The Experts below are selected from a list of 306 Experts worldwide ranked by ideXlab platform
Jeffrey S Simske - One of the best experts on this subject based on the ideXlab platform.
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genomic structure cdna sequence and expression of gly96 a growth factor inducible immediate early gene encoding a short lived Glycosylated Protein
Oncogene, 1993Co-Authors: Catherine H Charles, Jeong Kyo Yoon, Jeffrey S SimskeAbstract:: We report the cDNA sequence and genomic structure of gly96, an immediate early gene inducible by serum growth factors in mouse fibroblasts. It encodes a 153-amino acid Protein that does not share significant sequence similarity with any known Protein. In the adult mouse, gly96 is expressed predominantly in the lung, testes and the uterus. We have identified the Gly96 Protein in Balb/c 3T3 cells using affinity-purified antibodies recognizing the Gly96 polypeptide. We show that Gly96 is Glycosylated and has a short half-life in serum stimulated fibroblasts.
Ulrich H. Weidle - One of the best experts on this subject based on the ideXlab platform.
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Overexpression of the small transmembrane and Glycosylated Protein SMAGP supports metastasis formation of a rat pancreatic adenocarcinoma line
International Journal of Cancer, 2005Co-Authors: Nesrine Tarbe, Susanne Hummel, Ulrich H. Weidle, Margot ZöllerAbstract:Small cell transmembrane and Glycosylated Protein (SMAGP) was recently identified in the metastasizing rat pancreatic adenocarcinoma line BSp73ASML. SMAGP, an evolutionary conserved transmembrane Protein, is expressed on lateral epithelial cell membranes. SMAGP expression was restricted to or was upregulated in several metastasizing as compared to nonmetastasizing human and rat tumor lines. In contrast to nontransformed tissue, SMAGP was mainly expressed in the cytoplasm, as has already been described for high-grade human colorectal cancer. This raised the question on the impact of SMAGP on tumor progression. To answer the question, metastasis formation was evaluated in the nonmetastasizing rat pancreatic adenocarcinoma subline BSp73AS (AS), which was stably transfected with SMAGP cDNA (AS-SMAGP). Cytoplasmic SMAGP expression promoted cell agglomeration, but inhibited tumor cell proliferation, adhesion to and migration toward vitronectin and matrigel invasion, which was accompanied by a failure of actin reorganization. AS-SMAGP clones strongly promoted metastasis formation by dislodgment of normal tissue; 82% of rats developed lymph node metastasis as compared to 22% of rats receiving AS or mock-cDNA-transfected AS cells. The incidence of lung metastasis was increased from 6% in AS to 98% in AS-SMAGP tumor-bearing rats. Thus, SMAGP strongly promotes tumor progression. This likely is due to redistribution from the plasma membrane into the cytoplasm. SMAGP redistribution does not only facilitate tumor cell detachment from neighboring cells and the extracellular matrix, but obviously contributes actively by a not yet defined mechanism to tumor cell agglomeration and capillary plugging.
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SMAGP, a new small trans-membrane glycoProtein altered in cancer
Oncogene, 2004Co-Authors: Nesrine G Tarbé, Ulrich H. WeidleAbstract:Using the Affymetrix array technology, we previously identified an EST strongly expressed in several metastatic cell lines. In the present study, we cloned the corresponding cDNA that encodes a new glycoProtein composed of 97 amino acids and containing a trans-membrane domain. Therefore, we named it SMAGP for Small trans-Membrane And Glycosylated Protein. SMAGP is strongly conserved during evolution. It is expressed by normal epithelia of various organs, the Protein being notably localized to the lateral face of the plasma membrane of cohesive well-polarized epithelial cells. In addition, SMAGP contains binding domains for the Protein 4.1 and the PDZ domain of MAGUK Proteins. Similar Protein features are observed in several cell-surface Proteins involved via ternary complexes in intercellular processes leading to cytoskeleton assembly as well as intracellular signalling. Thus, SMAGP might similarly be involved in a scaffolding Protein complex, and therefore participate in the epithelium organization or in subsequent functions. Immunohistochemical data obtained using human breast, colon and lung cancer samples sustain this hypothesis since they showed that, in both primary tumours and metastases, reduced expression and/or cytoplasmic redistribution of SMAGP is superimposable with low histological tumour differentiation features, namely a lack of epithelial cell polarity and disorganized tissue phenotype.
Chihiro Sato - One of the best experts on this subject based on the ideXlab platform.
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pig sperm membrane microdomains contain a highly Glycosylated 15 25 kda wheat germ agglutinin binding Protein
Biochemical and Biophysical Research Communications, 2012Co-Authors: Waraporn Kasekarn, Takeru Kanazawa, Kazuki Hori, Tomoyuki Tsuchiyama, Xue Lian, Estelle Garenaux, Kessiri Kongmanas, Nongnuj Tanphaichitr, Hiroshi Yasue, Chihiro SatoAbstract:Abstract A highly Glycosylated Protein, which has unique, novel features in localization, structure, and potential function, is found in pig sperm, and named WGA-gp due to its high binding property with wheat germ agglutinin (WGA). WGA-gp is localized mainly in flagella and enriched in membrane microdomains or lipid rafts. It is not detected by ordinary Protein staining methods due to a high content of both N- and O-glycans consisting of neutral monosaccharides. Interestingly, WGA-gp may be involved in intracellular Ca2+ regulation. Treatment of sperm with anti-WGA-gp antibody enhances the amplitude of Ca2+ oscillation without changing the basal intracellular Ca2+ concentrations. All these features of WGA-gp, except for different carbohydrate structures occupying most part of the molecules, are similar to those of flagellasialin in sea urchin sperm, which regulates the intracellular Ca2+ concentration. Presence of carbohydrate-enriched flagellar Proteins involved in intracellular Ca2+ regulation may be a common feature among animal sperm.
Kenjiro Murata - One of the best experts on this subject based on the ideXlab platform.
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decreased fluidity of polymorphonuclear leukocyte membrane in streptozocin induced diabetic rats
Diabetes, 1990Co-Authors: Midori Masuda, Hiroshi Egawa, Takashi Murakami, Kenjiro MurataAbstract:Using flow cytometry with the excimer-forming lipid technique with pyrenedecanoic acid, we measured membrane fluidity of polymorphonuclear leukocytes (PMNs) from 20 streptozocin (STZ)-induced diabetic rats. Diabetes mellitus was induced in male Sprague-Dawley rats (body wt 243 ± 11 g) with an injection of 25 mg/kg i.v. STZ. Membrane fluidity of PMNs was significantly lower at 2 wk after the STZ injection when serum glucose reached the plateau (31.1 ± 5.8 mM), and after 3 wk, membrane fluidity remained unchanged. In 7 STZ-resistant rats for which serum glucose was r = −0.76) but not with serum lipid levels. Cross-incubation studies ascribed this observation to factors in the diabetic rat serum. Glycosylated Protein, which was separated from diabetic rat serum, decreased membrane fluidity of control rat PMNs. Human diabetic subjects have an increased risk for infection, which may be due partly to altered membrane fluidity of their PMNs.
Waraporn Kasekarn - One of the best experts on this subject based on the ideXlab platform.
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pig sperm membrane microdomains contain a highly Glycosylated 15 25 kda wheat germ agglutinin binding Protein
Biochemical and Biophysical Research Communications, 2012Co-Authors: Waraporn Kasekarn, Takeru Kanazawa, Kazuki Hori, Tomoyuki Tsuchiyama, Xue Lian, Estelle Garenaux, Kessiri Kongmanas, Nongnuj Tanphaichitr, Hiroshi Yasue, Chihiro SatoAbstract:Abstract A highly Glycosylated Protein, which has unique, novel features in localization, structure, and potential function, is found in pig sperm, and named WGA-gp due to its high binding property with wheat germ agglutinin (WGA). WGA-gp is localized mainly in flagella and enriched in membrane microdomains or lipid rafts. It is not detected by ordinary Protein staining methods due to a high content of both N- and O-glycans consisting of neutral monosaccharides. Interestingly, WGA-gp may be involved in intracellular Ca2+ regulation. Treatment of sperm with anti-WGA-gp antibody enhances the amplitude of Ca2+ oscillation without changing the basal intracellular Ca2+ concentrations. All these features of WGA-gp, except for different carbohydrate structures occupying most part of the molecules, are similar to those of flagellasialin in sea urchin sperm, which regulates the intracellular Ca2+ concentration. Presence of carbohydrate-enriched flagellar Proteins involved in intracellular Ca2+ regulation may be a common feature among animal sperm.