File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Second harmonic generation and multiphoton microscopic detection of collagen without the need for species specific antibodies

TitleSecond harmonic generation and multiphoton microscopic detection of collagen without the need for species specific antibodies
Authors
Issue Date2011
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/burns
Citation
Burns, 2011, v. 37 n. 6, p. 1001-1009 How to Cite?
AbstractHigh-resolution, high-contrast, three-dimensional images of live cell and tissue architecture can be obtained using second harmonic generation (SHG), which comprises non-absorptive frequency changes in an excitation laser line. SHG does not require any exogenous antibody or fluorophore labeling, and can generate images from unstained sections of several key endogenous biomolecules, in a wide variety of species and from different types of processed tissue. Here, we examined normal control human skin sections and human burn scar tissues using SHG on a multi-photon microscope (MPM). Examination and comparison of normal human skin and burn scar tissue demonstrated a clear arrangement of fibers in the dermis, similar to dermal collagen fiber signals. Fluorescence-staining confirmed the MPM-SHG collagen colocalization with antibody staining for dermal collagen type-I but not fibronectin or elastin. Furthermore, we were able to detect collagen MPM-SHG signal in human frozen sections as well as in unstained paraffin embedded tissue sections that were then compared with hematoxylin and eosin staining in the identical sections. This same approach was also successful in localizing collagen in porcine and ovine skin samples, and may be particularly important when species-specific antibodies may not be available. Collectively, our results demonstrate that MPM SHG-detection is a useful tool for high resolution examination of collagen architecture in both normal and wounded human, porcine and ovine dermal tissue. © 2011 Published by Elsevier Ltd and ISBI. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/170457
ISSN
2015 Impact Factor: 1.904
2015 SCImago Journal Rankings: 0.895
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChen, ACHen_US
dc.contributor.authorMcneilly, Cen_US
dc.contributor.authorLiu, APYen_US
dc.contributor.authorFlaim, CJen_US
dc.contributor.authorCuttle, Len_US
dc.contributor.authorKendall, Men_US
dc.contributor.authorKimble, RMen_US
dc.contributor.authorShimizu, Hen_US
dc.contributor.authorMcmillan, JRen_US
dc.date.accessioned2012-10-30T06:09:05Z-
dc.date.available2012-10-30T06:09:05Z-
dc.date.issued2011en_US
dc.identifier.citationBurns, 2011, v. 37 n. 6, p. 1001-1009en_US
dc.identifier.issn0305-4179en_US
dc.identifier.urihttp://hdl.handle.net/10722/170457-
dc.description.abstractHigh-resolution, high-contrast, three-dimensional images of live cell and tissue architecture can be obtained using second harmonic generation (SHG), which comprises non-absorptive frequency changes in an excitation laser line. SHG does not require any exogenous antibody or fluorophore labeling, and can generate images from unstained sections of several key endogenous biomolecules, in a wide variety of species and from different types of processed tissue. Here, we examined normal control human skin sections and human burn scar tissues using SHG on a multi-photon microscope (MPM). Examination and comparison of normal human skin and burn scar tissue demonstrated a clear arrangement of fibers in the dermis, similar to dermal collagen fiber signals. Fluorescence-staining confirmed the MPM-SHG collagen colocalization with antibody staining for dermal collagen type-I but not fibronectin or elastin. Furthermore, we were able to detect collagen MPM-SHG signal in human frozen sections as well as in unstained paraffin embedded tissue sections that were then compared with hematoxylin and eosin staining in the identical sections. This same approach was also successful in localizing collagen in porcine and ovine skin samples, and may be particularly important when species-specific antibodies may not be available. Collectively, our results demonstrate that MPM SHG-detection is a useful tool for high resolution examination of collagen architecture in both normal and wounded human, porcine and ovine dermal tissue. © 2011 Published by Elsevier Ltd and ISBI. All rights reserved.en_US
dc.languageengen_US
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/burnsen_US
dc.relation.ispartofBurnsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBurns - Pathologyen_US
dc.subject.meshChilden_US
dc.subject.meshCicatrix - Pathologyen_US
dc.subject.meshCollagen Type I - Analysisen_US
dc.subject.meshElastin - Analysisen_US
dc.subject.meshEpidermis - Chemistry - Pathologyen_US
dc.subject.meshFemaleen_US
dc.subject.meshFetusen_US
dc.subject.meshFibronectins - Analysisen_US
dc.subject.meshHumansen_US
dc.subject.meshMicroscopy, Fluorescence, Multiphoton - Methodsen_US
dc.subject.meshSheepen_US
dc.subject.meshSwineen_US
dc.titleSecond harmonic generation and multiphoton microscopic detection of collagen without the need for species specific antibodiesen_US
dc.typeArticleen_US
dc.identifier.emailLiu, APY:apyliu@hku.hken_US
dc.identifier.authorityLiu, APY=rp01357en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.burns.2011.03.013en_US
dc.identifier.pmid21501931-
dc.identifier.scopuseid_2-s2.0-79961226269en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79961226269&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume37en_US
dc.identifier.issue6en_US
dc.identifier.spage1001en_US
dc.identifier.epage1009en_US
dc.identifier.isiWOS:000294512900012-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridChen, ACH=35721611900en_US
dc.identifier.scopusauthoridMcNeilly, C=16043292500en_US
dc.identifier.scopusauthoridLiu, APY=37101892100en_US
dc.identifier.scopusauthoridFlaim, CJ=37101270500en_US
dc.identifier.scopusauthoridCuttle, L=6603414979en_US
dc.identifier.scopusauthoridKendall, M=7201638728en_US
dc.identifier.scopusauthoridKimble, RM=7005778883en_US
dc.identifier.scopusauthoridShimizu, H=34877687700en_US
dc.identifier.scopusauthoridMcMillan, JR=7102040630en_US
dc.identifier.citeulike9183082-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats