Protein glycation and in vivo distribution of human lens fluorescence
Mota, M. C. ; Carvalho, P. ; Ramalho, J. S. ; Cardoso, E. ; Gaspar, A. M. ; Abreu, G.
Springer
Published 1994
Springer
Published 1994
| ISSN: |
1573-2630
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|---|---|
| Keywords: |
cataract ; diabetes ; fluorescence ; furosine ; glycation ; Scheimpflug-photography
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| Source: |
Springer Online Journal Archives 1860-2000
|
| Topics: |
Medicine
|
| Notes: |
Abstract Glycated proteins formed by the Maillard reaction were measured by furosine determination in human normal lenses and in senile and diabetic cataracts. Furosine, an hydrolysis product of fructose-lysine adduct formed in the early stages of the Maillard reaction, was measured by high performance liquid chromatography (HPLC). Furosine levels in diabetic cataracts were found to be 3 to 4 times higher than those observed for senile cataracts. The increased glycation levels both in cortex and nucleus were related to the increase of fluorescence determined in vitro by fluorometry and in vivo by Scheimpflug photography. Lens proteins were incubated with glucose and it has been demonstrated that protein glycation occurred parallel with the increase in concentration of fluorescent chromophores that present similar characteristics as those observed in vivo. The results indicate that protein insolubilization seemed to involve preferentially glycated proteins and at least in diabetic cataracts, the process seems to be initiated in the cortical region.
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798296653966344192 |
|---|---|
| autor | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. |
| autorsonst | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. |
| book_url | http://dx.doi.org/10.1007/BF00951795 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM194445771 |
| issn | 1573-2630 |
| journal_name | International ophthalmology |
| materialart | 1 |
| notes | Abstract Glycated proteins formed by the Maillard reaction were measured by furosine determination in human normal lenses and in senile and diabetic cataracts. Furosine, an hydrolysis product of fructose-lysine adduct formed in the early stages of the Maillard reaction, was measured by high performance liquid chromatography (HPLC). Furosine levels in diabetic cataracts were found to be 3 to 4 times higher than those observed for senile cataracts. The increased glycation levels both in cortex and nucleus were related to the increase of fluorescence determined in vitro by fluorometry and in vivo by Scheimpflug photography. Lens proteins were incubated with glucose and it has been demonstrated that protein glycation occurred parallel with the increase in concentration of fluorescent chromophores that present similar characteristics as those observed in vivo. The results indicate that protein insolubilization seemed to involve preferentially glycated proteins and at least in diabetic cataracts, the process seems to be initiated in the cortical region. |
| package_name | Springer |
| publikationsjahr_anzeige | 1994 |
| publikationsjahr_facette | 1994 |
| publikationsjahr_intervall | 8009:1990-1994 |
| publikationsjahr_sort | 1994 |
| publisher | Springer |
| reference | 18 (1994), S. 187-193 |
| schlagwort | cataract diabetes fluorescence furosine glycation Scheimpflug-photography |
| search_space | articles |
| shingle_author_1 | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. |
| shingle_author_2 | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. |
| shingle_author_3 | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. |
| shingle_author_4 | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. |
| shingle_catch_all_1 | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. Protein glycation and in vivo distribution of human lens fluorescence cataract diabetes fluorescence furosine glycation Scheimpflug-photography cataract diabetes fluorescence furosine glycation Scheimpflug-photography Abstract Glycated proteins formed by the Maillard reaction were measured by furosine determination in human normal lenses and in senile and diabetic cataracts. Furosine, an hydrolysis product of fructose-lysine adduct formed in the early stages of the Maillard reaction, was measured by high performance liquid chromatography (HPLC). Furosine levels in diabetic cataracts were found to be 3 to 4 times higher than those observed for senile cataracts. The increased glycation levels both in cortex and nucleus were related to the increase of fluorescence determined in vitro by fluorometry and in vivo by Scheimpflug photography. Lens proteins were incubated with glucose and it has been demonstrated that protein glycation occurred parallel with the increase in concentration of fluorescent chromophores that present similar characteristics as those observed in vivo. The results indicate that protein insolubilization seemed to involve preferentially glycated proteins and at least in diabetic cataracts, the process seems to be initiated in the cortical region. 1573-2630 15732630 Springer |
| shingle_catch_all_2 | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. Protein glycation and in vivo distribution of human lens fluorescence cataract diabetes fluorescence furosine glycation Scheimpflug-photography cataract diabetes fluorescence furosine glycation Scheimpflug-photography Abstract Glycated proteins formed by the Maillard reaction were measured by furosine determination in human normal lenses and in senile and diabetic cataracts. Furosine, an hydrolysis product of fructose-lysine adduct formed in the early stages of the Maillard reaction, was measured by high performance liquid chromatography (HPLC). Furosine levels in diabetic cataracts were found to be 3 to 4 times higher than those observed for senile cataracts. The increased glycation levels both in cortex and nucleus were related to the increase of fluorescence determined in vitro by fluorometry and in vivo by Scheimpflug photography. Lens proteins were incubated with glucose and it has been demonstrated that protein glycation occurred parallel with the increase in concentration of fluorescent chromophores that present similar characteristics as those observed in vivo. The results indicate that protein insolubilization seemed to involve preferentially glycated proteins and at least in diabetic cataracts, the process seems to be initiated in the cortical region. 1573-2630 15732630 Springer |
| shingle_catch_all_3 | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. Protein glycation and in vivo distribution of human lens fluorescence cataract diabetes fluorescence furosine glycation Scheimpflug-photography cataract diabetes fluorescence furosine glycation Scheimpflug-photography Abstract Glycated proteins formed by the Maillard reaction were measured by furosine determination in human normal lenses and in senile and diabetic cataracts. Furosine, an hydrolysis product of fructose-lysine adduct formed in the early stages of the Maillard reaction, was measured by high performance liquid chromatography (HPLC). Furosine levels in diabetic cataracts were found to be 3 to 4 times higher than those observed for senile cataracts. The increased glycation levels both in cortex and nucleus were related to the increase of fluorescence determined in vitro by fluorometry and in vivo by Scheimpflug photography. Lens proteins were incubated with glucose and it has been demonstrated that protein glycation occurred parallel with the increase in concentration of fluorescent chromophores that present similar characteristics as those observed in vivo. The results indicate that protein insolubilization seemed to involve preferentially glycated proteins and at least in diabetic cataracts, the process seems to be initiated in the cortical region. 1573-2630 15732630 Springer |
| shingle_catch_all_4 | Mota, M. C. Carvalho, P. Ramalho, J. S. Cardoso, E. Gaspar, A. M. Abreu, G. Protein glycation and in vivo distribution of human lens fluorescence cataract diabetes fluorescence furosine glycation Scheimpflug-photography cataract diabetes fluorescence furosine glycation Scheimpflug-photography Abstract Glycated proteins formed by the Maillard reaction were measured by furosine determination in human normal lenses and in senile and diabetic cataracts. Furosine, an hydrolysis product of fructose-lysine adduct formed in the early stages of the Maillard reaction, was measured by high performance liquid chromatography (HPLC). Furosine levels in diabetic cataracts were found to be 3 to 4 times higher than those observed for senile cataracts. The increased glycation levels both in cortex and nucleus were related to the increase of fluorescence determined in vitro by fluorometry and in vivo by Scheimpflug photography. Lens proteins were incubated with glucose and it has been demonstrated that protein glycation occurred parallel with the increase in concentration of fluorescent chromophores that present similar characteristics as those observed in vivo. The results indicate that protein insolubilization seemed to involve preferentially glycated proteins and at least in diabetic cataracts, the process seems to be initiated in the cortical region. 1573-2630 15732630 Springer |
| shingle_title_1 | Protein glycation and in vivo distribution of human lens fluorescence |
| shingle_title_2 | Protein glycation and in vivo distribution of human lens fluorescence |
| shingle_title_3 | Protein glycation and in vivo distribution of human lens fluorescence |
| shingle_title_4 | Protein glycation and in vivo distribution of human lens fluorescence |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Springer Online Journal Archives 1860-2000 |
| timestamp | 2024-05-06T09:55:31.938Z |
| titel | Protein glycation and in vivo distribution of human lens fluorescence |
| titel_suche | Protein glycation and in vivo distribution of human lens fluorescence |
| topic | WW-YZ |
| uid | nat_lic_papers_NLM194445771 |