I‐branching N‐acetylglucosaminyltransferase regulates prostate cancer invasiveness by enhancing α5β1 integrin signaling

• Published in: Cancer science Vol. 107; no. 3; pp. 359 - 368
• Main Authors: Mikami, Jotaro, Tobisawa, Yuki, Yoneyama, Tohru, Hatakeyama, Shingo, Mori, Kazuyuki, Hashimoto, Yasuhiro, Koie, Takuya, Ohyama, Chikara, Fukuda, Minoru
• Format: Journal Article
• Language: English
• Published: England John Wiley & Sons, Inc 01.03.2016; John Wiley and Sons Inc
• Subjects: AKT protein; Androgens; Antigens; Breast cancer; Carbohydrates; Cell adhesion & migration; Cell growth; Cell Line, Tumor; Cell migration; Cell Movement; Cell surface; Disease-Free Survival; Fibronectin; Fibronectins - metabolism; Gene expression; glycolipid; Glycolipids; Glycoproteins; Humans; Integrin alpha5beta1 - metabolism; Invasiveness; I‐antigen; I‐branching N‐acetylglucosaminyltransferase; Kinases; Male; Medical prognosis; Metastasis; N-Acetylglucosaminyltransferases - physiology; Neoplasm Invasiveness; Original; Paraffin; Phosphatidylinositol 3-Kinases - metabolism; Phosphorylation; Proportional Hazards Models; Prostate cancer; Prostatic Neoplasms - enzymology; Prostatic Neoplasms - mortality; Prostatic Neoplasms - pathology; Proto-Oncogene Proteins c-akt - metabolism; Signal Transduction; Studies; Surgery; Survival analysis; Tumors; United States > US; Japan; glycolipid; I-branching N-acetylglucosaminyltransferase; prostate cancer; I-antigen; Cell migration
• ISSN: 1347-9032; 1349-7006; 1349-7006
• DOI: 10.1111/cas.12859

Cell surface carbohydrates are important for cell migration and invasion of prostate cancer (PCa). Accordingly, the I‐branching N‐acetylglucosaminyltransferase (GCNT2) converts linear i‐antigen to I‐branching glycan, and its expression is associated with breast cancer progression. In the present stu...