Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P17931 (galectin-3)
 2,860 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Glycoproteins secreted into plasma from T cells infected with human immunodeficiency virus (HIV) latent infection may provide insight into understanding the host response to HIV infection in vivo. Glycoproteomics, which evaluates the level of the glycoproteome, remains a novel approach to study this host response to HIV. In order to identify human glycoproteins secreted from T cells with latent HIV infection, the medium from cultured HIV replication-competent T cells was compared with the medium from cultured parental A3.01 cells via solid phase extraction of glycopeptides (SPEG) and high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS). Using these methods, 59 human glycoproteins were identified as having significantly different abundance levels between the media from these two cell lines. The relevance of these 59 proteins to HIV infection in vivo was assessed in plasma from HIV+ and HIV- subjects. Comparison between T cell and plasma revealed that six glycoproteins (galectin-3-binding protein, L-selectin, neogenin, adenosine deaminase CECR1, ICOS ligand and phospholipid transfer protein) were significantly elevated in the HIV+ T cells and plasma studies. These findings suggest that the response of T cells harboring latent HIV infection contributed, in part, to the glycoprotein changes in HIV+ plasma. These proteins, once validated, could provide insight into host-HIV interaction.
...
PMID:Glycoproteomic analysis identifies human glycoproteins secreted from HIV latently infected T cells and reveals their presence in HIV+ plasma. 2459 96

Although elevated expression of neogenin-1 has been detected in human gastric cancer tissue, its role in gastric tumorigenesis remains unclear due to the lack of neogenin-1 studies in cancer. Therefore, we demonstrated here the function and regulatory mechanism of neogenin-1 in gastric cancer. Neogenin-1 ablation decreased proliferation and migration of gastric cancer cells, whereas its over-expression reversed these effects. Xenografted analyses using gastric cancer cells displayed statistically significant inhibition of tumor growth by neogenin-1 depletion. Interestingly, galectin-3 interacted with HSF-1 directly, which facilitated nuclear-localization and binding on neogenin-1 promoter to drive its transcription and gastric cancer cell motility. The galectin-3-increased gastric cancer cell motility was down-regulated by HSF-1 depletion. Moreover, the parallel expression patterns of galectin-3 and neogenin-1, as well as those of HSF-1 and neogenin-1, were detected in the malignant tissues of gastric cancer patients. Taken together, high-expression of neogenin-1 promotes gastric cancer proliferation and motility and its expression is regulated by HSF-1 and galectin-3 interaction. In addition, we propose further studies for neogenin-1 and its associated pathways to provide them as a proper target for gastric cancer therapy.
...
PMID:Up-regulation of neogenin-1 increases cell proliferation and motility in gastric cancer. 2493 Apr 99