Fluorophores from Aging Human Articular Cartilage
Human articular cartilages of various ages were digested with collagenase, and the fluorescence of the digests was measured as a function of age. At acidic pH, all collagenase-treated fractions were found to contain two main fluorophores with fluorescence maxima at 395 and 385 nm (excitation at 295...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1991-11, Vol.110 (5), p.714-718 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Uchiyama, Akiyoshi Ohishi, Tsuyosi Takahashi, Masaaki Kushida, Kazuhiro Inoue, Tetsuo Fujie, Michio Horiuchi, Kentaro |
| description | Human articular cartilages of various ages were digested with collagenase, and the fluorescence of the digests was measured as a function of age. At acidic pH, all collagenase-treated fractions were found to contain two main fluorophores with fluorescence maxima at 395 and 385 nm (excitation at 295 and 335 nm, respectively). Each fluorophore was isolated from the hydrolysate and its structure was deduced from spectral and chemical data. The 395/295 nm fluorophore was identified as pyridinoline, which is one of the non-reducible cross-linkages in collagen. The 385/335 nm fluorophore was identical to pentosidine, which was isolated from human dura mater and characterized by Sell and Monnier in 1989. Our results showed that the amount of pentosidine per collagen in human articular cartilage increases linearly with age (r = 0.929,p |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a123646 |
| format | Article |
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At acidic pH, all collagenase-treated fractions were found to contain two main fluorophores with fluorescence maxima at 395 and 385 nm (excitation at 295 and 335 nm, respectively). Each fluorophore was isolated from the hydrolysate and its structure was deduced from spectral and chemical data. The 395/295 nm fluorophore was identified as pyridinoline, which is one of the non-reducible cross-linkages in collagen. The 385/335 nm fluorophore was identical to pentosidine, which was isolated from human dura mater and characterized by Sell and Monnier in 1989. Our results showed that the amount of pentosidine per collagen in human articular cartilage increases linearly with age (r = 0.929,p<0.005), while the amount of pyridinoline per collagen remained constant and was not correlated with age (r = 0.20). On the other hand, the amount of pentosidine per pyridinoline increased exponentially during life (r2= 0.839, p<0.05).</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a123646</identifier><identifier>PMID: 1664425</identifier><identifier>CODEN: JOBIAO</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Adult ; Aged ; Aged, 80 and over ; Aging ; Amino Acids - chemistry ; Amino Acids - isolation & purification ; Analytical, structural and metabolic biochemistry ; Arginine - analogs & derivatives ; Arginine - chemistry ; Arginine - isolation & purification ; Biological and medical sciences ; Cartilage, Articular - chemistry ; Cartilage, Articular - enzymology ; Chemical Fractionation ; Child ; Chromatography, High Pressure Liquid ; Cross-Linking Reagents ; Female ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Humans ; Lysine - analogs & derivatives ; Lysine - chemistry ; Lysine - isolation & purification ; Male ; Microbial Collagenase - chemistry ; Middle Aged ; Proteins ; Solubility ; Spectrometry, Fluorescence</subject><ispartof>Journal of biochemistry (Tokyo), 1991-11, Vol.110 (5), p.714-718</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5148051$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1664425$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Uchiyama, Akiyoshi</creatorcontrib><creatorcontrib>Ohishi, Tsuyosi</creatorcontrib><creatorcontrib>Takahashi, Masaaki</creatorcontrib><creatorcontrib>Kushida, Kazuhiro</creatorcontrib><creatorcontrib>Inoue, Tetsuo</creatorcontrib><creatorcontrib>Fujie, Michio</creatorcontrib><creatorcontrib>Horiuchi, Kentaro</creatorcontrib><title>Fluorophores from Aging Human Articular Cartilage</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Human articular cartilages of various ages were digested with collagenase, and the fluorescence of the digests was measured as a function of age. At acidic pH, all collagenase-treated fractions were found to contain two main fluorophores with fluorescence maxima at 395 and 385 nm (excitation at 295 and 335 nm, respectively). Each fluorophore was isolated from the hydrolysate and its structure was deduced from spectral and chemical data. The 395/295 nm fluorophore was identified as pyridinoline, which is one of the non-reducible cross-linkages in collagen. The 385/335 nm fluorophore was identical to pentosidine, which was isolated from human dura mater and characterized by Sell and Monnier in 1989. Our results showed that the amount of pentosidine per collagen in human articular cartilage increases linearly with age (r = 0.929,p<0.005), while the amount of pyridinoline per collagen remained constant and was not correlated with age (r = 0.20). On the other hand, the amount of pentosidine per pyridinoline increased exponentially during life (r2= 0.839, p<0.05).</description><subject>Adult</subject><subject>Aged</subject><subject>Aged, 80 and over</subject><subject>Aging</subject><subject>Amino Acids - chemistry</subject><subject>Amino Acids - isolation & purification</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Arginine - analogs & derivatives</subject><subject>Arginine - chemistry</subject><subject>Arginine - isolation & purification</subject><subject>Biological and medical sciences</subject><subject>Cartilage, Articular - chemistry</subject><subject>Cartilage, Articular - enzymology</subject><subject>Chemical Fractionation</subject><subject>Child</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cross-Linking Reagents</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Humans</subject><subject>Lysine - analogs & derivatives</subject><subject>Lysine - chemistry</subject><subject>Lysine - isolation & purification</subject><subject>Male</subject><subject>Microbial Collagenase - chemistry</subject><subject>Middle Aged</subject><subject>Proteins</subject><subject>Solubility</subject><subject>Spectrometry, Fluorescence</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkFtLw0AQhRdRtF5-gpAH9S11Z6_pYynWClXxBuJLmGw2bWqSrbsN1H9vSktffZoZzseZwyHkGmgf6IDfunXhfL5wrW-wCv1FZua27iMwroQ6ID3QUsVMSTgkPUoZxAMmPk_IaQiLzck4PybHoJQQTPYIjKvWebecO29DVHhXR8NZ2cyiSVtjEw39qjRthT4aYbdWOLPn5KjoHtuL3TwjH-O799Eknj7fP4yG07jkWq9iSISlmUAhNFdSJwaEMRIHBWVaCI5JjiyTGXZBwSAyWmgAmVNl8lzoTPEzcrP1XXr309qwSusyGFtV2FjXhlQzxSDR8l8QFBt0xUEHXu7ANqttni59WaP_TXdldPrVTsdgsCo8NqYMe0yCSKjc2MRbrAwru97L6L9TpbmW6eTzKxWv6k09scf0hf8BPtuB-A</recordid><startdate>19911101</startdate><enddate>19911101</enddate><creator>Uchiyama, Akiyoshi</creator><creator>Ohishi, Tsuyosi</creator><creator>Takahashi, Masaaki</creator><creator>Kushida, Kazuhiro</creator><creator>Inoue, Tetsuo</creator><creator>Fujie, Michio</creator><creator>Horiuchi, Kentaro</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QP</scope><scope>7X8</scope></search><sort><creationdate>19911101</creationdate><title>Fluorophores from Aging Human Articular Cartilage</title><author>Uchiyama, Akiyoshi ; Ohishi, Tsuyosi ; Takahashi, Masaaki ; Kushida, Kazuhiro ; Inoue, Tetsuo ; Fujie, Michio ; Horiuchi, Kentaro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i377t-184e0b4a44736578c14cc5a9f027443a8da2b5ba6511caa20f7115d06cdd47b63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Adult</topic><topic>Aged</topic><topic>Aged, 80 and over</topic><topic>Aging</topic><topic>Amino Acids - chemistry</topic><topic>Amino Acids - isolation & purification</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Arginine - analogs & derivatives</topic><topic>Arginine - chemistry</topic><topic>Arginine - isolation & purification</topic><topic>Biological and medical sciences</topic><topic>Cartilage, Articular - chemistry</topic><topic>Cartilage, Articular - enzymology</topic><topic>Chemical Fractionation</topic><topic>Child</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cross-Linking Reagents</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Humans</topic><topic>Lysine - analogs & derivatives</topic><topic>Lysine - chemistry</topic><topic>Lysine - isolation & purification</topic><topic>Male</topic><topic>Microbial Collagenase - chemistry</topic><topic>Middle Aged</topic><topic>Proteins</topic><topic>Solubility</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Uchiyama, Akiyoshi</creatorcontrib><creatorcontrib>Ohishi, Tsuyosi</creatorcontrib><creatorcontrib>Takahashi, Masaaki</creatorcontrib><creatorcontrib>Kushida, Kazuhiro</creatorcontrib><creatorcontrib>Inoue, Tetsuo</creatorcontrib><creatorcontrib>Fujie, Michio</creatorcontrib><creatorcontrib>Horiuchi, Kentaro</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Uchiyama, Akiyoshi</au><au>Ohishi, Tsuyosi</au><au>Takahashi, Masaaki</au><au>Kushida, Kazuhiro</au><au>Inoue, Tetsuo</au><au>Fujie, Michio</au><au>Horiuchi, Kentaro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fluorophores from Aging Human Articular Cartilage</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1991-11-01</date><risdate>1991</risdate><volume>110</volume><issue>5</issue><spage>714</spage><epage>718</epage><pages>714-718</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><coden>JOBIAO</coden><abstract>Human articular cartilages of various ages were digested with collagenase, and the fluorescence of the digests was measured as a function of age. At acidic pH, all collagenase-treated fractions were found to contain two main fluorophores with fluorescence maxima at 395 and 385 nm (excitation at 295 and 335 nm, respectively). Each fluorophore was isolated from the hydrolysate and its structure was deduced from spectral and chemical data. The 395/295 nm fluorophore was identified as pyridinoline, which is one of the non-reducible cross-linkages in collagen. The 385/335 nm fluorophore was identical to pentosidine, which was isolated from human dura mater and characterized by Sell and Monnier in 1989. Our results showed that the amount of pentosidine per collagen in human articular cartilage increases linearly with age (r = 0.929,p<0.005), while the amount of pyridinoline per collagen remained constant and was not correlated with age (r = 0.20). On the other hand, the amount of pentosidine per pyridinoline increased exponentially during life (r2= 0.839, p<0.05).</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>1664425</pmid><doi>10.1093/oxfordjournals.jbchem.a123646</doi><tpages>5</tpages></addata></record> |
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| subjects | Adult Aged Aged, 80 and over Aging Amino Acids - chemistry Amino Acids - isolation & purification Analytical, structural and metabolic biochemistry Arginine - analogs & derivatives Arginine - chemistry Arginine - isolation & purification Biological and medical sciences Cartilage, Articular - chemistry Cartilage, Articular - enzymology Chemical Fractionation Child Chromatography, High Pressure Liquid Cross-Linking Reagents Female Fundamental and applied biological sciences. Psychology Glycoproteins Humans Lysine - analogs & derivatives Lysine - chemistry Lysine - isolation & purification Male Microbial Collagenase - chemistry Middle Aged Proteins Solubility Spectrometry, Fluorescence |
| title | Fluorophores from Aging Human Articular Cartilage |
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