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Editor-in-chief
Maria Stella Graziani

Deputy Director
Martina Zaninotto

Associate Editors
Ferruccio Ceriotti
Davide Giavarina
Bruna Lo Sasso
Giampaolo Merlini
Martina Montagnana
Andrea Mosca
Paola Pezzati
Rossella Tomaiuolo
Matteo Vidali

EIC Assistant
Francesco Busardò

International Advisory Board Khosrow Adeli Canada
Sergio Bernardini Italy
Marcello Ciaccio Italy
Eleftherios Diamandis Canada
Philippe Gillery France
Kjell Grankvist Sweden
Hans Jacobs The Netherlands
Eric Kilpatrick UK
Magdalena Krintus Poland
Giuseppe Lippi Italy
Mario Plebani Italy
Sverre Sandberg Norway
Ana-Maria Simundic Croatia
Tommaso Trenti Italy
Cas Weykamp The Netherlands
Maria Willrich USA
Paul Yip Canada


Publisher
Biomedia srl
Via L. Temolo 4, 20126 Milano

Responsible Editor
Giuseppe Agosta

Editorial Secretary
Chiara Riva
Biomedia srl
Via L. Temolo 4, 20126 Milano
Tel. 0245498282
email: biochimica.clinica@sibioc.it

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ISSN print: 0393 – 0564
ISSN digital: 0392- 7091



BC: Articoli scritti da M. Savoia

Revisione e aggiornamento del documento di consenso SIBioC per la ricerca e quantificazione della proteina di Bence Jones
Update of the Italian Society of Clinical Biochemistry (SIBioC) Consensus document on the detection and quantification of the Bence Jones protein
<p>Bence Jones protein (BJP) refers to urine monoclonal free immunoglobulin light chains produced by the clonal expansion of a plasma cell in the bone marrow. BJP is strongly associated with systemic amyloidosis AL, light chain deposition disease, and multiple myeloma; less frequently, BJP may be recognized either in patients with monoclonal gammopathies of uncertain significance (MGUS) and with other plasma cell dyscrasias or in patients with malignant non-Hodgkin&#39;s lymphomas and chronic lymphocytic leukemia. This paper contains updated recommendations for the detection and the measurement of BJP in clinical practice from the Working Group &ldquo;Proteins&rdquo; of the Italian Society of Clinical Biochemistry (SIBioC), with specific indications for improving all the steps of the preanalytical, analytical, and postanalytical phases. The first morning void is the urine sample recommended for BJP detection, while 24-hours urine collection is preferred for BJP quantification. Native urine cannot be used for samples with low or very low content in urine total protein; in these cases, samples should be concentrated by using specific disposables, such as ultrafiltration membranes retaining proteins with molecular weight around 10 kDa. The required degree of concentration may vary according to sensitivity of the electrophoretic method utilized and the protein content of the sample. The detection of BJP may be performed directly by the recommended method agarose gel immunofixation (IFE) with specific polyvalent immunoglobulin antisera IgG-IgA-IgM, total  and  light chains; alternatively, an electrophoretic screening may be acceptable to rule out negative test results. However, positive test results should be confirmed by IFE. Tests based on immunometric methods can be used neither as screening test, nor for the BJP quantification; however, it could be useful for monitoring purposes, provided that the renal function of the patient is preserved. BJP measurement should be performed by the densitometric scanning of the electrophoretic peak corresponding to BJP, and results should be expressed as ratio of the BJP peak percentage to the urine total protein. Test results should be always integrated by standardized interpretative comments included in the laboratory reports.</p>
Biochimica Clinica ; 45(1) 075-086
Documenti SIBioC - SIBioC Documents
 
È tempo di ridefinire gli intervalli di riferimento e terapeutici della cupruria nella malattia di Wilson?
Is it time to redefine cupruria reference and therapeutic intervals in Wilson's Disease?
<p>Wilson&rsquo;s Disease (WD) is an autosomal recessive genetic disease caused by mutations to the copper-transporting gene <em>ATP7B</em>. WD leads to hepatic copper retention with subsequently clinical manifestations in different organs. The biochemical diagnostic approach includes measurement of serum ceruloplasmin levels and 24-hour urinary copper excretion (uCu/24h). WD patients are generally treated with D-penicillamine and cupruria is necessary to confirm the efficacy of maintenance treatment and the patient&#39;s adherence to therapy. A 30-year-old man was diagnosed with WD at the age of 5 and, since then, was treated with D-penicillamine. In this patient the uCu/24h values never fell within the range recommended by International Guidelines, but no clinical or subclinical progressions of the disease were found. The information derived from this single WD patient, monitored by serial clinical and laboratory checks for more than twenty years, may be useful for a better long-term management of WD, although we suggest that multicenter studies to re-define cupruria reference and therapeutic intervals are needed.</p>
Biochimica Clinica ; 44(3) e023-e026
Casi Clinici - Case Report
 
Mieloma multiplo: da plasmocitoma a coinvolgimento multiorgano
Multiple myeloma: from plasmacytoma to multi-organic involvement
<p>Solitary plasmacytoma is a rare form of plasma cell dyscrasia characterized by localized proliferation of neoplastic monoclonal plasmacells. The lesion can originate in bone or in soft tissue, with no or minimal evidence of bone marrow plasmacytosis (&lt;10%) and absence of end-organ damage signs such as hypercalcaemia, renal insufficiency, anaemia, or bone lesions (CRAB). We present a case of solitary bone plasmacytoma (SPB) that rapidly evolved to multiple myeloma (MM). A partial response was obtained within few months of chemotherapy but then the disease rapidly progressed with involvement of liver, kidneys and lungs. Salvage therapy (bendamustine-bortezomib-dexamethasone, 1 cycle) had no effect and the patient died shortly after. Biochemical work up plays a central role in the follow up of MM patients, as recommended by international guidelines. In some cases the disease is so aggressive that early diagnosis and treatment fail to improve the outcome.</p>
Biochimica Clinica ; 44(2) E16-E19
Casi Clinici - Case Report
 
Galectin-3 and Lp(a) plasma concentrations and advanced carotid atherosclerotic plaques: correlation with plaque presence and features
<p>Introduction: atherosclerosis is one of the leading causes of death and morbidity worldwide. It consists in thedevelopment of plaques in the intima media layers of arteries due to lipid accumulation and oxidation, causingmassive inflammation. We aim to better understand the role of Galectin-3 (Gal-3) and Lipoprotein(a) [Lp(a)] aspossible peripheral markers of plaque presence.<br />Methods: Gal-3 and Lp(a) were measured in plasma samples from 99 patients undergoing carotid endarterectomyand 78 healthy controls, by immunometric assays. Plaques were classified histologically, according to the AmericanHeart Association (AHA) guidelines as type Va (fibroatheroma), Vb (mainly calcific) and Vl (complicated lesion).<br />Results: Gal-3 and Lp(a) plasma levels are higher in patients compared to controls [19.8 ng/mL (SD 5.8) vs 14.0ng/mL (3.6)], p&lt;0.0001 and 8.4 mg/dL (IQR 4.0-25.1) vs 4.7 mg/dL (2.4-12.7), p=0.0003, respectively). Analysis ofROC curves confirmed the discriminating power of these markers obtaining an area under the curve of 0.806(p&lt;0.0001) for Gal-3 and 0.657 (p=0.0001) for Lp(a). At multivariate logistic regression, Gal-3 and Lp(a) plasma levelswere associated with plaque presence independently of each other as well as of age, sex, LDL-C levels and previousmyocardial infarction with an odds ratio of 1.22 (95%CI 1.08-1.38, p=0.002) and 1.05 (1.00-1.09, p=0.048)respectively. No differences of Gal-3 and Lp(a) plasma levels were observed among the plaque types.<br />Conclusion: our data showed that Gal-3 and Lp(a) are reliable markers of advanced atherosclerotic plaques. Theabsence of differences among the different lesion types suggests that the increase of Gal-3 and Lp(a) is independentof the specific plaque features.</p>
Biochimica Clinica ; 43(3) 289-295
Contributi Scientifici - Scientific Papers
 
Mieloma multiplo IgD lambda: “switch” isotipico immunoglobulinico dopo trapianto autologo
IgD lambda multiple myeloma: immunoglobulin isotype switch after autologous stem cell transplantation
<p>IgD multiple myeloma (MM) is a rare disease affecting less than 2% of patients with MM, and it is frequently characterized by an aggressive course. It is usually associated with low monoclonal protein levels, so adequate diagnostic procedures have to be performed in order to identify the involved monoclonal component (MC). We present a case of a 38-year-old man with acute kidney disease caused by an IgD lambda MM. Diagnosis was achieved by serum protein electrophoresis and immunofixation with anti IgD and IgE antisera. After autologous stem cell transplantations (ASCT) the patient developed a MC different from the original isotype, followed by an oligoclonal bands (OB) pattern. Recently, the occurrence of MC and OB unrelated to the original clone has been proven to be an important favorable prognostic factor in patients with MM who undergo ASCT. The role of the protein laboratory at diagnosis and during follow up of MM patients is highlighted.</p>
Biochimica Clinica ; 42(1) e01-e04
Casi clinici - Case report
 
Armonizzazione in Medicina di Laboratorio
Harmonization in Laboratory Medicine
F. Ceriotti  |  M. Panteghini  |  A. Tosetto  |  V. Valentini  |  L. Politi  |  R. Rolla  |  T. Guastafierro  |  T. Köken  |  E. Capoluongo  |  C. Mazzaccara  |  V. D'Argenio  |  V. D'Argenio  |  G. Lippi  |  M. Plebani  |  D. Giavarina  |  M. Berardi  |   A survey on sample matrix and preanalytical management in clinical laboratories  |  D. Bozzato  |  G. Messeri  |  M. Zaninotto  |  M. Vidali  |  A. Padoan  |  G. Parigi  |  A. Clerico  |  L. Sciacovelli  |  M. Ciaccio  |  G.L. Salvagno  |  M. Panteghini  |  F. Braga  |  G. Gessoni  |  M. Montagnana  |  N. Doğan  |  M. Barberis  |  M. Barberis  |  A. Marchetti  |  F. Borrillo  |  L. Bonfanti  |  P.M. Ness  |  G. Messeri  |  S. Nannini  |  J. Queraltò  |  M. Zaninotto  |  A. Mosca  |  BM. Henry  |  E. Fiorio  |  L. Crinò  |  M. A. V. Willrich  |  A. Modenese  |  M. Berardi  |  G. Nordera  |  M. Girelli  |  R. Tomaiuolo  |  D. Giavarina  |  R. Dittadi  |  L. Pighi  |  R. Danesi  |  M. Locatelli  |  F. Balboni  |  D. Cosseddu  |  M. Savoia  |  S. Bernardini  |  C. Domenichini  |  M. Lamonaca  |  M. Perrone  |  M. Perrone  |  P. Pradella  |  A. Padoan  |  L. Belloni  |  A. D'Avolio  |  T. Trenti  |  A. Fortunato  |  T. Trenti  | 
Biochimica Clinica ; 39(6) 546-547
Editoriale - Editorial