Coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis
Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-assoc...
Ausführliche Beschreibung
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| Autor*in: |
Fujimoto, N. [verfasserIn] Wada, N. [verfasserIn] Akiyama, M. [verfasserIn] |
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E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Science Ltd ; 2002 |
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Online-Ressource |
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2002 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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In: British journal of dermatology - Oxford : Wiley-Blackwell, 1892, 147(2002), 3, Seite 0 |
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volume:147 ; year:2002 ; number:3 ; pages:0 |
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| DOI / URN: |
10.1046/j.1365-2133.2002.04940.x |
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| 245 | 1 | 0 | |a Coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis |
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| 520 | |a Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-associated systemic amyloidosis (PASA). Methods A double immunofluorescence study of the lesional skin of PASA was undertaken. Amyloid proteins were extracted with distilled water from one case of PASA. Results The double immunofluorescence study showed that anti-λ light chain and anti-β2 microglobulin antibodies mostly reacted with the same area of amyloid deposit. Amyloid deposits from two patients with PASA who had never undergone haemodialysis showed a positive reaction with the antibodies for β2 microglobulin as well as immunoglobulin λ light chain. By the use of immunoblot assay of amyloid fibril proteins, polypeptides immunoreactive with antiγ light chain antibody (29 kDa) and with anti-β2 microglobulin antibody (12 kDa) were detected. Conclusions These results indicate that β2 microglobulin is a component of amyloid fibrils in PASA. | ||
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| 700 | 1 | |a Ishibashi, A. |4 oth | |
| 700 | 1 | |a Miyakawa, S. |4 oth | |
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10.1046/j.1365-2133.2002.04940.x doi (DE-627)NLEJ242122922 DE-627 ger DE-627 rakwb Fujimoto, N. verfasserin aut Coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-associated systemic amyloidosis (PASA). Methods A double immunofluorescence study of the lesional skin of PASA was undertaken. Amyloid proteins were extracted with distilled water from one case of PASA. Results The double immunofluorescence study showed that anti-λ light chain and anti-β2 microglobulin antibodies mostly reacted with the same area of amyloid deposit. Amyloid deposits from two patients with PASA who had never undergone haemodialysis showed a positive reaction with the antibodies for β2 microglobulin as well as immunoglobulin λ light chain. By the use of immunoblot assay of amyloid fibril proteins, polypeptides immunoreactive with antiγ light chain antibody (29 kDa) and with anti-β2 microglobulin antibody (12 kDa) were detected. Conclusions These results indicate that β2 microglobulin is a component of amyloid fibrils in PASA. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amyloid fibril Wada, N. verfasserin aut Akiyama, M. verfasserin aut Tajima, S. oth Ishibashi, A. oth Miyakawa, S. oth In British journal of dermatology Oxford : Wiley-Blackwell, 1892 147(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ24392786X (DE-600)2004086-6 1365-2133 nnns volume:147 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2133.2002.04940.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 147 2002 3 0 |
| spelling |
10.1046/j.1365-2133.2002.04940.x doi (DE-627)NLEJ242122922 DE-627 ger DE-627 rakwb Fujimoto, N. verfasserin aut Coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-associated systemic amyloidosis (PASA). Methods A double immunofluorescence study of the lesional skin of PASA was undertaken. Amyloid proteins were extracted with distilled water from one case of PASA. Results The double immunofluorescence study showed that anti-λ light chain and anti-β2 microglobulin antibodies mostly reacted with the same area of amyloid deposit. Amyloid deposits from two patients with PASA who had never undergone haemodialysis showed a positive reaction with the antibodies for β2 microglobulin as well as immunoglobulin λ light chain. By the use of immunoblot assay of amyloid fibril proteins, polypeptides immunoreactive with antiγ light chain antibody (29 kDa) and with anti-β2 microglobulin antibody (12 kDa) were detected. Conclusions These results indicate that β2 microglobulin is a component of amyloid fibrils in PASA. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amyloid fibril Wada, N. verfasserin aut Akiyama, M. verfasserin aut Tajima, S. oth Ishibashi, A. oth Miyakawa, S. oth In British journal of dermatology Oxford : Wiley-Blackwell, 1892 147(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ24392786X (DE-600)2004086-6 1365-2133 nnns volume:147 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2133.2002.04940.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 147 2002 3 0 |
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10.1046/j.1365-2133.2002.04940.x doi (DE-627)NLEJ242122922 DE-627 ger DE-627 rakwb Fujimoto, N. verfasserin aut Coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-associated systemic amyloidosis (PASA). Methods A double immunofluorescence study of the lesional skin of PASA was undertaken. Amyloid proteins were extracted with distilled water from one case of PASA. Results The double immunofluorescence study showed that anti-λ light chain and anti-β2 microglobulin antibodies mostly reacted with the same area of amyloid deposit. Amyloid deposits from two patients with PASA who had never undergone haemodialysis showed a positive reaction with the antibodies for β2 microglobulin as well as immunoglobulin λ light chain. By the use of immunoblot assay of amyloid fibril proteins, polypeptides immunoreactive with antiγ light chain antibody (29 kDa) and with anti-β2 microglobulin antibody (12 kDa) were detected. Conclusions These results indicate that β2 microglobulin is a component of amyloid fibrils in PASA. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amyloid fibril Wada, N. verfasserin aut Akiyama, M. verfasserin aut Tajima, S. oth Ishibashi, A. oth Miyakawa, S. oth In British journal of dermatology Oxford : Wiley-Blackwell, 1892 147(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ24392786X (DE-600)2004086-6 1365-2133 nnns volume:147 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2133.2002.04940.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 147 2002 3 0 |
| allfieldsGer |
10.1046/j.1365-2133.2002.04940.x doi (DE-627)NLEJ242122922 DE-627 ger DE-627 rakwb Fujimoto, N. verfasserin aut Coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-associated systemic amyloidosis (PASA). Methods A double immunofluorescence study of the lesional skin of PASA was undertaken. Amyloid proteins were extracted with distilled water from one case of PASA. Results The double immunofluorescence study showed that anti-λ light chain and anti-β2 microglobulin antibodies mostly reacted with the same area of amyloid deposit. Amyloid deposits from two patients with PASA who had never undergone haemodialysis showed a positive reaction with the antibodies for β2 microglobulin as well as immunoglobulin λ light chain. By the use of immunoblot assay of amyloid fibril proteins, polypeptides immunoreactive with antiγ light chain antibody (29 kDa) and with anti-β2 microglobulin antibody (12 kDa) were detected. Conclusions These results indicate that β2 microglobulin is a component of amyloid fibrils in PASA. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amyloid fibril Wada, N. verfasserin aut Akiyama, M. verfasserin aut Tajima, S. oth Ishibashi, A. oth Miyakawa, S. oth In British journal of dermatology Oxford : Wiley-Blackwell, 1892 147(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ24392786X (DE-600)2004086-6 1365-2133 nnns volume:147 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2133.2002.04940.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 147 2002 3 0 |
| allfieldsSound |
10.1046/j.1365-2133.2002.04940.x doi (DE-627)NLEJ242122922 DE-627 ger DE-627 rakwb Fujimoto, N. verfasserin aut Coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-associated systemic amyloidosis (PASA). Methods A double immunofluorescence study of the lesional skin of PASA was undertaken. Amyloid proteins were extracted with distilled water from one case of PASA. Results The double immunofluorescence study showed that anti-λ light chain and anti-β2 microglobulin antibodies mostly reacted with the same area of amyloid deposit. Amyloid deposits from two patients with PASA who had never undergone haemodialysis showed a positive reaction with the antibodies for β2 microglobulin as well as immunoglobulin λ light chain. By the use of immunoblot assay of amyloid fibril proteins, polypeptides immunoreactive with antiγ light chain antibody (29 kDa) and with anti-β2 microglobulin antibody (12 kDa) were detected. Conclusions These results indicate that β2 microglobulin is a component of amyloid fibrils in PASA. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amyloid fibril Wada, N. verfasserin aut Akiyama, M. verfasserin aut Tajima, S. oth Ishibashi, A. oth Miyakawa, S. oth In British journal of dermatology Oxford : Wiley-Blackwell, 1892 147(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ24392786X (DE-600)2004086-6 1365-2133 nnns volume:147 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2133.2002.04940.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 147 2002 3 0 |
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coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis |
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Coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis |
| abstract |
Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-associated systemic amyloidosis (PASA). Methods A double immunofluorescence study of the lesional skin of PASA was undertaken. Amyloid proteins were extracted with distilled water from one case of PASA. Results The double immunofluorescence study showed that anti-λ light chain and anti-β2 microglobulin antibodies mostly reacted with the same area of amyloid deposit. Amyloid deposits from two patients with PASA who had never undergone haemodialysis showed a positive reaction with the antibodies for β2 microglobulin as well as immunoglobulin λ light chain. By the use of immunoblot assay of amyloid fibril proteins, polypeptides immunoreactive with antiγ light chain antibody (29 kDa) and with anti-β2 microglobulin antibody (12 kDa) were detected. Conclusions These results indicate that β2 microglobulin is a component of amyloid fibrils in PASA. |
| abstractGer |
Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-associated systemic amyloidosis (PASA). Methods A double immunofluorescence study of the lesional skin of PASA was undertaken. Amyloid proteins were extracted with distilled water from one case of PASA. Results The double immunofluorescence study showed that anti-λ light chain and anti-β2 microglobulin antibodies mostly reacted with the same area of amyloid deposit. Amyloid deposits from two patients with PASA who had never undergone haemodialysis showed a positive reaction with the antibodies for β2 microglobulin as well as immunoglobulin λ light chain. By the use of immunoblot assay of amyloid fibril proteins, polypeptides immunoreactive with antiγ light chain antibody (29 kDa) and with anti-β2 microglobulin antibody (12 kDa) were detected. Conclusions These results indicate that β2 microglobulin is a component of amyloid fibrils in PASA. |
| abstract_unstemmed |
Background Systemic amyloidosis occurs as a result of amyloid deposition in various tissues. The amyloid fibrils in systemic amyloidosis have been reported to originate from immunoglobulin light chains. Objectives We studied the composition of amyloid fibrils from two patients with plasma cell-associated systemic amyloidosis (PASA). Methods A double immunofluorescence study of the lesional skin of PASA was undertaken. Amyloid proteins were extracted with distilled water from one case of PASA. Results The double immunofluorescence study showed that anti-λ light chain and anti-β2 microglobulin antibodies mostly reacted with the same area of amyloid deposit. Amyloid deposits from two patients with PASA who had never undergone haemodialysis showed a positive reaction with the antibodies for β2 microglobulin as well as immunoglobulin λ light chain. By the use of immunoblot assay of amyloid fibril proteins, polypeptides immunoreactive with antiγ light chain antibody (29 kDa) and with anti-β2 microglobulin antibody (12 kDa) were detected. Conclusions These results indicate that β2 microglobulin is a component of amyloid fibrils in PASA. |
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Coexistence of β2 microglobulin and λ light chain in amyloid fibrils of dialysis-unrelated plasma cell dyscrasia-associated systemic amyloidosis |
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Wada, N. Akiyama, M. Tajima, S. Ishibashi, A. Miyakawa, S. |
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