Nanoproteomic analysis of ischemia-dependent changes in signaling protein phosphorylation in colorectal normal and cancer tissue
Clinical diagnostic research relies upon the collection of tissue samples, and for those samples to be representative of the in vivo situation. Tissue collection procedures, including post-operative ischemia, can impact the molecular profile of the tissue at the genetic and proteomic level. Understa...
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| Veröffentlicht in: | Journal of translational medicine 2016-01, Vol.14 (6), p.6, Article 6 |
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| creator | Unger, Florian T Lange, Nicole Krüger, Jana Compton, Carolyn Moore, Helen Agrawal, Lokesh Juhl, Hartmut David, Kerstin A |
| description | Clinical diagnostic research relies upon the collection of tissue samples, and for those samples to be representative of the in vivo situation. Tissue collection procedures, including post-operative ischemia, can impact the molecular profile of the tissue at the genetic and proteomic level. Understanding the influence of factors such as ischemia on tissue samples is imperative in order to develop both markers of tissue quality and ultimately accurate diagnostic tests.
Using NanoPro1000 technology, a rapid and highly sensitive immunoassay platform, the phosphorylation status of clinically relevant cancer-related biomarkers in response to ischemia was quantified in tissue samples from 20 patients with primary colorectal cancer. Tumor tissue and adjacent normal tissue samples were collected and subjected to cold ischemia prior to nanoproteomic analysis of AKT, ERK1/2, MEK1/2, and c-MET. Ischemia-induced relative changes in overall phosphorylation and phosphorylation of individual isoforms were calculated and statistical significance determined. Any differences in baseline levels of phosphorylation between tumor tissue and normal tissue were also analyzed.
Changes in overall phosphorylation of the selected proteins in response to ischemia revealed minor variations in both normal and tumor tissue; however, significant changes were identified in the phosphorylation of individual isoforms. In normal tissue post-operative ischemia, phosphorylation was increased in two AKT isoforms, two ERK1/2 isoforms, and one MEK1/2 isoform and decreased in one MEK1/2 isoform and one c-MET isoform. Following ischemia in tumor tissue, one AKT isoform showed decreased phosphorylation and there was an overall increase in unphosphorylated ERK1/2, whereas an increase in the phosphorylation of two MEK1/2 isoforms was observed. There were no changes in c-MET phosphorylation in tumor tissue.
This study provides insight into the influence of post-operative ischemia on tissue sample biology, which may inform the future development of markers of tissue quality and assist in the development of diagnostic tests. |
| doi_str_mv | 10.1186/s12967-015-0752-1 |
| format | Article |
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Using NanoPro1000 technology, a rapid and highly sensitive immunoassay platform, the phosphorylation status of clinically relevant cancer-related biomarkers in response to ischemia was quantified in tissue samples from 20 patients with primary colorectal cancer. Tumor tissue and adjacent normal tissue samples were collected and subjected to cold ischemia prior to nanoproteomic analysis of AKT, ERK1/2, MEK1/2, and c-MET. Ischemia-induced relative changes in overall phosphorylation and phosphorylation of individual isoforms were calculated and statistical significance determined. Any differences in baseline levels of phosphorylation between tumor tissue and normal tissue were also analyzed.
Changes in overall phosphorylation of the selected proteins in response to ischemia revealed minor variations in both normal and tumor tissue; however, significant changes were identified in the phosphorylation of individual isoforms. In normal tissue post-operative ischemia, phosphorylation was increased in two AKT isoforms, two ERK1/2 isoforms, and one MEK1/2 isoform and decreased in one MEK1/2 isoform and one c-MET isoform. Following ischemia in tumor tissue, one AKT isoform showed decreased phosphorylation and there was an overall increase in unphosphorylated ERK1/2, whereas an increase in the phosphorylation of two MEK1/2 isoforms was observed. There were no changes in c-MET phosphorylation in tumor tissue.
This study provides insight into the influence of post-operative ischemia on tissue sample biology, which may inform the future development of markers of tissue quality and assist in the development of diagnostic tests.</description><identifier>ISSN: 1479-5876</identifier><identifier>EISSN: 1479-5876</identifier><identifier>DOI: 10.1186/s12967-015-0752-1</identifier><identifier>PMID: 26742633</identifier><language>eng</language><publisher>England: BioMed Central Ltd</publisher><subject>Biological Assay ; Care and treatment ; Cell Line, Tumor ; Colorectal cancer ; Colorectal Neoplasms - metabolism ; Complications and side effects ; Diagnosis ; ErbB Receptors - metabolism ; Extracellular Signal-Regulated MAP Kinases - metabolism ; Health aspects ; Humans ; Ischemia ; Ischemia - metabolism ; Luminescent Measurements ; Mitogen-Activated Protein Kinase Kinases - metabolism ; Nanotechnology - methods ; Phosphorylation ; Protein Isoforms - metabolism ; Proteins ; Proteomics - methods ; Proto-Oncogene Proteins c-akt - metabolism ; Proto-Oncogene Proteins c-met - metabolism ; Signal Transduction</subject><ispartof>Journal of translational medicine, 2016-01, Vol.14 (6), p.6, Article 6</ispartof><rights>COPYRIGHT 2016 BioMed Central Ltd.</rights><rights>Unger et al. 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c532t-3343ce2fb41ee91d51aa1ee9b19722ee07738d23f36d76d401fdb8cd91f3400a3</citedby><cites>FETCH-LOGICAL-c532t-3343ce2fb41ee91d51aa1ee9b19722ee07738d23f36d76d401fdb8cd91f3400a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4705760/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4705760/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26742633$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Unger, Florian T</creatorcontrib><creatorcontrib>Lange, Nicole</creatorcontrib><creatorcontrib>Krüger, Jana</creatorcontrib><creatorcontrib>Compton, Carolyn</creatorcontrib><creatorcontrib>Moore, Helen</creatorcontrib><creatorcontrib>Agrawal, Lokesh</creatorcontrib><creatorcontrib>Juhl, Hartmut</creatorcontrib><creatorcontrib>David, Kerstin A</creatorcontrib><title>Nanoproteomic analysis of ischemia-dependent changes in signaling protein phosphorylation in colorectal normal and cancer tissue</title><title>Journal of translational medicine</title><addtitle>J Transl Med</addtitle><description>Clinical diagnostic research relies upon the collection of tissue samples, and for those samples to be representative of the in vivo situation. Tissue collection procedures, including post-operative ischemia, can impact the molecular profile of the tissue at the genetic and proteomic level. Understanding the influence of factors such as ischemia on tissue samples is imperative in order to develop both markers of tissue quality and ultimately accurate diagnostic tests.
Using NanoPro1000 technology, a rapid and highly sensitive immunoassay platform, the phosphorylation status of clinically relevant cancer-related biomarkers in response to ischemia was quantified in tissue samples from 20 patients with primary colorectal cancer. Tumor tissue and adjacent normal tissue samples were collected and subjected to cold ischemia prior to nanoproteomic analysis of AKT, ERK1/2, MEK1/2, and c-MET. Ischemia-induced relative changes in overall phosphorylation and phosphorylation of individual isoforms were calculated and statistical significance determined. Any differences in baseline levels of phosphorylation between tumor tissue and normal tissue were also analyzed.
Changes in overall phosphorylation of the selected proteins in response to ischemia revealed minor variations in both normal and tumor tissue; however, significant changes were identified in the phosphorylation of individual isoforms. In normal tissue post-operative ischemia, phosphorylation was increased in two AKT isoforms, two ERK1/2 isoforms, and one MEK1/2 isoform and decreased in one MEK1/2 isoform and one c-MET isoform. Following ischemia in tumor tissue, one AKT isoform showed decreased phosphorylation and there was an overall increase in unphosphorylated ERK1/2, whereas an increase in the phosphorylation of two MEK1/2 isoforms was observed. There were no changes in c-MET phosphorylation in tumor tissue.
This study provides insight into the influence of post-operative ischemia on tissue sample biology, which may inform the future development of markers of tissue quality and assist in the development of diagnostic tests.</description><subject>Biological Assay</subject><subject>Care and treatment</subject><subject>Cell Line, Tumor</subject><subject>Colorectal cancer</subject><subject>Colorectal Neoplasms - metabolism</subject><subject>Complications and side effects</subject><subject>Diagnosis</subject><subject>ErbB Receptors - metabolism</subject><subject>Extracellular Signal-Regulated MAP Kinases - metabolism</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Ischemia</subject><subject>Ischemia - metabolism</subject><subject>Luminescent Measurements</subject><subject>Mitogen-Activated Protein Kinase Kinases - metabolism</subject><subject>Nanotechnology - methods</subject><subject>Phosphorylation</subject><subject>Protein Isoforms - metabolism</subject><subject>Proteins</subject><subject>Proteomics - methods</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>Proto-Oncogene Proteins c-met - metabolism</subject><subject>Signal Transduction</subject><issn>1479-5876</issn><issn>1479-5876</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkk1rFTEUhoMotlZ_gBsJuHEzNZ-TmY1Qil9QdKPrkJuczI1kkjGZK9ydP92Mt5YWJIRzSJ73JTm8CL2k5JLSoX9bKRt71REqO6Ik6-gjdE6FGjs5qP7xvf4MPav1ByFMSDE-RWesV4L1nJ-j319MykvJK-Q5WGySiccaKs4eh2r3MAfTOVggOUgrtnuTJqg4JFzD1NiQJvxX3U6Wfa5tl2M0a8hpg2yOuYBdTcQpl7kVkxy2JlkoeA21HuA5euJNrPDitl6g7x_ef7v-1N18_fj5-uqms5KzteNccAvM7wQFGKmT1Jit29FRMQZAlOKDY9zz3qneCUK92w3WjdRzQYjhF-jdyXc57GZwtn2nmKiXEmZTjjqboB_epLDXU_6lhSJS9aQZvLk1KPnnAeqq5zYhiNEkyIeqaYMGRcjYN_T1CZ1MBB2Sz83Rbri-EpJyOXK2GV7-h2rLtanbnMCHdv5AQE8CW3KtBfzd6ynRWyD0KRC6BUJvgdC0aV7d__ad4l8C-B9f27Rc</recordid><startdate>20160108</startdate><enddate>20160108</enddate><creator>Unger, Florian T</creator><creator>Lange, Nicole</creator><creator>Krüger, Jana</creator><creator>Compton, Carolyn</creator><creator>Moore, Helen</creator><creator>Agrawal, Lokesh</creator><creator>Juhl, Hartmut</creator><creator>David, Kerstin A</creator><general>BioMed Central Ltd</general><general>BioMed Central</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160108</creationdate><title>Nanoproteomic analysis of ischemia-dependent changes in signaling protein phosphorylation in colorectal normal and cancer tissue</title><author>Unger, Florian T ; Lange, Nicole ; Krüger, Jana ; Compton, Carolyn ; Moore, Helen ; Agrawal, Lokesh ; Juhl, Hartmut ; David, Kerstin A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-3343ce2fb41ee91d51aa1ee9b19722ee07738d23f36d76d401fdb8cd91f3400a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Biological Assay</topic><topic>Care and treatment</topic><topic>Cell Line, Tumor</topic><topic>Colorectal cancer</topic><topic>Colorectal Neoplasms - metabolism</topic><topic>Complications and side effects</topic><topic>Diagnosis</topic><topic>ErbB Receptors - metabolism</topic><topic>Extracellular Signal-Regulated MAP Kinases - metabolism</topic><topic>Health aspects</topic><topic>Humans</topic><topic>Ischemia</topic><topic>Ischemia - metabolism</topic><topic>Luminescent Measurements</topic><topic>Mitogen-Activated Protein Kinase Kinases - metabolism</topic><topic>Nanotechnology - methods</topic><topic>Phosphorylation</topic><topic>Protein Isoforms - metabolism</topic><topic>Proteins</topic><topic>Proteomics - methods</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>Proto-Oncogene Proteins c-met - metabolism</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Unger, Florian T</creatorcontrib><creatorcontrib>Lange, Nicole</creatorcontrib><creatorcontrib>Krüger, Jana</creatorcontrib><creatorcontrib>Compton, Carolyn</creatorcontrib><creatorcontrib>Moore, Helen</creatorcontrib><creatorcontrib>Agrawal, Lokesh</creatorcontrib><creatorcontrib>Juhl, Hartmut</creatorcontrib><creatorcontrib>David, Kerstin A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of translational medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Unger, Florian T</au><au>Lange, Nicole</au><au>Krüger, Jana</au><au>Compton, Carolyn</au><au>Moore, Helen</au><au>Agrawal, Lokesh</au><au>Juhl, Hartmut</au><au>David, Kerstin A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nanoproteomic analysis of ischemia-dependent changes in signaling protein phosphorylation in colorectal normal and cancer tissue</atitle><jtitle>Journal of translational medicine</jtitle><addtitle>J Transl Med</addtitle><date>2016-01-08</date><risdate>2016</risdate><volume>14</volume><issue>6</issue><spage>6</spage><pages>6-</pages><artnum>6</artnum><issn>1479-5876</issn><eissn>1479-5876</eissn><abstract>Clinical diagnostic research relies upon the collection of tissue samples, and for those samples to be representative of the in vivo situation. Tissue collection procedures, including post-operative ischemia, can impact the molecular profile of the tissue at the genetic and proteomic level. Understanding the influence of factors such as ischemia on tissue samples is imperative in order to develop both markers of tissue quality and ultimately accurate diagnostic tests.
Using NanoPro1000 technology, a rapid and highly sensitive immunoassay platform, the phosphorylation status of clinically relevant cancer-related biomarkers in response to ischemia was quantified in tissue samples from 20 patients with primary colorectal cancer. Tumor tissue and adjacent normal tissue samples were collected and subjected to cold ischemia prior to nanoproteomic analysis of AKT, ERK1/2, MEK1/2, and c-MET. Ischemia-induced relative changes in overall phosphorylation and phosphorylation of individual isoforms were calculated and statistical significance determined. Any differences in baseline levels of phosphorylation between tumor tissue and normal tissue were also analyzed.
Changes in overall phosphorylation of the selected proteins in response to ischemia revealed minor variations in both normal and tumor tissue; however, significant changes were identified in the phosphorylation of individual isoforms. In normal tissue post-operative ischemia, phosphorylation was increased in two AKT isoforms, two ERK1/2 isoforms, and one MEK1/2 isoform and decreased in one MEK1/2 isoform and one c-MET isoform. Following ischemia in tumor tissue, one AKT isoform showed decreased phosphorylation and there was an overall increase in unphosphorylated ERK1/2, whereas an increase in the phosphorylation of two MEK1/2 isoforms was observed. There were no changes in c-MET phosphorylation in tumor tissue.
This study provides insight into the influence of post-operative ischemia on tissue sample biology, which may inform the future development of markers of tissue quality and assist in the development of diagnostic tests.</abstract><cop>England</cop><pub>BioMed Central Ltd</pub><pmid>26742633</pmid><doi>10.1186/s12967-015-0752-1</doi><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; PubMed Central Open Access; Springer Nature OA Free Journals |
| subjects | Biological Assay Care and treatment Cell Line, Tumor Colorectal cancer Colorectal Neoplasms - metabolism Complications and side effects Diagnosis ErbB Receptors - metabolism Extracellular Signal-Regulated MAP Kinases - metabolism Health aspects Humans Ischemia Ischemia - metabolism Luminescent Measurements Mitogen-Activated Protein Kinase Kinases - metabolism Nanotechnology - methods Phosphorylation Protein Isoforms - metabolism Proteins Proteomics - methods Proto-Oncogene Proteins c-akt - metabolism Proto-Oncogene Proteins c-met - metabolism Signal Transduction |
| title | Nanoproteomic analysis of ischemia-dependent changes in signaling protein phosphorylation in colorectal normal and cancer tissue |
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