OBJECTIVE: To investigate the regulatory role of α-1, 6-fucosyltransferase (FUT8) in TGF-β1-induced proliferation, migration and fibrosis of human embryonic lung fibroblasts (MRC-5 cells) and explore the underlying molecular mechanism. METHODS: C57/BL6 mice were randomized into 4 groups for treatment with saline (control group), bleomycin, bleomycin+sh-NC or bleomycin+sh-FUT8, and pulmonary fibrosis was observed using Masson staining.MRC-5 cells were transfected with si-NC, FUT8 siRNA (si-FUT8), or both si-FUT8 and a galectin-3(Gal-3) overexpression plasmid (pcDNA3.1-Gal) prior to TGF-β1 treatment, and the changes in cell proliferation and migration were assessed using CCK-8 assay, BrdU assay, and wound healing assay; the changes in the expression levels of α-SMA, collagen I (COLIA1) and extracellular matrix fibronectin (FN) were detected with real-time quantitative PCR (RT-qPCR) and Western blotting.The interaction of FUT8 and Gal-3 was tested using coimmunoprecipitation (Co-IP) assay, and the effect of FUT8 silencing on Gal-3 and FAK/Akt signaling pathways was analyzed. RESULTS: FUT8 knockdown significantly reduced bleomycin-induced extracellular collagen deposition in the lung tissues of the mice.Silencing FUT8 obviously inhibited cell proliferation (P < 0.05) and migration mediated by TGF-β1.FUT8 knockdown down-regulated the mRNA and protein levels of α-SMA, COLIA1 and FN (P < 0.05) in the cells.Coimmunoprecipitation analysis showed that FUT8 interacted with Gal-3.Silencing FUT8 significantly down-regulated Gal-3 expression and inhibited the activation of the FAK/Akt signaling pathway (P < 0.05).Overexpression of Gal-3 obviously reversed the effects of FUT8 silencing on cell proliferation, migration and fibrosis (P < 0.05). CONCLUSION FUT8 regulates TGF-β1-induced proliferation, migration and fibrosis of MRC-5 cells by modulating Gal-3 expression, in which the FAK/Akt pathway may play a role.
Animals ; Bleomycin/metabolism* ; Fibroblasts/metabolism* ; Fibrosis ; Fucosyltransferases/metabolism* ; Galectin 3/genetics* ; Humans ; Lung/metabolism* ; Mice ; Proto-Oncogene Proteins c-akt/metabolism* ; Transforming Growth Factor beta1/metabolism*

BACKGROUNDIt is widely recognized that the diagnosis of parathyroid carcinoma (PC) is often difficult because of the overlap of characteristics between malignant and benign parathyroid tumors, especially at an early stage. Our study aimed to investigate the differential expression of Ki-67, galectin-3, fragile histidine triad (FHIT) gene, and parafibromin in PC, parathyroid adenoma (PA), parathyroid hyperplasia (PH), and normal parathyroid (NP) tissues; then to assess these expression values for use in differential diagnosis of malignant and benign parathyroid tumors.

METHODSData of 15 cases with PC, 19 PAs, and 8 PHs were retrospectively analyzed for their clinical characteristics. The expression of Ki-67, galectin-3, FHIT, and parafibromin were detected via immunohistochemistry in the above-mentioned specimens and 6 NPs as control.

RESULTSComplete loss of parafibromin expression was seen in 9 of 15 (60%) carcinomas, and all normal parathyroid tissues and parathyroid benign tumors stained positive for parafibromin except for one (4%) adenoma. Galectin-3 staining was positive in 11 of 15 (73%) carcinomas, 5 of 19 (26%) adenomas, 1 of 8 (12%) hyperplasias, and 0 of 6 normal tissues. The Ki-67 proliferative index was high in 4 of 15 (27%) carcinomas, 1 of 19 (5%) adenomas, and none of the hyperplasia or normal tissues. FHIT expression did not differ appreciably among the tumor types. The combination of overexpression of galectin-3 or loss of parafibromin increased sensitivity for PC to 87%, while the specificity of both positive galectin-3 and positive Ki-67 could reach 100%.

CONCLUSIONSThese data suggested that loss of parafibromin and overexpression of galectin-3 and Ki-67 might help to distinguish parathyroid carcinoma from other parathyroid tumors. And the combination of two or three of these markers might produce better sensitivity and/or specificity for the diagnosis of parathyroid carcinoma.

Acid Anhydride Hydrolases ; metabolism ; Galectin 3 ; metabolism ; Humans ; Immunohistochemistry ; Ki-67 Antigen ; metabolism ; Neoplasm Proteins ; metabolism ; Parathyroid Neoplasms ; metabolism ; Tumor Suppressor Proteins ; metabolism

OBJECTIVETo study the expression of Galectin-3 and CDC25B mRNA in gastric carcinoma and their correlation with clinical-pathological features and the survival time.

METHODSTissue microarray (TMA) technique and in situ hybridization were used to detect the expression of Galectin-3 and CDC25B mRNA in 220 gastric carcinoma specimens and 31 normal gastric mucosa samples.

RESULTSIn situ hybridization results revealed that from the 220 cases, the positive expression rate of Galectin-3 and CDC25B mRNA were 58.6% and 54.1%, respectively. There was significant relationship between the Galectin-3 mRNA expression and tumor diameter, advanced TNM stage, invasion depth, vessel invasion, lymph node and distant metastasis. There was significant relationship between CDC25B mRNA expression and tumor diameter, advanced TNM stage, vessel invasion, lymph node and distant metastasis. In addition, there was apositive relationship of Galectin-3 and CDC25B mRNA expression. Finally, the mean survival time in cases with Galectin-3 and CDC25B mRNA positive expression was significantly shorter than those without Galectin-3 and CDC25B expression.

CONCLUSIONThe expression of Galectin-3 and CDC25B mRNA appears to act as a promoting factor in the onset and development of gastric cancer. It can be used as a marker of prognosis of gastric carcinoma in clinical practice.

Female ; Galectin 3 ; genetics ; metabolism ; Gene Expression ; genetics ; Gene Expression Regulation, Neoplastic ; Humans ; Male ; Prognosis ; RNA, Messenger ; metabolism ; Stomach Neoplasms ; genetics ; metabolism ; pathology ; cdc25 Phosphatases ; genetics ; metabolism

OBJECTIVETo investigate the association between the expression of galectin- 3 protein and peritoneal metastasis in gastric cancer.

METHODThe expressions of galectin- 3 was detected in matching- samples including primary gastric cancer lesions,lymph node metastases,peritoneal metastases and paratumor normal tissues by immunohistochemistry. All specimens were gained from 35 patients who had synchronous peritoneal metastasis from gastric cancer.

RESULTSThe over- expression of galectin- 3 was observed in 97% (34/35) of the gastric cancer lesions, the peritoneal metastases and the lymph node metastases,whereas in 14% (5/35) of paratumor normal tissues. There were significant differences in the expression of galectin- 3 between paratumor normal tissues and the gastric carcinoma lesions,peritoneal metastases and lymph node metastases (P< 0.05),but there were no significant differences among the gastric cancer lesions,the peritoneal metastases,and the lymph node metastases (P> 0.05).

CONCLUSIONThe expression of galectin- 3 in gastric cancer lesions can be used as a biological marker of peritoneal metastasis from gastric cancer before operation and as a prognostic factor of gastric cancer.

Galectin 3 ; metabolism ; Humans ; Immunohistochemistry ; Lymph Nodes ; metabolism ; pathology ; Lymphatic Metastasis ; Neoplasm Staging ; Peritoneal Neoplasms ; metabolism ; pathology ; secondary ; Stomach Neoplasms ; metabolism ; pathology

OBJECTIVE: To investigate the expression of galectin-3 and VEGF in laryngeal squamous cell carcinoma (LSCC) tissue and to analyze its role in differentiation, growth and metastasis of the tumor. METHOD: The expression of galectin-3 and VEGF were detected with SP immunohistochemistry staining and western blot in twenty-nine specimens of LSCC and eighteen specimens of laryngeal benign lesion. RESULT: The expression of galectin-3 (89.7%) and VEGF (86.2%) in LSCC were remarkably higher than that in normal control tissue (P<0.05), and the expression of galectin-3 (89.7%) and VEGF (86.2%) in higher histodifferentiation specimens were higher than that in lower histodifferentiation specimens (P<0.05). Moreover, the expression level of galectin-3 and VEGF was detected a statistical positive correlation (r=0.423, P<0.05) in LSCC. CONCLUSION The high level expression of galectin-3 and VEGF in LSCC could play an important role in tumorous histodifferentiation and metastasis.
Carcinoma, Squamous Cell ; metabolism ; pathology ; Female ; Galectin 3 ; metabolism ; Humans ; Laryngeal Neoplasms ; metabolism ; pathology ; Male ; Middle Aged ; Vascular Endothelial Growth Factor A ; metabolism

OBJECTIVETo study the expression of Galectin-3 in human hepatocellular carcinoma (HCC) tissues and the clinical value of serum Galectin-3 in the diagnosis of hepatocellular carcinoma.

METHODSImmunohistochemistry method was used to detect the expression of Galectin-3 in the 46 pairs of HCC tissues and their para cancerous tissues. The relationship between expression levels of Galectin-3 and clinical parameters was analyzed. Serum Galectin-3 in different liver diseases were measured with ELISA. The sensitivity and specificity of galectin-3, alpha fetoprotein (AFP) and gamma-glutamyltranspeptidase II (GGT-II) for diagnosis of HCC were compared and the complementary diagnostic values of Galectin-3 and AFP and GGT-II for HCC were studied.

RESULTS(1) The positive rate of Galectin-3 in the tissue of HCC was 78.2%, dramatically higher than that in para cancerous tissues (15.2%) (P is less than 0.01). The expression levels were correlated with differentiation and with the high expression in poor differentiation tissues; (2) Based on ROC curve, the cut-off of serum Galectin-3 for HCC diagnosis was set as 0.62mug/L, the serum galectin-3 positive rate was 64.5% in HCC cases, which was apparently higher than that in liver cirrhosis, chronic hepatitis and healthy persons (P is less than 0.05); (3) Serum Galectin-3 was not correlated with AFP and GGT-II. Combined determination of the three markers had the complementary diagnostic value for HCC and might increase the diagnostic sensitivity to 94.7%.

CONCLUSIONGalectin-3 is overexpressed in HCC tissues and is correlated with the tumor differentiation, suggesting that Galectin-3 may be associated with the carcinogenesis and development of HCC. Serum galectin-3 increases in the HCC cases and combined determination of serum Galectin-3, AFP and GGT-II can increase the diagnostic efficiency for HCC. Galectin-3 could be a novel serum tumor marker for HCC.

Carcinoma, Hepatocellular ; blood ; metabolism ; Female ; Galectin 3 ; blood ; metabolism ; Humans ; Liver ; metabolism ; Liver Neoplasms ; blood ; metabolism ; Male ; Middle Aged ; Serum ; chemistry

Galectin-3, a member of the beta-galactoside-binding protein family, has been implicated in mammalian sperm maturation. We examined galectin-3 expression in the testis and epididymis of sexually mature and immature bulls. Western blot analysis showed varying levels of galectin-3 in the bull testis and epididymis, and galectin-3 immunoreactivity was higher in the mature testis and epididymis than in immature organs. Galectin-3 was primarily localized in interstitial cells of the immature bull testis and in the peritubular myoid and interstitial cells of the mature testis. In the immature epididymis head, galectin-3 was primarily in the principal and basal cells of the epithelium. In the mature epididymis head, moderate levels of galectin-3 were detected in the sperm, while low levels were found in the stereocilia, epithelium and connective tissue. In the immature epididymis body, moderate protein levels were detected in the principal cells, while lower levels were found in the basal cells. The mature epididymis body showed moderate levels of galectin-3 immunostaining in the stereocilia and epithelium, but low levels in the connective tissue. In the immature epididymis tail, only low levels of galectin-3 staining were found in the epithelium, whereas the mature epididymis tail showed high levels of galectin-3 in the principal cells, moderate levels in the basal cells and low levels in connective tissue. These findings suggest that galectin-3 expression plays a role in the maturation and activation of sperm in bulls.
Aging/physiology ; Animals ; Blotting, Western ; Cattle ; Epididymis/*metabolism ; Galectin 3/*metabolism ; Gene Expression Regulation/physiology ; Immunohistochemistry ; Male ; Sexual Maturation/*physiology ; Testis/*metabolism

OBJECTIVETo investigate the expression of galectin-3 (Gal-3) in prolactinomas.

METHODSExpressions of Gal-3 were evaluated by immunohistochemistry using polyclonal antibody in 16 invasive prolactinomas and 16 prolactinomas.

RESULTSGal-3 was expressed both in invasive prolactinomas and noninvasive prolactinomas while significantly higher expression seen in the invasive prolactinomas (P < 0.05).

CONCLUSIONGal-3 expression may be used as a useful indicator to determine the invasiveness and prognosis of prolactinomas.

Adolescent ; Adult ; Aged ; Female ; Galectin 3 ; biosynthesis ; genetics ; Humans ; Male ; Middle Aged ; Neoplasm Invasiveness ; Pituitary Neoplasms ; metabolism ; pathology ; Prognosis ; Prolactinoma ; metabolism ; pathology

OBJECTIVETo investigate the levels of galectin-3 in the serum and surgical specimens from patients with malignant and benign thyroid lesions and explore their clinical significance.

METHODSSerum samples were collected from 159 patients with thyroid neoplasms and 16 normal subjects for detection of galectin-3 level using ELISA. The expressions of galectin-3 protein and mRNA were also detected in the surgical specimens by immunohistochemistry and in situ hybridization.

RESULTSGalectin-3 protein and mRNA were expressed at a rate of 96.67% in 66 cases of papillary thyroid carcinoma, 83.33% in 6 cases of follicular thyroid carcinoma, 16.67% in 36 cases of papillary hyperplasia, and 11.74% in 51 cases of thyroid adenoma. The expression level of galectin-3 mRNA was slightly lower than but positively correlated with its protein expression. Patients with thyroid carcinoma had significantly higher serum concentration of galectin-3 than those with benign thyroid lesions (papillary hyperplasia and thyroid adenoma) and normal subjects (P<0.001). In patients with papillary thyroid carcinoma, galectin-3 positivity in the tumor tissue was associated with a significantly higher serum galectin-3 level in comparison with the negative cases (P<0.05).

CONCLUSIONDetection of galectin-3 in both the serum and surgical specimens can improve the diagnosis rate of thyroid carcinoma.

Adult ; Aged ; Case-Control Studies ; Early Detection of Cancer ; Female ; Galectin 3 ; blood ; metabolism ; Humans ; Immunohistochemistry ; Male ; Middle Aged ; Thyroid Neoplasms ; blood ; diagnosis ; metabolism ; Young Adult

The present paper aims to investigate whether or not vasculogenic mimicry (VM) exists in laryngeal squamous cell carcinoma (LSCC), and to elucidate its relationship to microvessel density (MVD), galectin-3 (Gal-3) expression, and clinicopathological factors of patients with LSCC. VM, score of MVD and expression of Gal-3 protein were detected by immunohistochemistry and histochemistry in 83 specimens of LSCC tissue and 20 specimens of normal laryngeal tissue. The positive rate of VM in normal laryngeal tissues was 0%, and was 33.7% in LSCC tissues. There was a significant difference between the two groups (P<0. 01). VM or MVD was significantly related to differentiation, pTNM stages and lymph node metastasis of LSCC (P<0.05), but not to age, gender and tumor site (P>0. 05). And there was a positive correlation between every two of VM, score of MVD, and Gal-3 protein (P< 0. 05). The results suggest that expression of Gal-3 protein may be related to the initiation, angiogenesis and VM formation in LSCC; And VM, angiogenesis and Gal-3 protein may be involved in the development, invasion and metastasis of LSCC.
Carcinoma, Squamous Cell ; blood supply ; Galectin 3 ; metabolism ; Head and Neck Neoplasms ; blood supply ; Humans ; Immunohistochemistry ; Laryngeal Neoplasms ; blood supply ; Lymphatic Metastasis ; Neovascularization, Pathologic ; Prognosis