, 0.03%) was observed. Thus the effect of H2O2 on biologically relevant extracellular matrices for the formation of collagen scaffolds was shown.


PLoS ONE ◽  
2021 ◽  
Vol 16 (10) ◽  
pp. e0258699
Author(s):  
Shunji Hattori ◽  
Tomomi Kiriyama-Tanaka ◽  
Masashi Kusubata ◽  
Yuki Taga ◽  
Testuya Ebihara ◽  
...  

We investigated the characteristics of extracellular matrix (ECM) in the soft tissue of two frozen baby woolly mammoths (Mammuthus primigenius) that died and were buried in Siberian permafrost approximately 40,000 years ago. Morphological and biochemical analyses of mammoth lung and liver demonstrated that those soft tissues were preserved at the gross anatomical and histological levels. The ultrastructure of ECM components, namely a fibrillar structure with a collagen-characteristic pattern of cross-striation, was clearly visible with transmission and scanning electron microscopy. Type I and type IV collagens were detected by immunohistochemical observation. Quantitative amino acid analysis of liver and lung tissues of the baby mammoths indicated that collagenous protein is selectively preserved in these tissues as a main protein. Type I and type III collagens were detected as major components by means of liquid chromatography–mass spectrometry analysis after digestion with trypsin. These results indicate that the triple helical collagen molecule, which is resistant to proteinase digestion, has been preserved in the soft tissues of these frozen mammoths for 40,000 years.


Author(s):  
Ivaneta D Yoncheva ◽  
Denislav E Biserov ◽  
Maria N Negreva MD

The myocardium consists of several types of cells: cardiomyocytes, cardiac fibroblasts, endothelial cells and smooth muscle cells. Fibroblasts are cells of mesenchymal origin and are present in all tissues in the body. Cardiac damage can activate available CFBs, provoke transformation of endothelial or epithelial cells into fibroblasts, or induce the production of CFBs from hematopoietic cells and bone marrow. The change in ECM is a key point in the remodeling of the heart in response to the disease process. Disruption of the reticular structure of the ECM alters the connection between myocardial cells and blood vessels, thereby disrupting the structure and function of the heart muscle. Type I and III collagen fibrils are the predominant part of the ECM of the heart. They are synthesized as procollagen, which is converted to a mature collagen molecule. Procollagen type I propeptide (PICP), amino-terminal propeptide type I procollagen (PINP) and N terminal type III collagen peptide (PIIINP) are released in proportional amounts in the synthesis of collagen types I and III and can be used as serum markers for these processes. On the other hand the differentiation from CFBs to myoFB is supported by the transforming growth factor beta (TGF-β), connective tissue growth factor (CTGF), a number of cytokines in the ECM and others. The scientific community is faced with the question of which biomarkers to use to identify the early stages of development of cardiac fibrosis, as well as how to assess the degree of progression of this pathological process.


2021 ◽  
Author(s):  
Shunji Hattori ◽  
Tomomi Kiriyama-Tanaka ◽  
Masashi Kusubata ◽  
Yuki Taga ◽  
Testuya Ebihara ◽  
...  

We investigated the characteristics of extracellular matrix (ECM) in the soft tissue of two frozen baby woolly mammoths ( Mammuthus primigenius ) that died and were buried in Siberian permafrost approximately 40,000 years ago. Morphological and biochemical analyses of mammoth lung and liver demonstrated that those soft tissues were preserved at the gross anatomical and histological levels. The ultrastructure of ECM components, namely a fibrillar structure with a collagen-characteristic pattern of cross-striation, was clearly visible with transmission and scanning electron microscopy. Type I and type IV collagens were detected by immunohistochemical observation. Quantitative amino acid analysis of liver and lung tissues of the baby mammoths indicated that collagenous protein is selectively preserved in these tissues as a main protein. Type I and type III collagens were detected as major components by means of liquid chromatography–mass spectrometry analysis after digestion with trypsin. These results indicate that the triple helical collagen molecule, which is resistant to proteinase digestion, has been preserved in the soft tissues of these frozen mammoths for 40,000 years.


2021 ◽  
Vol 12 (1) ◽  
pp. 6-13
Author(s):  
L. V. Vasilyeva ◽  
E. N. Bezzubtseva ◽  
E. V. Gosteva ◽  
E. F. Evstratova

Osteoporosis is a progressive multifactorial systemic disease of the skeletal system characterized by the damage of the microarchitectonics of the bone tissue, which leads to the occurrence of low-energy fractures and impairment of the quality of life of individuals. The risk factors for the development of osteoporosis include smoking, which inhibits calcium absorption in the intestine and not only contributes to the reduction of bone density but also acts as a predictor of bronchopulmonary pathology. The systemic inflammation that develops in patients with chronic obstructive pulmonary disease, associated with the production of interleukins (IL)-6, IL-1, IL-8, and tumor necrosis factor – α, stimulates osteoclast-mediated bone resorption and a low level of osteoprotegerin closes the circle. In clinical practice, the determination of markers of bone resorption is required. This is a tartrate-resistant acid phosphatase, the 5β fraction of which signals the end of the resorption process; these are hydroxypyridine crosslinks – pyridoline (PYD) and deoxypyridoline, that stabilize the bone collagen molecule. Genetic factors also play an important role in the development of osteoporosis. The presence of the GG genotype or the G allele of the 283 A> G polymorphism (Bsml) of the VDR gene is a predictor of osteoporosis of the lumbar vertebrae L1-L4. The substitution of cytosine for thymine (C> T) in exon 17 of the calcitonin gene (CALCR) at position 1340 leads to the substitution of the amino acid proline (CCG) for leucine (CTG) at position 463 of the receptor protein molecule and affects bone density. But the most phylogenetically ancient mechanism for regulating the development and maintenance of tissue homeostasis by controlling cell proliferation, differentiation, migration, and apoptosis is the Wnt signaling pathway (SP-Wnt). Alterations in Wnt signaling observed in cases of genetic mutations cause various diseases of the human skeleton. A systematic literature search was carried out using the Scopus, PubMed, Web of Science databases.


2020 ◽  
Vol 58 (4) ◽  
Author(s):  
Takeshi Nagai ◽  
Masataka Saito ◽  
Yasuhiro Tanoue ◽  
Norihisa Kai ◽  
Nobutaka Suzuki

Research background. Animal collagen has been widely utilized in foods, cosmetics, and biomedical fields. The non-edible portion, such as fish skins and bones, are generated during cooking processes. Most of them are currently discarded as wastes, although the nutritional values of the skins and bones are high. It needs to utilize the non-edible portion for the reduction of environmental impact, as it may be one of source of environmental pollution. Experimental approach. Collagen was prepared from Sakhalin taimen skins as wastes generated during cooking processes. Next, the color, SDS-polyacrylamide gel electrophoresis, ultraviolet absorption, subunit composition, amino acid composition, denaturation temperature, and attenuated total reflectance-Fourier transform infrared spectroscopy analysis were conducted to explore the properties of the collagen. Lastly, it tried to improve the functional properties of the collagen using chemical modification technique for future applications. Results and conclusions. Cold acetone treatment made it possible to easily remove the fats and pigments from skins. The odorless and pure-white collagen was obtained with high-yield. The α3 chain did not exist in the collagen. Sakhalin taimen skin collagen had rich α-helix and low β-sheet structures. Succinylation caused the secondary structural changes of the collagen molecule. Moreover, succinylation made it possible not only to increase the viscosity of collagen solution and but also to improve the solubility of collagen in the physiological conditions around pH=6. Novelty and scientific contribution. This finding was the first report on the absence of the α3 chain in Salmonid fish skin collagens. The succinylated collagen from Sakhalin taimen skins as useful biomass has potential to utilize in foods, cosmetics, and its related industries.


2020 ◽  
Vol 13 (5) ◽  
pp. 42-61
Author(s):  
A. K. Gulevsky ◽  

This review presents the current scientific literature data about structure, properties, and functions of collagen, which is known as one of the most abundant human and animal proteins. The building of collagen molecule from the primary structure to submolecular formations, the main stages of its synthesis and biodegradation are briefly described. The information about collagen diversity, its features and metabolic ways in various tissues, including skin, tendons, bones, etc. is presented. The problems of pathologies caused by collagen synthesis and breakdown disorders as well as age-related changes in collagen properties and their causes are discussed. A comparative analysis of the advantages and disadvantages of collagen and its derivatives obtaining from various sources (animals, marine, and recombinant) is given. The most productive methods for collagen extraction from various tissues are shown. The concept of collagen hydrolysis conditions influence on the physicochemical properties and biological activity of the obtained products is described. The applications of collagen and its products in various fields of industrial activity, such as pharmaceutical, cosmetic industry and medicine, are discussed. Further prospective directions of fundamental and applied investigations in this area of research are outlined.


2020 ◽  
Vol 11 (3) ◽  
pp. 61
Author(s):  
Hiroshi Matsui ◽  
Yasumitsu Matsuo

Collagen films with proton conduction are a candidate of next generation of fuel-cell electrolyte. To clarify a relation between proton conductivity and formation of water networks in the collagen film originating from a tilapia’s scale, we systematically measured the ac conductivity, infrared absorption spectrum, and weight change as a function of relative humidity (RH) at room temperature. The integrated absorbance concerning an O–H stretching mode of water molecules increases above 60% RH in accordance with the weight change. The dc conductivity varies in the vicinity of 60 and 83% RH. From those results, we have determined the dc conductivity vs. hydration number (N) per unit (Gly-X-Y). The proton conduction is negligible in the collagen molecule itself, but dominated by the hydration shell, the development of which is characterized with three regions. For 0 < N < 2, the conductivity is extremely small, because the water molecule in the primary hydration shell has a little hydrogen bonded with each other. For 2 < N < 4, a quasi-one-dimensional proton conduction occurs through intra-water bridges in the helix. For 4 < N, the water molecule fills the helix, and inter-water bridges are formed in between the adjacent helices, so that a proton-conducting network is extended three dimensional.


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