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- Publisher Website: 10.1046/j.0902-0055.2001.00094.x
- Scopus: eid_2-s2.0-0036010894
- PMID: 11929562
- WOS: WOS:000175140000012
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Article: Differences in Candida albicans adhesion to intact and denatured type 1 collagen in vitro
Title | Differences in Candida albicans adhesion to intact and denatured type 1 collagen in vitro |
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Authors | |
Keywords | Adhesion Candida albicans Collagen Gelatin |
Issue Date | 2002 |
Publisher | Blackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/OMI |
Citation | Oral Microbiology and Immunology, 2002, v. 17 n. 2, p. 129-131 How to Cite? |
Abstract | An inhibition assay of Candida albicans adhesion to gelatin-immobilized membranes was compared with that to intact type I collagen-immobilized membranes using an arginine-glycine-aspartic acid (RGD) containing peptide. As compared with a protein-free membrane, gelatin and collagen significantly enhanced the adherence of C. albicans. The adhesion of the yeast to gelatin was significantly inhibited by the RGD peptides, but not by arginine-glycine-glutamic acid (RGE) peptides. In contrast, attachment to collagen was not inhibited by RGD peptides. These results suggest that the RGD sequence of gelatin and the integrin-like proteins of yeasts may be involved in adherence. |
Persistent Identifier | http://hdl.handle.net/10722/66220 |
ISSN | 2011 Impact Factor: 2.807 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Makihira, S | en_HK |
dc.contributor.author | Nikawa, H | en_HK |
dc.contributor.author | Tamagami, M | en_HK |
dc.contributor.author | Hamada, T | en_HK |
dc.contributor.author | Samaranayake, LP | en_HK |
dc.date.accessioned | 2010-09-06T05:44:34Z | - |
dc.date.available | 2010-09-06T05:44:34Z | - |
dc.date.issued | 2002 | en_HK |
dc.identifier.citation | Oral Microbiology and Immunology, 2002, v. 17 n. 2, p. 129-131 | en_HK |
dc.identifier.issn | 0902-0055 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/66220 | - |
dc.description.abstract | An inhibition assay of Candida albicans adhesion to gelatin-immobilized membranes was compared with that to intact type I collagen-immobilized membranes using an arginine-glycine-aspartic acid (RGD) containing peptide. As compared with a protein-free membrane, gelatin and collagen significantly enhanced the adherence of C. albicans. The adhesion of the yeast to gelatin was significantly inhibited by the RGD peptides, but not by arginine-glycine-glutamic acid (RGE) peptides. In contrast, attachment to collagen was not inhibited by RGD peptides. These results suggest that the RGD sequence of gelatin and the integrin-like proteins of yeasts may be involved in adherence. | - |
dc.language | eng | en_HK |
dc.publisher | Blackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/OMI | en_HK |
dc.relation.ispartof | Oral Microbiology and Immunology | en_HK |
dc.rights | The definitive version is available at www.blackwell-synergy.com | - |
dc.subject | Adhesion | - |
dc.subject | Candida albicans | - |
dc.subject | Collagen | - |
dc.subject | Gelatin | - |
dc.subject.mesh | Adhesiveness | - |
dc.subject.mesh | Candida albicans - drug effects - physiology | - |
dc.subject.mesh | Collagen Type I - chemistry | - |
dc.subject.mesh | Gelatin - chemistry | - |
dc.subject.mesh | Membranes, Artificial | - |
dc.title | Differences in Candida albicans adhesion to intact and denatured type 1 collagen in vitro | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Samaranayake, LP: lakshman@hku.hk | en_HK |
dc.identifier.authority | Samaranayake, LP=rp00023 | en_HK |
dc.identifier.doi | 10.1046/j.0902-0055.2001.00094.x | - |
dc.identifier.pmid | 11929562 | - |
dc.identifier.scopus | eid_2-s2.0-0036010894 | - |
dc.identifier.hkuros | 66185 | en_HK |
dc.identifier.volume | 17 | - |
dc.identifier.issue | 2 | - |
dc.identifier.spage | 129 | - |
dc.identifier.epage | 131 | - |
dc.identifier.isi | WOS:000175140000012 | - |
dc.publisher.place | Denmark | - |
dc.identifier.issnl | 0902-0055 | - |