Expression of carcinoembryonic antigen (CEA) and nonspecific crossreacting antigen (NCA) in gastrointestinal cancer; the correlation with degree of differentiation. 1993

Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
Department of Surgery II, Nagoya University School of Medicine, Japan.

In spite of its reputation as a tumour marker, little is known about the function of carcinoembryonic antigen (CEA). We examined the mRNA expression of CEA and NCA in 26 gastric and 14 colorectal cancers together with adjacent morphologically normal mucosae. There was no significant difference between the CEA mRNA levels of colorectal cancer and adjacent mucosa, whereas the CEA mRNA levels were significantly elevated in gastric cancer compared with normal gastric mucosa. The expression of NCA, on the other hand, was more cancer-specific and was significantly up-regulated in both gastric and colorectal cancers compared with the corresponding normal mucosae. No correlation was found between the mRNA level and plasma CEA value. No significant up-regulation was recognised in the node positive cancer, cancer with distant metastasis, or the metastatic tissues themselves. Marked diversity in the degree of differentiation in gastric cancer tissues, however, resulted in varied expression of the CEA gene family, compared with the constantly high expression found in colorectal cancer. Further analysis revealed significant up-regulation of NCA in well and moderately differentiated gastric cancers over poorly differentiated cancers, suggesting that NCA might have roles in differentiation.

UI MeSH Term Description Entries
D008562 Membrane Glycoproteins Glycoproteins found on the membrane or surface of cells. Cell Surface Glycoproteins,Surface Glycoproteins,Cell Surface Glycoprotein,Membrane Glycoprotein,Surface Glycoprotein,Glycoprotein, Cell Surface,Glycoprotein, Membrane,Glycoprotein, Surface,Glycoproteins, Cell Surface,Glycoproteins, Membrane,Glycoproteins, Surface,Surface Glycoprotein, Cell,Surface Glycoproteins, Cell
D009367 Neoplasm Staging Methods which attempt to express in replicable terms the extent of the neoplasm in the patient. Cancer Staging,Staging, Neoplasm,Tumor Staging,TNM Classification,TNM Staging,TNM Staging System,Classification, TNM,Classifications, TNM,Staging System, TNM,Staging Systems, TNM,Staging, Cancer,Staging, TNM,Staging, Tumor,System, TNM Staging,Systems, TNM Staging,TNM Classifications,TNM Staging Systems
D012004 Rectal Neoplasms Tumors or cancer of the RECTUM. Cancer of Rectum,Rectal Cancer,Rectal Tumors,Cancer of the Rectum,Neoplasms, Rectal,Rectum Cancer,Rectum Neoplasms,Cancer, Rectal,Cancer, Rectum,Neoplasm, Rectal,Neoplasm, Rectum,Rectal Cancers,Rectal Neoplasm,Rectal Tumor,Rectum Cancers,Rectum Neoplasm,Tumor, Rectal
D002272 Carcinoembryonic Antigen A glycoprotein that is secreted into the luminal surface of the epithelia in the gastrointestinal tract. It is found in the feces and pancreaticobiliary secretions and is used to monitor the response to colon cancer treatment. Antigens, CD66e,CD66e Antigen,Antigen, CD66e,Antigen, Carcinoembryonic,CD66e Antigens
D003110 Colonic Neoplasms Tumors or cancer of the COLON. Cancer of Colon,Colon Adenocarcinoma,Colon Cancer,Cancer of the Colon,Colon Neoplasms,Colonic Cancer,Neoplasms, Colonic,Adenocarcinoma, Colon,Adenocarcinomas, Colon,Cancer, Colon,Cancer, Colonic,Cancers, Colon,Cancers, Colonic,Colon Adenocarcinomas,Colon Cancers,Colon Neoplasm,Colonic Cancers,Colonic Neoplasm,Neoplasm, Colon,Neoplasm, Colonic,Neoplasms, Colon
D005753 Gastric Mucosa Lining of the STOMACH, consisting of an inner EPITHELIUM, a middle LAMINA PROPRIA, and an outer MUSCULARIS MUCOSAE. The surface cells produce MUCUS that protects the stomach from attack by digestive acid and enzymes. When the epithelium invaginates into the LAMINA PROPRIA at various region of the stomach (CARDIA; GASTRIC FUNDUS; and PYLORUS), different tubular gastric glands are formed. These glands consist of cells that secrete mucus, enzymes, HYDROCHLORIC ACID, or hormones. Cardiac Glands,Gastric Glands,Pyloric Glands,Cardiac Gland,Gastric Gland,Gastric Mucosas,Gland, Cardiac,Gland, Gastric,Gland, Pyloric,Glands, Cardiac,Glands, Gastric,Glands, Pyloric,Mucosa, Gastric,Mucosas, Gastric,Pyloric Gland
D005770 Gastrointestinal Neoplasms Tumors or cancer of the GASTROINTESTINAL TRACT, from the MOUTH to the ANAL CANAL. Gastrointestinal Cancer,Cancer of Gastrointestinal Tract,Cancer of the Gastrointestinal Tract,Neoplasms, Gastrointestinal,Cancer, Gastrointestinal,Cancers, Gastrointestinal,Gastrointestinal Cancers,Gastrointestinal Neoplasm,Gastrointestinal Tract Cancer,Gastrointestinal Tract Cancers,Neoplasm, Gastrointestinal
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000951 Antigens, Neoplasm Proteins, glycoprotein, or lipoprotein moieties on surfaces of tumor cells that are usually identified by monoclonal antibodies. Many of these are of either embryonic or viral origin. Neoplasm Antigens,Tumor Antigen,Tumor Antigens,Antigen, Tumor,Antigens, Tumor
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated

Related Publications

Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
January 1989, Archivum immunologiae et therapiae experimentalis,
Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
January 1993, British journal of cancer,
Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
January 1988, Biochemical and biophysical research communications,
Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
October 1976, British journal of cancer,
Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
February 1990, FEBS letters,
Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
November 1983, Cancer,
Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
July 1987, Biochemical and biophysical research communications,
Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
January 1987, Archivum immunologiae et therapiae experimentalis,
Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
March 1985, American journal of clinical pathology,
Y Kodera, and K Isobe, and M Yamauchi, and T Satta, and T Hasegawa, and S Oikawa, and K Kondoh, and S Akiyama, and K Itoh, and I Nakashima
September 1981, Journal of the National Cancer Institute,
Copied contents to your clipboard!