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Deposition of kappa and lambda light chains in amyloid filaments of dialysis-related amyloidosis.
J Am Soc Nephrol. 1995 Oct; 6(4):1262-70.JA

Abstract

beta 2-Microglobulin (beta 2m) is considered to be the amyloidogenic precursor in dialysis-related amyloidosis, although the implication of other relevant cofactors in the pathogenesis of this disease has also been hypothesized. It is conceivable that substances found in amyloid deposits might represent something more than simple codeposition, possibly playing a pathogenic role in amyloidogenesis. Along these lines, a detailed analysis of the protein composition of amyloid fibrils purified from synovial material surgically obtained from nine patients on long-term dialysis was carried out. By the use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, several other protein components, in addition to beta 2m, were found. These were characterized by NH2 amino-terminal sequencing and immunoblotting. In fibrils obtained by water extraction, which fulfill the electron microscopy criteria of highly pure amyloid material, polyclonal kappa and lambda light chains were detected with a concentration of 15 micrograms/mL in the water extraction material; the beta 2m concentration was 200 micrograms/mL. Light microscopy immunohistochemistry was performed on samples from five patients. Amyloid deposits reacted with anti-beta 2m, and anti-light (kappa, lambda), chain antibodies. The immunoreaction of amyloid filaments to anti-beta 2m, anti-lambda, and anti-kappa light chain antibodies was also tested by electron microscopy by use of the immunogold staining procedure. Amyloid filaments were labeled by the three antibodies and showed a different intensity of immunostaining apparently related to their different aggregation pattern. These observations demonstrate that polyclonal immunoglobulin light chains (kappa and lambda) are not contaminants but, together with beta 2m, represent a major constituent of amyloid deposits in dialysis-related osteoarticular amyloidosis, thus indicating their possible role in amyloidogenesis.

Authors+Show Affiliations

Renal Unit, Ospedale San Paolo, Milano, Italy.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8589295

Citation

Brancaccio, D, et al. "Deposition of Kappa and Lambda Light Chains in Amyloid Filaments of Dialysis-related Amyloidosis." Journal of the American Society of Nephrology : JASN, vol. 6, no. 4, 1995, pp. 1262-70.
Brancaccio D, Ghiggeri GM, Braidotti P, et al. Deposition of kappa and lambda light chains in amyloid filaments of dialysis-related amyloidosis. J Am Soc Nephrol. 1995;6(4):1262-70.
Brancaccio, D., Ghiggeri, G. M., Braidotti, P., Garberi, A., Gallieni, M., Bellotti, V., Zoni, U., Gusmano, R., & Coggi, G. (1995). Deposition of kappa and lambda light chains in amyloid filaments of dialysis-related amyloidosis. Journal of the American Society of Nephrology : JASN, 6(4), 1262-70.
Brancaccio D, et al. Deposition of Kappa and Lambda Light Chains in Amyloid Filaments of Dialysis-related Amyloidosis. J Am Soc Nephrol. 1995;6(4):1262-70. PubMed PMID: 8589295.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Deposition of kappa and lambda light chains in amyloid filaments of dialysis-related amyloidosis. AU - Brancaccio,D, AU - Ghiggeri,G M, AU - Braidotti,P, AU - Garberi,A, AU - Gallieni,M, AU - Bellotti,V, AU - Zoni,U, AU - Gusmano,R, AU - Coggi,G, PY - 1995/10/1/pubmed PY - 1995/10/1/medline PY - 1995/10/1/entrez SP - 1262 EP - 70 JF - Journal of the American Society of Nephrology : JASN JO - J. Am. Soc. Nephrol. VL - 6 IS - 4 N2 - beta 2-Microglobulin (beta 2m) is considered to be the amyloidogenic precursor in dialysis-related amyloidosis, although the implication of other relevant cofactors in the pathogenesis of this disease has also been hypothesized. It is conceivable that substances found in amyloid deposits might represent something more than simple codeposition, possibly playing a pathogenic role in amyloidogenesis. Along these lines, a detailed analysis of the protein composition of amyloid fibrils purified from synovial material surgically obtained from nine patients on long-term dialysis was carried out. By the use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, several other protein components, in addition to beta 2m, were found. These were characterized by NH2 amino-terminal sequencing and immunoblotting. In fibrils obtained by water extraction, which fulfill the electron microscopy criteria of highly pure amyloid material, polyclonal kappa and lambda light chains were detected with a concentration of 15 micrograms/mL in the water extraction material; the beta 2m concentration was 200 micrograms/mL. Light microscopy immunohistochemistry was performed on samples from five patients. Amyloid deposits reacted with anti-beta 2m, and anti-light (kappa, lambda), chain antibodies. The immunoreaction of amyloid filaments to anti-beta 2m, anti-lambda, and anti-kappa light chain antibodies was also tested by electron microscopy by use of the immunogold staining procedure. Amyloid filaments were labeled by the three antibodies and showed a different intensity of immunostaining apparently related to their different aggregation pattern. These observations demonstrate that polyclonal immunoglobulin light chains (kappa and lambda) are not contaminants but, together with beta 2m, represent a major constituent of amyloid deposits in dialysis-related osteoarticular amyloidosis, thus indicating their possible role in amyloidogenesis. SN - 1046-6673 UR - https://www.unboundmedicine.com/medline/citation/8589295/Deposition_of_kappa_and_lambda_light_chains_in_amyloid_filaments_of_dialysis_related_amyloidosis_ L2 - http://jasn.asnjournals.org/cgi/pmidlookup?view=long&pmid=8589295 DB - PRIME DP - Unbound Medicine ER -