Infrared spectroscopic studies of cells and tissues: triple helix proteins as a potential biomarker for tumors
In this work, the infrared (IR) spectra of living neural cells in suspension, native brain tissue, and native brain tumor tissue were investigated. Methods were developed to overcome the strong IR signal of liquid water so that the signal from the cellular biochemicals could be seen. Measurements co...
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description | In this work, the infrared (IR) spectra of living neural cells in suspension, native brain tissue, and native brain tumor tissue were investigated. Methods were developed to overcome the strong IR signal of liquid water so that the signal from the cellular biochemicals could be seen. Measurements could be performed during surgeries, within minutes after resection. Comparison between normal tissue, different cell lineages in suspension, and tumors allowed preliminary assignments of IR bands to be made. The most dramatic difference between tissues and cells was found to be in weaker IR absorbances usually assigned to the triple helix of collagens. Triple helix domains are common in larger structural proteins, and are typically found in the extracellular matrix (ECM) of tissues. An algorithm to correct offsets and calculate the band heights and positions of these bands was developed, so the variance between identical measurements could be assessed. The initial results indicate the triple helix signal is surprisingly consistent between different individuals, and is altered in tumor tissues. Taken together, these preliminary investigations indicate this triple helix signal may be a reliable biomarker for a tumor-like microenvironment. Thus, this signal has potential to aid in the intra-operational delineation of brain tumor borders. |
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Methods were developed to overcome the strong IR signal of liquid water so that the signal from the cellular biochemicals could be seen. Measurements could be performed during surgeries, within minutes after resection. Comparison between normal tissue, different cell lineages in suspension, and tumors allowed preliminary assignments of IR bands to be made. The most dramatic difference between tissues and cells was found to be in weaker IR absorbances usually assigned to the triple helix of collagens. Triple helix domains are common in larger structural proteins, and are typically found in the extracellular matrix (ECM) of tissues. An algorithm to correct offsets and calculate the band heights and positions of these bands was developed, so the variance between identical measurements could be assessed. The initial results indicate the triple helix signal is surprisingly consistent between different individuals, and is altered in tumor tissues. Taken together, these preliminary investigations indicate this triple helix signal may be a reliable biomarker for a tumor-like microenvironment. Thus, this signal has potential to aid in the intra-operational delineation of brain tumor borders.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0058332</identifier><identifier>PMID: 23526977</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Algorithms ; Analysis ; Animals ; Bands ; Biological markers ; Biology ; Biomarkers ; Biomarkers, Tumor - chemistry ; Biomarkers, Tumor - metabolism ; Brain ; Brain - metabolism ; Brain cancer ; Brain Neoplasms - metabolism ; Brain tumors ; Cell Line ; Cell Line, Tumor ; Chemistry ; Collagen ; Collagen - chemistry ; Collagen - metabolism ; Extracellular matrix ; Extracellular Matrix - metabolism ; Gene expression ; Glioblastoma - metabolism ; Humans ; Infrared spectra ; Infrared spectroscopy ; Medicine ; Meningeal Neoplasms - metabolism ; Meningioma - metabolism ; Mice ; Mice, Nude ; Microscopy ; Models, Molecular ; Neoplasm Proteins - chemistry ; Neoplasm Proteins - metabolism ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Neurosciences ; Neurosurgery ; Offsets ; Physics ; Protein Structure, Secondary ; Proteins ; Rats ; Spectrophotometry, Infrared - methods ; Spectrophotometry, Infrared - statistics & numerical data ; Structural proteins ; Tissues ; Tumor Microenvironment ; Tumors ; Water</subject><ispartof>PloS one, 2013-03, Vol.8 (3), p.e58332-e58332</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Stelling et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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Methods were developed to overcome the strong IR signal of liquid water so that the signal from the cellular biochemicals could be seen. Measurements could be performed during surgeries, within minutes after resection. Comparison between normal tissue, different cell lineages in suspension, and tumors allowed preliminary assignments of IR bands to be made. The most dramatic difference between tissues and cells was found to be in weaker IR absorbances usually assigned to the triple helix of collagens. Triple helix domains are common in larger structural proteins, and are typically found in the extracellular matrix (ECM) of tissues. An algorithm to correct offsets and calculate the band heights and positions of these bands was developed, so the variance between identical measurements could be assessed. The initial results indicate the triple helix signal is surprisingly consistent between different individuals, and is altered in tumor tissues. Taken together, these preliminary investigations indicate this triple helix signal may be a reliable biomarker for a tumor-like microenvironment. Thus, this signal has potential to aid in the intra-operational delineation of brain tumor borders.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23526977</pmid><doi>10.1371/journal.pone.0058332</doi><tpages>e58332</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS); EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
subjects | Algorithms Analysis Animals Bands Biological markers Biology Biomarkers Biomarkers, Tumor - chemistry Biomarkers, Tumor - metabolism Brain Brain - metabolism Brain cancer Brain Neoplasms - metabolism Brain tumors Cell Line Cell Line, Tumor Chemistry Collagen Collagen - chemistry Collagen - metabolism Extracellular matrix Extracellular Matrix - metabolism Gene expression Glioblastoma - metabolism Humans Infrared spectra Infrared spectroscopy Medicine Meningeal Neoplasms - metabolism Meningioma - metabolism Mice Mice, Nude Microscopy Models, Molecular Neoplasm Proteins - chemistry Neoplasm Proteins - metabolism Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism Neurosciences Neurosurgery Offsets Physics Protein Structure, Secondary Proteins Rats Spectrophotometry, Infrared - methods Spectrophotometry, Infrared - statistics & numerical data Structural proteins Tissues Tumor Microenvironment Tumors Water |
title | Infrared spectroscopic studies of cells and tissues: triple helix proteins as a potential biomarker for tumors |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-16T22%3A19%3A03IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Infrared%20spectroscopic%20studies%20of%20cells%20and%20tissues:%20triple%20helix%20proteins%20as%20a%20potential%20biomarker%20for%20tumors&rft.jtitle=PloS%20one&rft.au=Stelling,%20Allison%20L&rft.date=2013-03-20&rft.volume=8&rft.issue=3&rft.spage=e58332&rft.epage=e58332&rft.pages=e58332-e58332&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0058332&rft_dat=%3Cgale_plos_%3EA478193070%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1330889272&rft_id=info:pmid/23526977&rft_galeid=A478193070&rft_doaj_id=oai_doaj_org_article_6c914b4e37984c109138586fac3646a1&rfr_iscdi=true |