Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P52742 (pT3)
 1,034 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The heterodimeric CD97 protein is a member of the EGF-TM7 family of class II seven-transmembrane (7TM) receptors of 75-90 kDa and structurally related to the secretin receptor family. CD97 is expressed on leucocytes, lymphocytes and in cells of the hematopoietic system. The precise role for CD97 is still unknown. The ubiquitously expressed CD55 (also known as decay accelerating factor, DAF) protects host cells from complement attack. In addition, CD55 is a bacterial/viral receptor and was identified as a ligand for CD97. Employing computer aided UV-laser microdissection CD97 and CD55 were investigated in C-cells of non-neoplastic thyroid specimens (n=3) and in medullary thyroid carcinomas (n=54) by multiplex RT-PCR. Frozen sections of all tissues were investigated by immunohistochemistry. All non-malignant thyroid specimens expressed CD97 mRNA weakly and were devoid of immunoreactive CD97 protein. Transcripts for CD97 were detected in all 54 MTC tissue specimens and CD97 gene activity directly correlated with the histopathological stage of the MTC. CD97 transcriptional activity was high in advanced stages of MTC such as pT3/4. pT1/2 tumors with exclusive intrathyroidal growth revealed weak CD97 expression. CD55 gene expression was significantly lower in normal C-cells than in tumor tissues and all MTC displayed strong and specific CD55 immunostaining. We did not observe a correlation between the expression of CD55 mRNA or protein, respectively, and pTNM classification. In summary, in the present study we have identified CD97 as a novel marker expressed in dedifferentiated neoplastic human thyroid C-cells. CD97 and CD55 may facilitate adhesion of C-cell carcinoma to surrounding surfaces which would result in rapid tumor cell spread.
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PMID:Expression of CD97 and CD55 in human medullary thyroid carcinomas. 1471 4

Protein N-glycosylation is one of the most important post-translational modifications and is involved in many biological processes, with aberrant changes in protein N-glycosylation patterns being closely associated with several diseases, including the progression and spreading of tumours. In light of this, identifying these aberrant protein glycoforms in tumours could be useful for understanding the molecular mechanism of this multifactorial disease, developing specific biomarkers and finding novel therapeutic targets. We investigated the urinary N-glycoproteome of clear cell renal cell carcinoma (ccRCC) patients at different stages (n = 15 at pT1 and n = 15 at pT3), and of non-ccRCC subjects (n = 15), using an N-glyco-FASP-based method. Using label-free nLC-ESI MS/MS, we identified and quantified several N-glycoproteins with altered expression and abnormal changes affecting the occupancy of the glycosylation site in the urine of RCC patients compared to control. In particular, nine of them had a specific trend that was directly related to the stage progression: CD97, COCH and P3IP1 were up-expressed whilst APOB, FINC, CERU, CFAH, HPT and PLTP were down-expressed in ccRCC patients. Overall, these results expand our knowledge related to the role of this post-translational modification in ccRCC and translation of this information into pre-clinical studies could have a significant impact on the discovery of novel biomarkers and therapeutic target in kidney cancer.
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PMID:In-Depth Mapping of the Urinary N-Glycoproteome: Distinct Signatures of ccRCC-related Progression. 3196 43