Expression of UDP‐N‐acetyl‐α‐D‐galactosamine–polypeptide galNAc N‐acetylgalactosaminyl transferase‐3 in relation to differentiation and prognosis in patients with colorectal carcinoma

Abstract

Neuropeptide Y (NPY), an inhibitory neuropeptide expressed by a moderately dense population of wide‐field amacrine cells in the rat retina, acts through multiple (Y1–y6) G‐protein–coupled receptors. This study determined the cellular localization of Y1 receptors and the synaptic connectivity of Y1 processes in the inner plexiform layer (IPL) of the rat retina. Specific Y1 immunoreactivity was localized to horizontal cell bodies in the distal inner nuclear layer and their processes in the outer plexiform layer. Immunoreactivity was also prominent in cell processes located in strata 2 and 4, and puncta in strata 4 and 5 of the IPL. Double‐label immunohistochemical experiments with calbindin, a horizontal cell marker, confirmed Y1 immunostaining in all horizontal cells. Double‐label immunohistochemical experiments, using antibodies to choline acetyltransferase and vesicular acetylcholine transporter to label cholinergic amacrine cell processes, demonstrated that Y1 immunoreactivity in strata 2 and 4 of the IPL was localized to cholinergic amacrine cell processes. Electron microscopic studies of the inner retina showed that Y1‐immunostained amacrine cell processes and puncta received synaptic inputs from unlabeled amacrine cell processes (65.2%) and bipolar cell axon terminals (34.8%). Y1‐immunoreactive amacrine cell processes most frequently formed synaptic outputs onto unlabeled amacrine cell processes (34.0%) and ganglion cell dendrites (54.1%). NPY immunoreactivity in the rat retina is distributed primarily to strata 1 and 5 of the IPL, and the present findings, thus, suggest that NPY acts in a paracrine manner on Y1 receptors to influence both horizontal and amacrine cells. J. Comp. Neurol. 454:373–382, 2002. © 2002 Wiley‐Liss, Inc.

Integrated assessment by multiple gene expression analysis of quercetin bioactivity on anticancer–related mechanisms in colon cancer cells in vitro

“…GALNT1 is involved in glycosylation. It was recently found that high expression of GALNT1 in colorectal carcinomas is associated with a better prognosis [47]. Two vacuolar ATPases (ATP6V1C1 and ATP6V0B) were also downregulated.…”

Expression of GalNAc-T3 and its relationships with clinicopathological factors in 61 extrahepatic bile duct carcinomas analyzed using stepwise sections—Special reference to its association with lymph node metastases—

“…In the adenocarcinomas of some organs, including the pancreas and gallbladder, the presence of weak expression or diffuse-type GalNAc-T3 expression in EBDCs T Inoue et al localization of GalNAc-T3 was correlated with tumor aggressiveness. [24][25][26][27][28][29] On the other hand, early-stage gastric carcinomas with submucosal invasion tended to show positive (strong or granular) GalNAc-T3 expression, while early-stage undifferentiated gastric carcinomas showing positive GalNAc-T3 expression were associated with significantly higher frequencies of metastatic lymph node involvement. 30 In addition, GalNAc-T3-positive esophageal squamous cell carcinomas exhibited more aggressive behavior.…”

“…Although most previous studies evaluating GalNAc-T3 expression by immunohistochemistry have divided the observed expression patterns into high-intensity (strong, positive) and low-intensity (weak, negative) groups, [24][25][26][27][28]30,31 Miyahara et al 29 divided the GalNAc-T3 expression patterns of gallbladder carcinomas into granular and diffuse types, mostly corresponding to highintensity and low-intensity expression, respectively. We also found that the immunohistochemical staining of GalNAc-T3 in EBDCs showed granulartype and diffuse-type expression patterns, and these features of EBDCs were similar to those reported for gallbladder adenocarcinomas.…”

“…18,24 Colorectal carcinomas showed a lower intensity of GalNAc-T3 expression than normal colorectal epithelium, 24 while breast carcinomas showed a higher intensity than normal breast glandular tissue. 18 Furthermore, in the current study, the diffuse type of GalNAc-T3 expression in EBDCs was associated with positive lymph node metastasis.…”

“…17,18 Furthermore, recent studies have suggested a relationship between GalNAc-T3 expression and the tumor differentiation or progression, including prognosis, of human adenocarcinomas in the colon, lung, stomach, pancreas and gallbladder. [24][25][26][27][28][29][30] Although the GalNAc-T subtypes are usually localized in the Golgi apparatus, their subcellular localization alters following malignant transformation due to reorganization of the Golgi apparatus elements. 8,19,20 Therefore, not only the levels but also the patterns of GalNAc-T3 expression, such as the subcellular distribution, may be associated with the malignant transformation and differentiation of adenocarcinoma cells.…”