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A Spatiotemporal analysis using second harmonic generation reveals enhancement of Type I Collagen polymerization by dermatan sulfate glycosaminoglycans

Jha, KK and Sarkar, P and Biswas, R and Bhat, R and Raghunathan, V (2019) A Spatiotemporal analysis using second harmonic generation reveals enhancement of Type I Collagen polymerization by dermatan sulfate glycosaminoglycans. In: Advances in Microscopic Imaging II 2019, 26-27 Jun 2019, Munich, Germany.

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Official URL: https://doi.org/10.1117/12.2526896


Type 1 Collagen is the most abundant member of the family of collagens, which are the dominant proteins constituting the extracellular matrix (ECM) of multicellular organisms. Within tissues, Type 1 collagen exhibits a fibrillar geometry that serves as a mechanical scaffold for cells. The latter remodel the collagen through the secretion of proteoglycans (proteins with long chains of sulfated glycosaminoglycans (GAGs)), both within physiological and pathological contexts. The dermatan sulfate proteoglycans (DS-PGs) are abundantly present within the developing organs and are known to be dysregulated in diseases such as cancer. How DS alters the fibrillar architecture of collagen is however, not well known. Herein, we have used second harmonic generation (SHG) microscopy to dissect the effects of DS GAGs on Type1 Collagen polymerization. We observe that the presence of DS during polymerization enhances the width and number of the fibers, the surface occupancy (which we define as the ability of the collagen matrix to fill a given volume) and the mean SHG signals. We then image polymerizing collagen matrices at temporal intervals: at very early time points (<6 h), the SHG signals in both control and DS-treated polymerizing Type-1 collagen are low and do not show any difference. However, there is a sudden increase in SHG signals 6 h onwards, with a sharper and significantly increased enhancement in the presence of DS. Our results suggest the presence of DS kinetically alters the collagen polymerization leading to significant changes in its eventual architecture. © SPIE-OSA 2019

Item Type: Conference Paper
Publication: Optics InfoBase Conference Papers
Publisher: OSA - The Optical Society
Additional Information: The copyright of this article belongs to OSA - The Optical Society
Keywords: Glycoproteins; Harmonic generation; Nonlinear optics; Polymerization; Scaffolds (biology); Sulfur compounds, Collagen matrices; Extracellular matrices; Glycosaminoglycans; Multicellular organisms; Second harmonic generation microscopies (SHG); Spatiotemporal analysis; Sulfated glycosaminoglycans; Temporal intervals, Collagen
Department/Centre: Division of Biological Sciences > Molecular Reproduction, Development & Genetics
Division of Electrical Sciences > Electrical Communication Engineering
Date Deposited: 07 Apr 2021 10:59
Last Modified: 07 Apr 2021 10:59
URI: http://eprints.iisc.ac.in/id/eprint/65551

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