The effect of a collagen tripeptide fragment (GER) on fibroblast adhesion and spreading depends on properties of an adhesive surface

Иванова, В. П.; Kovaleva, Z. V.; Anokhina, V. V.; Кривченко, А. И.

doi:10.1134/s1990519x13010057

Cited by 6 publications

(3 citation statements)

References 48 publications

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“…Although the mechanism by which the cells sense the collagen molecular direction is not completely clear, some candidates are proposed as triggers of collagen‐induced cell alignment. Exposure of cryptic RGD‐motifs or native GER‐containing motifs in collagen molecules have been reported to guide the cell spreading, indicating that the specific binding sites between collagen molecules and integrin receptors play a key role in controlling the cell behaviors. Integrin molecules mediate the extracellular information into the intracellular cytoskeletal components; the cellular alignment is considered to be induced by the cytoskeletal rearrangement in response to the sensing of extracellular collagen molecular orientation by integrin.…”

Section: Discussionmentioning

confidence: 99%

Quantitative regulation of bone‐mimetic, oriented collagen/apatite matrix structure depends on the degree of osteoblast alignment on oriented collagen substrates

Matsugaki

Isobe

Saku

et al. 2014

J Biomedical Materials Res

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Bone tissue has a specific anisotropic morphology derived from collagen fiber alignment and the related apatite crystal orientation as a bone quality index. However, the precise mechanism of cellular regulation of the crystallographic orientation of apatite has not been clarified. In this study, anisotropic construction of cell-produced mineralized matrix in vitro was established by initiating organized cellular alignment and subsequent oriented bone-like matrix (collagen/apatite) production. The oriented collagen substrates with three anisotropic levels were prepared by a hydrodynamic method. Primary osteoblasts were cultured on the fabricated substrates until mineralized matrix formation is confirmed. Osteoblast alignment was successfully regulated by the level of substrate collagen orientation, with preferential alignment along the direction of the collagen fibers. Notably, both fibrous orientation of newly synthesized collagen matrix and c-axis of produced apatite crystals showed preferential orientation along the cell direction. Because the degree of anisotropy of the deposited apatite crystals showed dependency on the directional distribution of osteoblasts cultured on the oriented collagen substrates, the cell orientation determines the crystallographic anisotropy of produced apatite crystals. To the best of our knowledge, this is the first report demonstrating that bone tissue anisotropy, even the alignment of apatite crystals, is controllable by varying the degree of osteoblast alignment via regulating the level of substrate orientation.

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Section: Discussionmentioning

confidence: 99%

Quantitative regulation of bone‐mimetic, oriented collagen/apatite matrix structure depends on the degree of osteoblast alignment on oriented collagen substrates

Matsugaki

Isobe

Saku

et al. 2014

J Biomedical Materials Res

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“…Peptides or fragments of some of these molecules are capable of cell stimulation that could lead to enhanced cell proliferation or survival. 47 – 49 Also present in the CM 10-50–kDa fraction are small leucine-rich proteoglycans (SLRPs) involved in ECM assembly (e.g., decorin, fibromodulin, and lumican). 50 Proteoglycans (e.g., HSPG2, ESM-1, and SLRPs) can play a role in adhesion, migration, proliferation, and survival through binding and delivery or sequestration of growth factors and interaction with ECM components.…”

Section: Discussionmentioning

confidence: 99%

Two Bioactive Molecular Weight Fractions of a Conditioned Medium Enhance RPE Cell Survival on Age-Related Macular Degeneration and Aged Bruch's Membrane

Sugino

Sun

Springer

et al. 2016

Trans. Vis. Sci. Tech.

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PurposeTo characterize molecular weight fractions of bovine corneal endothelial cell conditioned medium (CM) supporting retinal pigment epithelium (RPE) cell survival on aged and age-related macular degeneration (AMD) Bruch's membrane.MethodsCM was subject to size separation using centrifugal filters. Retentate and filtrate fractions were tested for bioactivity by analyzing RPE survival on submacular Bruch's membrane of aged and AMD donor eyes and behavior on collagen I-coated tissue culture wells. Protein and peptide composition of active fractions was determined by mass spectrometry.ResultsTwo bioactive fractions, 3-kDa filtrate and a 10-50–kDa fraction, were necessary for RPE survival on aged and AMD Bruch's membrane. The 3-kDa filtrate, but not the 10-50–kDa fraction, supported RPE growth on collagen 1‐coated tissue culture plates. Mass spectrometry of the 10-50–kDa fraction identified 175 extracellular proteins, including growth factors and extracellular matrix molecules. Transforming growth factor (TGF)β-2 was identified as unique to active CM. Peptides representing 29 unique proteins were identified in the 3-KDa filtrate.ConclusionsThese results indicate there is a minimum of two bioactive molecules in CM, one found in the 3-kDa filtrate and one in the 10-50–kDa fraction, and that bioactive molecules in both fractions must be present to ensure RPE survival on Bruch's membrane. Mass spectrometry analysis suggested proteins to test in future studies to identify proteins that may contribute to CM bioactivity.Translational RelevanceResults of this study are the first steps in development of an adjunct to cell-based therapy to ensure cell transplant survival and functionality in AMD patients.

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“…(Fu et al, 2015). The collagen tri-peptide fragment GER and its multiple repeats affect the adhesion and spreading of mouse embryonic fibroblasts to different substrates (Ivanova et al, 2012). In addition, a lot of other collagen peptides have also been reported or separated from the collagen hydrolysates, such as DGAR (Sila and Bougatef, 2016), GAOGLOGP (Saiga et al, 2008) and GFOGP (Ichimura et al, 2009).…”

Section: Collagen Hydrolysates and Collagen Peptidesmentioning

confidence: 99%

Potential Health Functions of Collagen Bioactive Peptides: A Review

Chen¹,

Li²,

Huang³

2020

American Journal of Biochemistry and Biotechnology

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Collagen is the most abundant protein in nature and widely exits in animals. However collagen usage is not good enough, which is a waste of natural resources and an environmental burden. Collagen peptides have some special characters and functions. These functions can decide their usage. Therefore producing, discovering and using new functional collagen peptides are promising way to deal with this issue. Collagen peptides are produced by hydrolysing collagen or gelatin via chemical or biochemical methods. Biochemical hydrolysation is more proper to produce functional collagen peptides than chemical hydrolysation. The collagen hydrolysates or peptides have four levels of functions: Nutrition, basic functions, special biological functions and other useful properties. The nutrition is providing amino acids and small peptides. The basic functions are improving the state of connective tissues, such as skin and bone. The special biology functions include antioxidant, antihypertensive and other bioactive benefits. Other useful functions include antifreeze, metal chelation and forming edible film. All these functions decide that they can be used in food as well as other fields. The present work is a compilation of current information on the preparations and functions of collagen peptides. At last, recommendation for the further research of collagen peptides is proposed.

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The effect of a collagen tripeptide fragment (GER) on fibroblast adhesion and spreading depends on properties of an adhesive surface

Cited by 6 publications

References 48 publications

Quantitative regulation of bone‐mimetic, oriented collagen/apatite matrix structure depends on the degree of osteoblast alignment on oriented collagen substrates

Quantitative regulation of bone‐mimetic, oriented collagen/apatite matrix structure depends on the degree of osteoblast alignment on oriented collagen substrates

Two Bioactive Molecular Weight Fractions of a Conditioned Medium Enhance RPE Cell Survival on Age-Related Macular Degeneration and Aged Bruch's Membrane

Potential Health Functions of Collagen Bioactive Peptides: A Review

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