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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 C. Cosma

Determinazione di anticorpi anti SARS-CoV-2 in matrice salivare in individui vaccinati e in pazienti COVID-19
Determination of anti-sars-cov-2 antibodies in salivary samples from vaccinated individuals and COVID-19 patients.
<p>Introduction: Saliva is a promising biological fluid to be used for measuring a number of analytes. Aim of this ppaperis to verify if salivary anti-SARS-CoV-2 antibodies determination could be suitable for monitoring the viral spread andvaccination efficacy during the COVID-19 epidemic.Methods: a total of 69 subjects were enrolled at the Padova University Hospital: 39 COVID-19 patients and 30 health careworkers (HCW), who underwent a complete vaccination cycle with BNT162b2. All subjects collected a salivary sample,using Salivette, (SARSTEDT AG &amp; Co, N&uuml;mbrecht, Germany). For 9 HCW, salivary samples were collected at threedifferent times within the same day. A serum sample was also obtained for all individuals. Salivary COVID-19 N/S1 RBD(sal-IgG) and serum anti-SARS-CoV-2 S-RBD IgG Ab (ser-IgG) were used for determining anti SARS-CoV-2 antibodies.Results: positive sal-IgG were found in 67/69 (97.1%) samples; in serum samples, the positivity for ser-IgG was foundin 68/69 (98.6%). The sal-IgG median levels differed from COVID-19 to vaccinated HCW, being 0,21 kAU/L in patientssamples and 0,8 kAU/L in vaccinated HCV samples (p =0.030). Median levels for ser-IgG in COVID-19 and patientsvaccinated HCW were 121 kBAU/L and 940 kBAU/L (p &lt;0.001) respectively. A statistically significant correlation was foundbetween ser-IgG levels and time post-vaccination in HCW (rho =-0.6292, p &lt;0.001). Sal-IgG levels were not influencedby the daytime of collection (rho =0.148, p=0.373). Passing-Bablok regressions showed that sal-IgG and ser-IgGcomparability was assessable only when ser-IgG values were divided by 1000, showing slope and intercept values of 0.016(95%CI: 0.016-0.078) and 0,221 (95%CI:-0.097 to 0.786), respectively.Conclusions: sal-IgG are detectable both in COVID-19 and in vaccinated individuals and the values are not influencedby the daytime of collection. As expected sal-IgG were much lower than ser-IgG.</p>
Biochimica Clinica ; 47(1) 041-045
Contributi Scientifici - Scientific Paper
 
Glycated albumin is correlated to insulin resistance and β-cell secretory function in subjects at risk of developing diabetes
<p>Insulin resistance and &beta;-cell secretory function represent two main issues in the pathogenesis of type 2 diabetes mellitus (T2DM). Conflicting results have been obtained about the association between glycated albumin (GA) and body mass index (BMI), insulin resistance and &beta;-cell function in diabetic patients. Actually, the relationship (if any) between GA and the markers of glucose homeostasis and insulin resistance in subjects at risk of developing diabetes, has not been completely elucidated yet. Two hundred and one patients undergoing to oral glucose tolerance test (OGTT) were enrolled in the study. Routine laboratory tests, including fasting insulin, were performed at enrollment. GA was measured on plasma-EDTA by quantILab<sup>&reg;</sup> Glycated Albumin (Instrumentation Laboratory, A Werfen Company) on ILab Taurus analyzer. According to the plasma glucose concentration measured after 2 hours of glucose intake (2h- PG), 13 subjects (6.4%) were classified as impaired glucose tolerance (IGT). GA weakly correlated with fasting plasma glucose (FPG) (r=0.21; P=0.002), with HbA1c (r=0.16; P=0.024) but not with 2h-PG (P=0.7). GA, but not HbA1c, was negatively correlated to HOmeostasis Model Assessment for &beta; cell fuction (HOMA-&beta;) (r<sup>2</sup>=0.23; P&lt;0.001), to HOMA for insulin resistence (HOMA-IR) (r<sup>2</sup>=0.15; P&lt;0.0001) and to BMI (r<sup>2</sup>=0.05; P=0.001). In a stepwise multivariate regression analysis including HbA1c, HOMA-&beta;, plasma albumin, BMI, eGFR, age, FPG, and HOMA-IR as predictors of GA, only HbA1c (&beta;-coefficient: 0.04; P=0.038) and HOMA-&beta; (&beta;-coefficient: -0.01; P&lt;0.0001) were able to predict GA levels (r<sup>2</sup>=0.26; P&lt;0.001 for the model). Our results demonstrated that GA was associated to HOMA-&beta; and, to a lesser extent, to HOMA-IR and BMI. The increase of GA values can be explained by the reduction of &beta;-cell secretory function in subjects with no significant increase of FPG and 2h-PG.</p>
Biochimica Clinica ; 42(3) 234-239
Contributi Scientifici - Scientific papers