2008年1月24日 星期四
2008年1月23日 星期三
galectin family pretty
http://stweb.cgu.edu.tw/~b9309005/TLR/galectin.pretty
藉由pretty的結果，可以比較galectin family中不同的galectin gene中的consense sequence的比較
藉由pretty的結果，可以比較galectin family中不同的galectin gene中的consense sequence的比較
galectin-1 phylogenetics
藉由比較不同物種的galectin-1可以知道其他物種於人類galectin-1的相似程度，經過分析過後可以知道與人類最相近的是rhesus monkey，第二相近的則是house mouse
Galectin-1 mapping
http://stweb.cgu.edu.tw/~b9309005/TLR/galectin-1.map
這是將galectin-1作mapping的結果，可以知道restriction enzyme 的切點
這是將galectin-1作mapping的結果，可以知道restriction enzyme 的切點
Galectin-7
GENE FUNCTION
Cao et al. (2003) reported the role of the carbohydrate-binding protein, galectin-7, in reepithelialization of corneal wounds. They found that expression of galectin-7 was markedly upregulated in corneal epithelium after injury and that exogenous galectin-7 stimulated reepithelialization of corneal wounds. The stimulatory effect of galectin-7 on corneal epithelial wound closure was specifically inhibited by beta-lactose, a competing sugar, but unaffected by sucrose, an irrelevant disaccharide.
Cao et al. (2003) reported the role of the carbohydrate-binding protein, galectin-7, in reepithelialization of corneal wounds. They found that expression of galectin-7 was markedly upregulated in corneal epithelium after injury and that exogenous galectin-7 stimulated reepithelialization of corneal wounds. The stimulatory effect of galectin-7 on corneal epithelial wound closure was specifically inhibited by beta-lactose, a competing sugar, but unaffected by sucrose, an irrelevant disaccharide.
GenBank: NM_002307
Protein: EAW56818
Galectin-4
Gene map locus 19q13.2
Huflejt et al. (1997) found that LGALS4 is expressed as a 38-kD protein in the human colon adenocarcinoma T84 cell line.In confluent T84 cells, LGALS4 is mainly cytosolic and is concentrated at the basal membrane. In subconfluent T84 cells, it is found in attachment sites of newly seeded cells and is concentrated at the leading edge of lamellipodia. Based on the localization of LGALS4 and the ability of immobilized recombinant rat Lgals4 to enhance adhesion of T84 cells, Huflejt et al. (1997) suggested that LGALS4 plays a role in cell adhesion.
GenBank: NM_006149
Protein : EAW56820
Reference:
http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602518
Galectin-3
Gene map locus 14q21-q22
Gene function
Galectin-3 is expressed in various tissues and organs, but is significantly absent in normal hepatocytes. However, evaluation of patient liver biopsies for galectin-3 expression revealed that hepatocellular carcinoma (HCC) frequently expressed significant levels of this lectin; 76% were immunohistochemically positive. Further investigations showed that galectin-3 expression in HCC is independent of whether the patient had prior hepatitis B virus infection (Hsu et al., 1999). Hsu et al. (1999) suggested that deregulated expression of galectin-3 can result in tumor transformation and invasiveness, or confer propensity for tumor cell survival.
In the thyroid, expression of galectin-3 protein had been described in differentiated follicular cancer, suggesting that the immunohistochemical study of galectin-3 may be a potential marker of malignancy in thyroid neoplasms. Martins et al. (2002) analyzed galectin-3 protein and mRNA expression in thyroid tissues from 87 patients with histomorphologic diagnosis of multinodular goiter (MNG), follicular adenoma, follicular carcinoma, papillary carcinoma, and 5 normal tissues.
Yoshimura et al. (2003) found increased expression of the LGALS3 gene in human nonsmall cell lung cancer, and suggested that it may play a role in the process of metastasis in this malignancy but not in small cell lung cancer. They considered that LGALS3 may be a phenotypic marker that excludes small cell lung cancer and a novel target molecule in therapy of nonsmall cell lung cancer.
Ohshima et al. (2003) found that galectin-3 mRNA and protein are expressed throughout synovial tissue in rheumatoid arthritis (RA; 180300) and that both galectin-3 and its binding protein are found at sites of joint destruction. In addition, levels of galectin-3 in serum and synovial fluid as well as levels of its binding protein in synovial fluid were significantly elevated in RA compared to osteoarthritis and healthy controls (p less than 0.001).
Henderson et al. (2006) found that galectin-3 was upregulated in established human fibrotic liver disease. In experimental hepatic fibrosis in rats, galectin-3 upregulation was associated with induction and resolution of fibrosis.
Galectin-3 is expressed in various tissues and organs, but is significantly absent in normal hepatocytes. However, evaluation of patient liver biopsies for galectin-3 expression revealed that hepatocellular carcinoma (HCC) frequently expressed significant levels of this lectin; 76% were immunohistochemically positive. Further investigations showed that galectin-3 expression in HCC is independent of whether the patient had prior hepatitis B virus infection (Hsu et al., 1999). Hsu et al. (1999) suggested that deregulated expression of galectin-3 can result in tumor transformation and invasiveness, or confer propensity for tumor cell survival.
In the thyroid, expression of galectin-3 protein had been described in differentiated follicular cancer, suggesting that the immunohistochemical study of galectin-3 may be a potential marker of malignancy in thyroid neoplasms. Martins et al. (2002) analyzed galectin-3 protein and mRNA expression in thyroid tissues from 87 patients with histomorphologic diagnosis of multinodular goiter (MNG), follicular adenoma, follicular carcinoma, papillary carcinoma, and 5 normal tissues.
Yoshimura et al. (2003) found increased expression of the LGALS3 gene in human nonsmall cell lung cancer, and suggested that it may play a role in the process of metastasis in this malignancy but not in small cell lung cancer. They considered that LGALS3 may be a phenotypic marker that excludes small cell lung cancer and a novel target molecule in therapy of nonsmall cell lung cancer.
Ohshima et al. (2003) found that galectin-3 mRNA and protein are expressed throughout synovial tissue in rheumatoid arthritis (RA; 180300) and that both galectin-3 and its binding protein are found at sites of joint destruction. In addition, levels of galectin-3 in serum and synovial fluid as well as levels of its binding protein in synovial fluid were significantly elevated in RA compared to osteoarthritis and healthy controls (p less than 0.001).
Henderson et al. (2006) found that galectin-3 was upregulated in established human fibrotic liver disease. In experimental hepatic fibrosis in rats, galectin-3 upregulation was associated with induction and resolution of fibrosis.
GenBank: NM_002306
Protein: EAW80660.
Galectin-2
Gal-2 is encoded by the LSGALS1 gene and LGALS2在 chromosome 22q13.1 上
Gene fuction
Ozaki et al. (2004) demonstrated that galectin-2 binds to lymphotoxin-alpha (LTA; 153440).
Ozaki et al. (2004) demonstrated that galectin-2 binds to lymphotoxin-alpha (LTA; 153440).
GenBank: NM_006498
Protein: EAW60167.
Reference:
Galectin-1
Gal-1 is encoded by the LSGALS1 gene 在chromosome 22q12的位置上
Gene fuction
Baldini et al. (1993) stated that the mouse beta-galactoside-binding protein is an autocrine regulator of cell proliferation with a role in the maintenance of G0 and in the control of G2 traverse.
Gene fuctionBaldini et al. (1993) stated that the mouse beta-galactoside-binding protein is an autocrine regulator of cell proliferation with a role in the maintenance of G0 and in the control of G2 traverse.
Nipah virus (NiV) is an emerging pathogen that causes severe, often fatal, febrile encephalitis. Levroney et al. (2005) examined the effect of GAL1 on cell fusion mediated by the heavily glycosylated fusion (F) and attachment (G) proteins of NiV. Immunoblot analysis showed that both proteins bound GAL1. NiV envelope-mediated cell-cell fusion was blocked by dimeric GAL1, but not by a monomeric GAL1 mutant, in a paramyxovirus-specific manner. GAL1 binding occurred at specific virus N-glycans and caused aberrant oligomerization of NiV-F and NiV-G, suggesting a mechanism for fusion inhibition. Levroney et al. (2005) proposed that GAL1-mediated production of IL6 (147620) may assist in augmenting the innate immune response against NiV.
A number of distinct interactions influence binding of human immunodeficiency virus (HIV)-1 (see 609423) to the host cell surface. Ouellet et al. (2005) challenged cells and lymphoid tissue explants with HIV-1 and found that recombinant GAL1, but not GAL3 (LGALS3; 153619), increased virus production in a dose-dependent manner by facilitating and accelerating attachment of HIV-1 to the cell surface, even in the presence of various HIV-1 absorption and binding blockers (e.g., anti-CD4 (186940)). Inhibition of HIV-1 fusion using the T-20 peptide (enfuvirtide) was not affected by the presence of GAL1. Because GAL1 is highly expressed in HIV-1 reservoir organs, such as thymus and lymph nodes, and is secreted by activated CD8 (see 186910)-positive T cells, which are present in high levels in HIV-1-infected patients, Ouellet et al. (2005) proposed that GAL1 may be a significant factor that augments the efficiency of the HIV-1 infection process.
Using a yeast 2-hybrid assay, Thijssen et al. (2006) found that GAL1 is the receptor for anginex, an antiangiogenic drug. GAL1 was overexpressed in endothelial cells of different human tumors, and its knockdown in cultured human endothelial cells inhibited cell proliferation and migration.
GenBank: NM_002305
Protein: EAW60178
Reference:
Galectin family
Galectins 是一個carbohydate-binding protein 的家族，可以與 beta-galactosides作結合並且它們在系統發展的過程中，有著高度保留的amino-acid-sequences，約130 amino acids和 用來與beta-galactosides結合的carbohydrate recognition domain(CRD)。
目前已經被發現的galectin family共有 15 種。有些galectins的只有一個CRD的生物活性 monomer，包含galectins-5, -7, -10, 也有 homodimer ，galectins-1, -2, -11,13–14, -15 或者有的是藉由theirnon-lectin domain 聚集合成oligomers ，galectin-3; 有些則有2個 CRD 連接著short linker peptide (galectins-4, -6, -8, -9, -12)。
Galectins 在生物體的分布不只有在脊椎動物上，也可以在無脊椎動物身上發現，包括線蟲、昆蟲、軟體動物，甚至最近在真菌也有發現。Galectin可以和 galactose-binding 的活性，與很多的生物現象有關，像是發育、分化、型態、腫瘤轉移、細胞凋亡，RNA splicing等等。而不同的galectin的作用與它們辨認的 carbohydrate有關。
Galectin 的型態有3種類型：proto, chimera and tandem-repeat types (fig.1)
目前已經被發現的galectin family共有 15 種。有些galectins的只有一個CRD的生物活性 monomer，包含galectins-5, -7, -10, 也有 homodimer ，galectins-1, -2, -11,13–14, -15 或者有的是藉由theirnon-lectin domain 聚集合成oligomers ，galectin-3; 有些則有2個 CRD 連接著short linker peptide (galectins-4, -6, -8, -9, -12)。
Galectins 在生物體的分布不只有在脊椎動物上，也可以在無脊椎動物身上發現，包括線蟲、昆蟲、軟體動物，甚至最近在真菌也有發現。Galectin可以和 galactose-binding 的活性，與很多的生物現象有關，像是發育、分化、型態、腫瘤轉移、細胞凋亡，RNA splicing等等。而不同的galectin的作用與它們辨認的 carbohydrate有關。
Galectin 的型態有3種類型：proto, chimera and tandem-repeat types (fig.1)
Reference:
Galectin-1: a small protein with major functions. Glycobiology. 2006 Nov;16(11):137R-157R. Epub 2006 Jul 13.
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