Structural relationship of lambda-type light chains with AL amyloidosis
Copyright 1999 Academic Press.
| Veröffentlicht in: | Clinical immunology (Orlando, Fla.). - 1999. - 90(1999), 3 vom: 01. März, Seite 399-403 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
1999
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| Zugriff auf das übergeordnete Werk: | Clinical immunology (Orlando, Fla.) |
| Schlagworte: | Comparative Study Journal Article Research Support, Non-U.S. Gov't Immunoglobulin Light Chains Immunoglobulin Variable Region Bence Jones Protein 9006-99-9 |
| Zusammenfassung: | Copyright 1999 Academic Press. Three human amyloidogenic Bence Jones proteins, NIG76 VlambdaII, NIG204 VlambdaI, and NIG250 VlambdaV, were characterized. In a comparative study, three amino acids, Ser-25a, Thr-68, and Val-95, were found to be common to amyloidogenic proteins of the VlambdaII subgroup. NIG204 had an insertion of Pro residue following position 30 (30a). Proteins having an insertion at this position are invariantly amyloidogenic. NIG250 had a characteristic VlambdaV VL domain, with Mcg+ and KERN+ CL domain isotypes. Following the protein DEL, this is the second example of this subgroup. No common residue is found in the other subgroup proteins but unique substitutions do occur. It would seem that any substitution that causes an alteration in the protein conformation may lead to its being more prone to association with the amyloid processes |
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| Beschreibung: | Date Completed 13.04.1999 Date Revised 15.11.2006 published: Print Citation Status MEDLINE |
| ISSN: | 1521-7035 |