ArticlePloS one2016
β-Aminopropionitrile-Induced Reduction in Enzymatic Crosslinking Causes In Vitro Changes in Collagen Morphology and Molecular Composition.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 32 citations in OpenAlex.
- Comparing the expression patterns and differences of LOX and LOXL1 during the development of myodural bridge and ligamentum flavum.Frontiers in cell and developmental biology · 2026Article
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- Minoxidil restores thymic growth in 22q11.2 deletion syndrome by limiting Sox9Journal of human immunity · 2025Article
- Hyperglycemia inhibits AAA expansion: examining the role of lysyl oxidase.American journal of physiology. Heart and circulatory physiology · 2025Article
- Dissecting the influence of cellular senescence on cell mechanics and extracellular matrix formation in vitro.Aging cell · 2023Article
- Lysyl oxidase-like 1 deficiency alters ultrastructural and biomechanical properties of the peripapillary sclera in mice.Matrix biology plus · 2022Article
- Lysyl oxidase promotes renal fibrosis via accelerating collagen cross-link driving by β-arrestin/ERK/STAT3 pathway.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Articular cartilage and osteochondral tissue engineering techniques: Recent advances and challenges.Bioactive materials · 2021Review
- Molecular engineering of piezoelectricity in collagen-mimicking peptide assemblies.Nature communications · 2021Article
- Elevated intracellular copper contributes a unique role to kidney fibrosis by lysyl oxidase mediated matrix crosslinking.Cell death & disease · 2020Article
- Substrate Strain Mitigates Effects of β-Aminopropionitrile-Induced Reduction in Enzymatic Crosslinking.Calcified tissue international · 2019Article
- Effect of Collagen Cross-Link Deficiency on Incorporation of Grafted Bone.Dentistry journal · 2019Article
- Bone quality assessment of osteogenic cell cultures by Raman microscopy.Journal of Raman spectroscopy : JRS · 2019Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Type I collagen morphology can be characterized using fibril D-spacing, a metric which describes the periodicity of repeating bands of gap and overlap regions of collagen molecules arranged into collagen fibrils. This fibrillar structure is stabilized by enzymatic crosslinks initiated by lysyl oxidase (LOX), a step which can be disrupted using β-aminopropionitrile (BAPN). Murine in vivo studies have confirmed effects of BAPN on collagen nanostructure and the objective of this study was to evaluate the mechanism of these effects in vitro by measuring D-spacing, evaluating the ratio of mature to immature crosslinks, and quantifying gene expression of type I collagen and LOX. Osteoblasts were cultured in complete media, and differentiated using ascorbic acid, in the presence or absence of 0.25mM BAPN-fumarate. The matrix produced was imaged using atomic force microscopy (AFM) and 2D Fast Fourier transforms were performed to extract D-spacing from individual fibrils. The experiment was repeated for quantitative reverse transcription polymerase chain reaction (qRT-PCR) and Fourier Transform infrared spectroscopy (FTIR) analyses. The D-spacing distribution of collagen produced in the presence of BAPN was shifted toward higher D-spacing values, indicating BAPN affects the morphology of collagen produced in vitro, supporting aforementioned in vivo experiments. In contrast, no difference in gene expression was found for any target gene, suggesting LOX inhibition does not upregulate the LOX gene to compensate for the reduction in aldehyde formation, or regulate expression of genes encoding type I collagen. Finally, the mature to immature crosslink ratio decreased with BAPN treatment and was linked to a reduction in peak percent area of mature crosslink hydroxylysylpyridinoline (HP). In conclusion, in vitro treatment of osteoblasts with low levels of BAPN did not induce changes in genes encoding LOX or type I collagen, but led to an increase in collagen D-spacing as well as a decrease in mature crosslinks.
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