Evidence map›Paper›PMID 18567838›Full record

ArticleBlood2008

Biologic and genetic characterization of the novel amyloidogenic lambda light chain-secreting human cell lines, ALMC-1 and ALMC-2.

Bonnie K Arendt, Marina Ramirez-Alvarado, Laura A Sikkink, Jonathan J Keats, Gregory J Ahmann, Angela Dispenzieri, Rafael Fonseca, Rhett P Ketterling, Ryan A Knudson, Erin M Mulvihill and 4 more

Open access · greenAbstract readCase Reports
In one paragraph

Article in Blood, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
  2. The molecular landscape of AL amyloidosis.British journal of haematology · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Stabilization of amyloidogenic immunoglobulin light chains by small molecules.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Role of domain interactions in the aggregation of full-length immunoglobulin light chains.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors at 3 institutions in 1 country.

Bonnie K ArendtDepartment of Immunology, Mayo Clinic, Rochester, MN 55905, USA.
Marina Ramirez-Alvarado
Laura A Sikkink
Jonathan J Keats
Gregory J Ahmann
Angela Dispenzieri
Rafael Fonseca
Rhett P Ketterling
Ryan A Knudson
Erin M Mulvihill
Renee C Tschumper
Xiaosheng Wu
Steven R Zeldenrust
Diane F Jelinek
Mayo Clinic in Arizona · USMayo Clinic · USWinnMed · US

Funding

TISSUE BANK AND CLINICAL/LABORATORY DATABASEP01CA062242 · NCI · MAYO CLINIC ROCHESTER · PI THERNEAU, TERRY M · 1994 to 2009
$12.9M
Mechanisms of Aggregation in Light Chain AmyloidosisR01GM071514 · NIGMS · MAYO CLINIC ROCHESTER · PI RAMIREZ-ALVARADO, MARINA · 2006 to 2014
$2.8M
NCI NIH HHS CA062242NCI NIH HHS P01 CA062242NIGMS NIH HHS GM071514NIGMS NIH HHS R01 GM071514
6 · The paper itself

Abstract

Primary systemic amyloidosis (AL) is a rare monoclonal plasma cell (PC) disorder characterized by the deposition of misfolded immunoglobulin (Ig) light chains (LC) in vital organs throughout the body. To our knowledge, no cell lines have ever been established from AL patients. Here we describe the establishment of the ALMC-1 and ALMC-2 cell lines from an AL patient. Both cell lines exhibit a PC phenotype and display cytokine-dependent growth. Using a comprehensive genetic approach, we established the genetic relationship between the cell lines and the primary patient cells, and we were also able to identify new genetic changes accompanying tumor progression that may explain the natural history of this patient's disease. Importantly, we demonstrate that free lambda LC secreted by both cell lines contained a beta structure and formed amyloid fibrils. Despite absolute Ig LC variable gene sequence identity, the proteins show differences in amyloid formation kinetics that are abolished by the presence of Na(2)SO(4). The formation of amyloid fibrils from these naturally secreting human LC cell lines is unprecedented. Moreover, these cell lines will provide an invaluable tool to better understand AL, from the combined perspectives of amyloidogenic protein structure and amyloid formation, genetics, and cell biology.

Indexed as

Amino Acid SequenceAmyloidAmyloidosisBase SequenceCell LineChromosome AberrationsCytokinesDNA PrimersFemaleGenes, ImmunoglobulinHumansImmunoglobulin lambda-ChainsIn Situ Hybridization, FluorescenceMicroscopy, Electron, TransmissionMiddle AgedModels, MolecularAmyloidCytokinesDNA PrimersImmunoglobulin lambda-Chains

Identifiers

PMID18567838
PMCPMC2518895
OpenAlexW2077274888

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.