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Induction in mice of human light-chain-associated amyloidosis.
Am J Pathol. 1992 Mar; 140(3):629-37.AJ

Abstract

Primary (idiopathic) or multiple myeloma-associated amyloidosis is characterized by the deposition in tissue of monoclonal light chains or light-chain fragments (AL amyloidosis). In contrast to other types of amyloidosis, information regarding the pathogenesis of light-chain-related amyloid has heretofore been limited due to the lack of a suitable in vivo model. The authors report the successful experimental induction of human AL amyloid deposits. The repeated injection into mice of Bence Jones proteins obtained from two patients with AL amyloidosis produced the histopathologic lesions characteristic of this disease. Partial dehydration of animals before protein injection resulted in the acceleration of amyloid formation. The human proteins were deposited as amyloid within the mouse renal blood vessel walls and parenchymal tissue, as well as in other organs. The deposits were Congo red-positive, exhibited green birefringence, and had a fibrillar ultrastructure. As evidenced immunohistochemically, the experimentally induced amyloid deposits consisted of the injected human light chains, and in addition, contained mouse amyloid P component (AP); mouse immunoglobulin (Ig) or inflammatory-associated amyloid A protein was not detected. Extraction and characterization of the amyloid deposits found within the mouse kidney revealed the presence of a predominantly intact human light polypeptide chain. Mice injected in identical manner with a non-amyloid-associated Bence Jones protein had no or only rare amyloid deposits. The experimental mouse model provides a means to ascertain the amyloidogenic potential of human monoclonal light chains and to study further the pathogenesis of AL amyloidosis.

Authors+Show Affiliations

Department of Medicine, University of Tennessee Medical Center/Graduate School of Medicine, Knoxville 37920.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

1546744

Citation

Solomon, A, et al. "Induction in Mice of Human Light-chain-associated Amyloidosis." The American Journal of Pathology, vol. 140, no. 3, 1992, pp. 629-37.
Solomon A, Weiss DT, Pepys MB. Induction in mice of human light-chain-associated amyloidosis. Am J Pathol. 1992;140(3):629-37.
Solomon, A., Weiss, D. T., & Pepys, M. B. (1992). Induction in mice of human light-chain-associated amyloidosis. The American Journal of Pathology, 140(3), 629-37.
Solomon A, Weiss DT, Pepys MB. Induction in Mice of Human Light-chain-associated Amyloidosis. Am J Pathol. 1992;140(3):629-37. PubMed PMID: 1546744.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Induction in mice of human light-chain-associated amyloidosis. AU - Solomon,A, AU - Weiss,D T, AU - Pepys,M B, PY - 1992/3/1/pubmed PY - 1992/3/1/medline PY - 1992/3/1/entrez SP - 629 EP - 37 JF - The American journal of pathology JO - Am J Pathol VL - 140 IS - 3 N2 - Primary (idiopathic) or multiple myeloma-associated amyloidosis is characterized by the deposition in tissue of monoclonal light chains or light-chain fragments (AL amyloidosis). In contrast to other types of amyloidosis, information regarding the pathogenesis of light-chain-related amyloid has heretofore been limited due to the lack of a suitable in vivo model. The authors report the successful experimental induction of human AL amyloid deposits. The repeated injection into mice of Bence Jones proteins obtained from two patients with AL amyloidosis produced the histopathologic lesions characteristic of this disease. Partial dehydration of animals before protein injection resulted in the acceleration of amyloid formation. The human proteins were deposited as amyloid within the mouse renal blood vessel walls and parenchymal tissue, as well as in other organs. The deposits were Congo red-positive, exhibited green birefringence, and had a fibrillar ultrastructure. As evidenced immunohistochemically, the experimentally induced amyloid deposits consisted of the injected human light chains, and in addition, contained mouse amyloid P component (AP); mouse immunoglobulin (Ig) or inflammatory-associated amyloid A protein was not detected. Extraction and characterization of the amyloid deposits found within the mouse kidney revealed the presence of a predominantly intact human light polypeptide chain. Mice injected in identical manner with a non-amyloid-associated Bence Jones protein had no or only rare amyloid deposits. The experimental mouse model provides a means to ascertain the amyloidogenic potential of human monoclonal light chains and to study further the pathogenesis of AL amyloidosis. SN - 0002-9440 UR - https://www.unboundmedicine.com/medline/citation/1546744/Induction_in_mice_of_human_light_chain_associated_amyloidosis_ L2 - https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/1546744/ DB - PRIME DP - Unbound Medicine ER -