File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Crescentic nodular glomerulosclerosis secondary to truncated immunoglobulin α heavy chain deposition

TitleCrescentic nodular glomerulosclerosis secondary to truncated immunoglobulin α heavy chain deposition
Authors
Keywordsα heavy chain
glomerulonephropathy
Immunoglobulin
immunoglobulin A
Issue Date1996
PublisherWB Saunders Co. The Journal's web site is located at http://www.elsevier.com/locate/ajkd
Citation
American Journal Of Kidney Diseases, 1996, v. 28 n. 2, p. 283-288 How to Cite?
AbstractNodular glomerulosclerosis secondary to deposition of monoclonal immunoglobulin (Ig) light chains with or without heavy chains is a recognized clinicopathological entity. Recent reports have demonstrated that an identical glomerular lesion may also occur as a result of truncated τ Ig heavy chain deposition. We investigated the nature of Ig deposits in a patient who presented with rapidly progressive renal failure secondary to crescentic nodular glomerulosclerosis. This patient had a relapsing clinical course responsive to treatment with steroid and cyclophosphamide therapy. In this case, both the glomeruli and tubular basement membrane contained granular immune deposits that were reactive to polyclonal antibodies against α but not τ or μ Ig heavy chains and nonreactive to anti-κ and anti-λ light chain reagents. A monoclonal population of plasma cells secreting α and κ chains was present in the patient's marrow despite the finding of a normal percentage of plasma cells. Serum immunoelectrophoresis was normal, but immunofixation demonstrated the presence of a monoclonal α/κ band. Immunoblot under dissociating and nondissociating conditions showed that both the patient's urine and serum contained Ig fragments that comprised dimer or monomer of an abnormally short α Ig heavy chain (approximately 26 kd) with or without associated κ light chain. The identity of the abnormal serum α Ig heavy chain with that of the glomerular Ig deposits was supported by the finding that both were nonreactive against α1 and α2 subclass-specific monoclonal antibodies despite their reactivity to polyclonal antibodies. Because these monoclonal antibodies would react with structural determinants, which differ between α1 and α2 Ig heavy chains but not those common between them, and because the differences in amino acid sequence between the two largely lie in the CH1 and CH2 domains of the α Ig heavy chain, it is hypothesized that the abnormally short α Ig heavy chain produced by plasma cells in this patient contains deleted CH1 and CH2 domains similar to the findings in patients with τ Ig heavy chain deposition disease.
Persistent Identifierhttp://hdl.handle.net/10722/148055
ISSN
2015 Impact Factor: 6.269
2015 SCImago Journal Rankings: 2.313
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCheng, IKPen_HK
dc.contributor.authorHo, SKNen_HK
dc.contributor.authorChan, DTMen_HK
dc.contributor.authorChan, KWen_HK
dc.date.accessioned2012-05-29T06:10:36Z-
dc.date.available2012-05-29T06:10:36Z-
dc.date.issued1996en_HK
dc.identifier.citationAmerican Journal Of Kidney Diseases, 1996, v. 28 n. 2, p. 283-288en_HK
dc.identifier.issn0272-6386en_HK
dc.identifier.urihttp://hdl.handle.net/10722/148055-
dc.description.abstractNodular glomerulosclerosis secondary to deposition of monoclonal immunoglobulin (Ig) light chains with or without heavy chains is a recognized clinicopathological entity. Recent reports have demonstrated that an identical glomerular lesion may also occur as a result of truncated τ Ig heavy chain deposition. We investigated the nature of Ig deposits in a patient who presented with rapidly progressive renal failure secondary to crescentic nodular glomerulosclerosis. This patient had a relapsing clinical course responsive to treatment with steroid and cyclophosphamide therapy. In this case, both the glomeruli and tubular basement membrane contained granular immune deposits that were reactive to polyclonal antibodies against α but not τ or μ Ig heavy chains and nonreactive to anti-κ and anti-λ light chain reagents. A monoclonal population of plasma cells secreting α and κ chains was present in the patient's marrow despite the finding of a normal percentage of plasma cells. Serum immunoelectrophoresis was normal, but immunofixation demonstrated the presence of a monoclonal α/κ band. Immunoblot under dissociating and nondissociating conditions showed that both the patient's urine and serum contained Ig fragments that comprised dimer or monomer of an abnormally short α Ig heavy chain (approximately 26 kd) with or without associated κ light chain. The identity of the abnormal serum α Ig heavy chain with that of the glomerular Ig deposits was supported by the finding that both were nonreactive against α1 and α2 subclass-specific monoclonal antibodies despite their reactivity to polyclonal antibodies. Because these monoclonal antibodies would react with structural determinants, which differ between α1 and α2 Ig heavy chains but not those common between them, and because the differences in amino acid sequence between the two largely lie in the CH1 and CH2 domains of the α Ig heavy chain, it is hypothesized that the abnormally short α Ig heavy chain produced by plasma cells in this patient contains deleted CH1 and CH2 domains similar to the findings in patients with τ Ig heavy chain deposition disease.en_HK
dc.languageengen_US
dc.publisherWB Saunders Co. The Journal's web site is located at http://www.elsevier.com/locate/ajkden_HK
dc.relation.ispartofAmerican Journal of Kidney Diseasesen_HK
dc.subjectα heavy chainen_HK
dc.subjectglomerulonephropathyen_HK
dc.subjectImmunoglobulinen_HK
dc.subjectimmunoglobulin Aen_HK
dc.subject.meshBiopsyen_US
dc.subject.meshCombined Modality Therapyen_US
dc.subject.meshGlomerulonephritis, Iga - Diagnosis - Immunology - Pathology - Therapyen_US
dc.subject.meshHeavy Chain Disease - Diagnosis - Immunology - Pathology - Therapyen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunoglobulin Light Chains - Analysisen_US
dc.subject.meshImmunoglobulin Alpha-Chains - Analysisen_US
dc.subject.meshKidney - Immunology - Pathologyen_US
dc.subject.meshMaleen_US
dc.subject.meshMiddle Ageden_US
dc.subject.meshRecurrenceen_US
dc.titleCrescentic nodular glomerulosclerosis secondary to truncated immunoglobulin α heavy chain depositionen_HK
dc.typeArticleen_HK
dc.identifier.emailChan, DTM:dtmchan@hku.hken_HK
dc.identifier.emailChan, KW:hrmtckw@hku.hken_HK
dc.identifier.authorityChan, DTM=rp00394en_HK
dc.identifier.authorityChan, KW=rp00330en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0272-6386(96)90315-7-
dc.identifier.pmid8768927-
dc.identifier.scopuseid_2-s2.0-0029843823en_HK
dc.identifier.hkuros25764-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0029843823&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume28en_HK
dc.identifier.issue2en_HK
dc.identifier.spage283en_HK
dc.identifier.epage288en_HK
dc.identifier.isiWOS:A1996VA60000019-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridCheng, IKP=7102537483en_HK
dc.identifier.scopusauthoridHo, SKN=36839065300en_HK
dc.identifier.scopusauthoridChan, DTM=7402687700en_HK
dc.identifier.scopusauthoridChan, KW=16444133100en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats