Cloning and Expression of Nope, a New Mouse Gene of the Immunoglobulin Superfamily Related to Guidance Receptors

Genomics ◽  
2000 ◽  
Vol 64 (1) ◽  
pp. 15-23 ◽  
Author(s):  
J.Michael Salbaum ◽  
Claudia Kappen
Keyword(s):  
Mouse Gene ◽  
Cloning And Expression ◽  
Immunoglobulin Superfamily ◽  
Guidance Receptors

Cloning and expression of new receptors belonging to the immunoglobulin superfamily from the marine sponge Geodia cydonium

1999 ◽  
Vol 49 (9) ◽  
pp. 751-763 ◽  
Author(s):  
Barbara Blumbach ◽  
Bärbel Diehl-Seifert ◽  
Jürgen Seack ◽  
Renate Steffen ◽  
Isabel M. Müller ◽  
...  
Keyword(s):  
Marine Sponge ◽  
Cloning And Expression ◽  
Immunoglobulin Superfamily ◽  
Geodia Cydonium

197 MOLECULAR CLONING AND EXPRESSION OF THE CASHMERE GOAT IZUMO GENE

2011 ◽  
Vol 23 (1) ◽  
pp. 199
Author(s):  
R. H. Na ◽  
L. Liang ◽  
L. Fu
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Transmembrane Protein ◽  
Northern Blotting ◽  
Cloning And Expression ◽  
Immunoglobulin Superfamily ◽  
Predicted Amino Acid Sequence ◽  
Type I ◽  
Cashmere Goat ◽  
Calculated Molecular Mass

During the fertilization process, complex events are involved in the fusion between the reacted spermatozoa and the mature oocyte. Fusion implies that many proteins are present on the cell membrane of the gametes. Recently, a new protein, Izumo, has been shown to play a role in the sperm–egg fusion. Izumo was identified through the generation of a monoclonal antibody that inhibits this fusion. This protein belongs to the immunoglobulin superfamily type I transmembrane protein. Izumo can be detected only after acrosome reaction at the spermatozoal surface. The cashmere goat Izumo gene was identified and cloned by 3′ and 5′ rapid amplification of cDNA ends-PCR. The expression of cashmere goat Izumo was examined by RT-PCR and Northern blotting. The full-length cDNA of cashmere goat Izumo contains 1536 bp and an open reading frame of 1035 bp, encoding a polypeptide of 344 amino acids with a calculated molecular mass of 38.76 kDa and a theoretical isoelectric point of 8.18. This predicted amino acid sequence showed 89.82% amino acid identity with the bovine Izumo. The deduced amino acid sequence contained 3 conserved domains of the signal peptide, immunoglobulin-like domain, and transmembrane region. Reverse transcription-PCR and Northern blotting analysis showed that cashmere goat Izumo transcripts were highly expressed in the testis, caput, corpus, cauda epididymis. Cashmere goat Izumo may play a role in the biological process of fertilization. This work was supported by the National Natural Science Foundation (No. 30560103 and No.30740043), China, and the China Postdoctoral Science Foundation.

scholarly journals Molecular cloning and expression of a new rat liver cell-CAM105 isoform. Differential phosphorylation of isoforms

1992 ◽  
Vol 285 (1) ◽  
pp. 47-53 ◽  
Author(s):  
O Culic ◽  
Q H Huang ◽  
D Flanagan ◽  
D Hixson ◽  
S H Lin
Keyword(s):  
Cell Adhesion Molecule ◽  
Short Form ◽  
Structural Features ◽  
Cloning And Expression ◽  
Immunoglobulin Superfamily ◽  
Long Form ◽  
Predominant Form ◽  
Differential Phosphorylation ◽  
Isolated Cell

An hepatocyte cell-adhesion molecule (cell-CAM105) was recently shown to be identical with the liver plasma-membrane ecto-ATPase. This protein has structural features of the immunoglobulin superfamily and is homologous with carcinoembryonic antigen proteins. We have cloned a cDNA encoding a new form of the cell-CAM105 which is a variant of the previously isolated clone. In addition to having a shorter cytoplasmic domain, the new isoform also has substitutions clustered in the first 130 amino acids of the extracellular domain. Both of these isoforms are expressed on the surface of hepatocytes with the shorter variant being the predominant form. The previously isolated cell-CAM105 (long form) has more potential phosphorylation sites than does the new isoform (short form). Both isoforms are found to be phosphorylated after incubation with [32P]phosphate in vitro, with the long form being phosphorylated to a significantly higher extent. This observed differential phosphorylation could be one of the mechanisms for the regulation of isoform functions. Using antipeptide antibodies specific for the long form and antibodies that are reactive with both isoforms, we have shown that both isoforms are localized in the canalicular domain of hepatocytes. The sequence differences between these two isoforms suggest that they are probably derived from different genes rather than from alternative splicing.

scholarly journals Cloning and expression analysis of a novel mouse gene with sequence similarity to the Drosophila fat facets gene

1997 ◽  
Vol 63 (1) ◽  
pp. 29-38 ◽  
Author(s):  
Stephen A Wood ◽  
Wendy S Pascoe ◽  
KeLin Ru ◽  
Toshiya Yamada ◽  
Jens Hirchenhain ◽  
...  
Keyword(s):  
Expression Analysis ◽  
Sequence Similarity ◽  
Mouse Gene ◽  
Cloning And Expression ◽  
Fat Facets

scholarly journals CLONING AND EXPRESSION OF VACCINIA VIRUS PROTEIN (B18) IN HETEROLOGOUS HOST

2017 ◽  
Vol 5 (8(SE)) ◽  
pp. 57-71
Author(s):  
Swaroop Sarkar ◽  
V.V.S. Suryanarayana
Keyword(s):  
Vaccinia Virus ◽  
Cloning And Expression ◽  
Immunoglobulin Superfamily ◽  
Virus Protein ◽  
Affinity Column ◽  
Heterologous Host ◽  
Signaling Mechanism ◽  
Affinity Column Chromatography ◽  
Alpha Receptors ◽  
New Strategies

B18 is an immunoglobulin superfamily glycoprotein produced by vaccinia virus which resembles to interferon alpha receptors. It acts both in solution and also when associated with the cell surface. This B18 protein was expressed in heterologous host and purified based on affinity column chromatography. The purified B18 protein has been evaluated for biological activity in Pig Kidney- 15 cells (PK-15) which has been reported to have α –interferon receptors and signaling mechanism. The CPE was more than 90% in the presence of protein and around 50% in the absence. B-18 can enhance the infectivity of FMDV to cells having α –interferon receptors. This provides the basis for developing new strategies for improving attenuated vaccines and its capacity to act as an enhancer protein.

Cloning and Expression of an Immunoglobulin Superfamily Gene (IGSF1) in Xq25

Genomics ◽  
1998 ◽  
Vol 48 (2) ◽  
pp. 157-162 ◽  
Author(s):  
Richard Mazzarella ◽  
Gina Pengue ◽  
Jonathan Jones ◽  
Carmela Jones ◽  
David Schlessinger
Keyword(s):  
Cloning And Expression ◽  
Immunoglobulin Superfamily

Genomic analysis of C-type lectins

2002 ◽  
Vol 69 ◽  
pp. 59-72 ◽  
Author(s):  
Kurt Drickamer ◽  
Andrew J. Fadden
Keyword(s):  
Biological Effects ◽  
Cell Signalling ◽  
Genomic Analysis ◽  
Binding Activity ◽  
Immunoglobulin Superfamily ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition ◽  
Calcium Dependent ◽  
Binding Domains ◽  
Carbohydrate Recognition Domains

Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are present in vertebrates only. At the cell surface, calcium-dependent (C-type) lectins and galectins are found in model invertebrates and vertebrates, but not in yeast; immunoglobulin superfamily (I-type) lectins are only found in vertebrates. The evolutionary appearance of different classes of sugar-binding protein modules parallels a development towards more complex oligosaccharides that provide increased opportunities for specific recognition phenomena. An overall picture of the lectins present in humans can now be proposed. Based on our knowledge of the structures of several of the C-type carbohydrate-recognition domains, it is possible to suggest ligand-binding activity that may be associated with novel C-type lectin-like domains identified in a systematic screen of the human genome. Further analysis of the sequences of proteins containing these domains can be used as a basis for proposing potential biological functions.

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