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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

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Via L. Temolo 4, 20126 Milano

Responsible Editor
Giuseppe Agosta

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Chiara Riva
Biomedia srl
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Tel. 0245498282


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

BC: Articoli scritti da A. Paolicchi

Disfibrinogenemia indotta da una catena leggera libera kappa delle immunoglobuline
Ig-free light chains induced dysfibrinogenemia
<p>Despite several pathological conditions are associated with free&nbsp;light chains (FLC) deposition in human tissues, only few cases of human diseases caused by the specific binding&nbsp;activity of monoclonal FLC are described. A 65-year old male patient, with highly abnormal functional coagulation&nbsp;tests and undetectable functional fibrinogen was admitted to the Hematological Clinic of the University Hospital of&nbsp;Pisa. The same tests were within the reference intervals one year before. After excluding a number of causes for&nbsp;abnormal coagulation tests, we focused on potential causes of acquired dysfibrinogenemia. Due to the presence of&nbsp;abnormal values of FLC, we performed an immunofixation: while serum did not show any detectable monoclonal&nbsp;band, the immunofixation of a plasma sample revealed the presence of monoclonal FLC of kappa type co-migrating&nbsp;with fibrinogen. The serum kappa FLC concentrations were much lower than plasma levels, suggesting that the&nbsp;majority of these FLC were bound to fibrinogen, remaining associated to fibrin after clotting. Bone marrow biopsy&nbsp;showed 4% monoclonal plasma cells producing kappa light chains. The patient was diagnosed as affected by a FLC&nbsp;MGUS. After two courses of dexamethasone, the plasma concentration of kappa FLC decreased substantially and&nbsp;most of the coagulation tests normalized. The nature of the interaction between fibrinogen and kappa FLC is currently&nbsp;under investigation to elucidate the mechanism able to inhibit fibrinogen polymerization.</p>
Biochimica Clinica ; 39(5) e16-e18
Casi clinici - Case report
Forme molecolari della y-glutammiltransferasi: caratteristiche e biogenesi
y-Glutamyltransferase (GGT) fractions: characteristics and biogenesis.
<p>Four GGT fractions (b-, m-, s- and f- GGT) have been described in plasma. The aim of this study was to characterize their molecular nature in human plasma and bile. Plasma was obtained from healthy volunteers and primary bile was collected from patients undergoing liver transplant. For each GGT fraction we determined MW, density, sedimentation conditions in centrifugation assays, and the sensitivity to detergent [deoxycholic acid (DOC)] and protease (papain). A partial purification of b-GGT for immunogold analysis was obtained by ultracentrifugation. Plasma b-GGT showed a MW of 2000 kDa and a density between 1.063-1.210 g/mL. Treatment with 1% DOC converted b-GGT into s-GGT fraction, while b-GGT was not sensible to papain treatment. Plasma m-GGT and s-GGT showed a MW of 1000 and 200 kDa, and their densities were between 1.006-1.063 g/mL and 1.063-1.210 g/mL, respectively. Both fractions were unaffected by DOC treatment, while GGT activity was completely recovered in f-GGT peak after their incubation with papain. Plasma f-GGT showed a MW of 70 kDa and a density &gt;1.21 g/mL. In human hepatic bile we identified two peaks showing the same characteristics of plasma b- and f-GGT fractions. Collected data showed that b-GGT is constituted by membrane microvesicles both in bile and plasma, as confirmed by immunogold; m-GGT and s-GGT might be constituted by bile-acid micelles, while f-GGT represents the free-soluble form of the enzyme. The&#160; understanding of the nature and properties of plasma GGT fractions may allow a better clinical utilization of GGT as a clinical biomarker.&#65279;</p>
Biochimica Clinica ; 36(2) 112-120
Contributi Scientifici - Scientific Papers