Anti-Zinc Transporter Protein 8 Antibody Testing Is Not Informative in Routine Prediabetes Screening in Young Patients with Autoimmune Thyroiditis and Celiac Disease

2016 ◽  
Vol 86 (2) ◽  
pp. 100-105 ◽  
Author(s):  
Daniela Larizza ◽  
Mara De Amici ◽  
Catherine Klersy ◽  
Michela Albanesi ◽  
Riccardo Albertini ◽  
...  
2021 ◽  
Vol 35 ◽  
pp. 205873842110087
Author(s):  
Taoufik Ben Houmich ◽  
Brahim Admou

Celiac disease (CD) is characterized by clinical polymorphism, with classic, asymptomatic or oligosymptomatic, and extra-intestinal forms, which may lead to diagnostic delay and exposure to serious complications. CD is a multidisciplinary health concern involving general medicine, pediatric, and adult gastroenterology, among other disciplines. Immunology and pathology laboratories have a fundamental role in diagnosing and monitoring CD. The diagnosis consists of serological testing based on IgA anti-transglutaminase (TG2) antibodies combined with IgA quantification to rule out IgA deficiency, a potential misleading factor of CD diagnosis. Positive TG2 serology should be corroborated by anti-endomysium antibody testing before considering an intestinal biopsy. Owing to multiple differential diagnoses, celiac disease cannot be confirmed based on serological positivity alone, nor on isolated villous atrophy. In children with classical signs or even when asymptomatic, with high levels of CD-linked markers and positive HLA DQ2 and/or DQ8 molecules, the current trend is to confirm the diagnosis on basis of the non-systematic use of the biopsy, which remains obligatory in adults. The main challenge in managing CD is the implementation and compliance with a gluten-free diet (GFD). This explains the key role of the dietitian and the active participation of patients and their families throughout the disease-management process. The presence of the gluten in several forms of medicine requires the sensitization of physicians when prescribing, and particularly when dispensing gluten-containing formulations by pharmacists. This underlines the importance of the contribution of the pharmacist in the care of patients with CD within the framework of close collaboration with physicians and nutritionists.


2019 ◽  
Vol 20 (4) ◽  
pp. 414-420 ◽  
Author(s):  
Marcia Puñales ◽  
Marilia Dornelles Bastos ◽  
Ana Regina L. Ramos ◽  
Raquel Borges Pinto ◽  
Eduardo A. Ott ◽  
...  

2020 ◽  
Vol 32 (5) ◽  
pp. 663-664
Author(s):  
Graziano Barera ◽  
Katia Maruca ◽  
Paola Sgaramella ◽  
Marina Di Stefano ◽  
Stefano Mora

2004 ◽  
Vol 38 (7) ◽  
pp. 613-614 ◽  
Author(s):  
Josef S??kora ◽  
Jana Varva??ovsk?? ◽  
Ren??ta Pomaha??ov?? ◽  
Konrad Siala ◽  
Franti??ek Sto??ick??

2007 ◽  
Vol 292 (1) ◽  
pp. F217-F229 ◽  
Author(s):  
P. Kaler ◽  
R. Prasad

Previously, in our laboratory a 40-kDa zinc transporter protein was purified and functionally reconstituted in proteoliposomes (Kumar R, Prasad R. Biochim Biophys Acta 1419: 23–32, 1999). Furthermore, we now report the identification of Slc39a10 cDNA encoding the 40-kDa zinc transporter protein by isolating a cloned DNA complementary to zinc transporter mRNA. cDNA was constructed from immunoenriched mRNA encoding the zinc transporter. cDNA was inserted into pBR322 using poly(dC)- poly(dG) tailing. Escherichia coli DH5α cells were transformed, and colonies were screened for zinc transporter cDNA by insertional inactivation. Plasmid DNA was purified from the ampicillin-sensitive clones, and the cDNA was sequenced from both strands. A basic local alignment research tool (BLAST) search of cDNA revealed that it belongs to the Slc39 gene family of zinc transporters and was designated as Slc39a10. Zinc transporter protein deduced on the basis of cDNA sequence was named rZip10 and consists of 385 amino acids with 9 predicted transmembrane domains. The Slc39a10 gene was abundantly expressed in both rat and human tissues. Increased extracellular zinc concentration resulted in upregulation of Slc39a10 in LLC-PK1cells expressing rZip10, which was downregulated at higher zinc concentrations. These cells accumulated more zinc than control cells. rZip10-mediated zinc uptake activity was time-, temperature-, and concentration-dependent and saturable which followed Michaelis-Menten kinetics with a Kmof 19.2 μM and Vmaxof 50 pmol·min−1·mg protein−1. This activity was competitively inhibited by cadmium with Kiof 91 μM. rZip10-mediated zinc uptake was inhibited by COOH group-modifying agents such as DCC. Immunofluorescence studies showed that rZip10 localizes to the plasma membrane of LLC-PK1cells.


2016 ◽  
Vol 169 ◽  
pp. 49-54 ◽  
Author(s):  
Norelle R. Reilly ◽  
Benjamin Lebwohl ◽  
Kaziwe Mollazadegan ◽  
Karl Michaëlsson ◽  
Peter H.R. Green ◽  
...  

2001 ◽  
Vol 24 (5) ◽  
pp. 298-302 ◽  
Author(s):  
G. F. Meloni ◽  
P. A. Tomasi ◽  
A. Bertoncelli ◽  
G. Fanciulli ◽  
G. Delitala ◽  
...  

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