Human PLXDC1 / TEM7 Protein
- Known as:
- Human PLXDC1 / TEM7 Protein
- Catalog number:
- PL1-H5225
- Product Quantity:
- 100ug
- Category:
- -
- Supplier:
- acrobyosystems
- Gene target:
- Human PLXDC1 / TEM7 Protein
Related genes to: Human PLXDC1 / TEM7 Protein
- Gene:
- PLXDC1 NIH gene
- Name:
- plexin domain containing 1
- Previous symbol:
- -
- Synonyms:
- TEM3, TEM7
- Chromosome:
- 17q12
- Locus Type:
- gene with protein product
- Date approved:
- 2003-08-27
- Date modifiied:
- 2016-10-05
- Gene:
- PLXDC2 NIH gene
- Name:
- plexin domain containing 2
- Previous symbol:
- -
- Synonyms:
- TEM7R, FLJ14623
- Chromosome:
- 10p12.31
- Locus Type:
- gene with protein product
- Date approved:
- 2003-08-27
- Date modifiied:
- 2016-10-05
Related products to: Human PLXDC1 / TEM7 Protein
Related articles to: Human PLXDC1 / TEM7 Protein
- The cornea is richly innervated by the trigeminal ganglion (TG) and its function supported by secretions from the adjacent lacrimal (LG) and meibomian glands (MG). In this study we examined how pigment epithelium-derived factor (PEDF) gene deletion affects the cornea structure and function. - Source: PubMed
Shang ZhenyingLi ChenxiLiu XuemeiXu ManhongZhang XiaominLi XiaorongBarnstable Colin JZhao ShaozhenTombran-Tink Joyce - The rhesus monkey rhadinovirus (RRV), a γ2-herpesvirus of rhesus macaques, shares many biological features with the human pathogenic Kaposi's sarcoma-associated herpesvirus (KSHV). Both viruses, as well as the more distantly related Epstein-Barr virus, engage cellular receptors from the Eph family of receptor tyrosine kinases (Ephs). However, the importance of the Eph interaction for RRV entry varies between cell types suggesting the existence of Eph-independent entry pathways. We therefore aimed to identify additional cellular receptors for RRV by affinity enrichment and mass spectrometry. We identified an additional receptor family, the Plexin domain containing proteins 1 and 2 (Plxdc1/2) that bind the RRV gH/gL glycoprotein complex. Preincubation of RRV with soluble Plxdc2 decoy receptor reduced infection by ~60%, while overexpression of Plxdc1 and 2 dramatically enhanced RRV susceptibility and cell-cell fusion of otherwise marginally permissive Raji cells. While the Plxdc2 interaction is conserved between two RRV strains, 26-95 and 17577, Plxdc1 specifically interacts with RRV 26-95 gH. The Plxdc interaction is mediated by a short motif at the N-terminus of RRV gH that is partially conserved between isolate 26-95 and isolate 17577, but absent in KSHV gH. Mutation of this motif abrogated the interaction with Plxdc1/2 and reduced RRV infection in a cell type-specific manner. Taken together, our findings characterize Plxdc1/2 as novel interaction partners and entry receptors for RRV and support the concept of the N-terminal domain of the gammaherpesviral gH/gL complex as a multifunctional receptor-binding domain. Further, Plxdc1/2 usage defines an important biological difference between KSHV and RRV. - Source: PubMed
Publication date: 2021/03/03
Großkopf Anna KSchlagowski SarahFricke ThomasEnsser ArminDesrosiers Ronald CHahn Alexander S - Pigment Epithelium Derived Factor (PEDF) is a secreted factor that has broad biological activities. It was first identified as a neurotrophic factor and later as the most potent natural antiangiogenic factor, a stem cell niche factor, and an inhibitor of cancer cell growth. Numerous animal models demonstrated its therapeutic value in treating blinding diseases and diverse cancer types. A long-standing challenge is to reveal how PEDF acts on its target cells and the identities of the cell-surface receptors responsible for its activities. Here we report the identification of transmembrane proteins PLXDC1 and PLXDC2 as cell-surface receptors for PEDF. Using distinct cellular models, we demonstrate their cell type-specific receptor activities through loss of function and gain of function studies. Our experiments suggest that PEDF receptors form homooligomers under basal conditions, and PEDF dissociates the homooligomer to activate the receptors. Mutations in the intracellular domain can have profound effects on receptor activities. - Source: PubMed
Publication date: 2014/12/23
Cheng GuoZhong MingKawaguchi RikiKassai MikiAl-Ubaidi MuayyadDeng JunTer-Stepanian MariamSun Hui - Plexin-domain containing 2 (Plxdc2) is a relatively uncharacterised transmembrane protein with an area of nidogen homology and a plexin repeat (PSI domain) in its extracellular region. Here, we describe Plxdc2 expression in the embryonic mouse, with particular emphasis on the developing central nervous system. Using light microscopy and optical projection tomography (OPT), we analyse RNA in situ hybridization patterns and expression of two reporter genes, beta-geo (a fusion of beta-galactosidase to neomycin phosphotransferase) and placental alkaline phosphatase (PLAP) in a Plxdc2 gene trap mouse line (KST37; [Leighton, P.A., Mitchell, K.J., Goodrich, L.V., Lu, X., Pinson, K., Scherz, P., Skarnes, W.C., Tessier-Lavigne, M., 2001. Defining brain wiring patterns and mechanisms through gene trapping in mice. Nature 410, 174-179]). At mid-embryonic stages (E9.5-E11.5) Plxdc2-betageo expression is prominent in a number of patterning centres of the brain, including the cortical hem, midbrain-hindbrain boundary and the midbrain floorplate. Plxdc2 is expressed in other tissues, most notably the limbs, lung buds and developing heart, as well as the spinal cord and dorsal root ganglia. At E15.5, expression is apparent in a large number of discrete nuclei and structures throughout the brain, including the glial wedge and derivatives of the cortical hem. Plxdc2-betageo expression is particularly strong in the developing Purkinje cell layer, especially in the posterior half of the cerebellum. The PLAP marker is expressed in a number of axonal tracts, including the posterior commissure, mammillotegmental tract and cerebellar peduncle. We compare Plxdc2-betageo expression in the embryonic brain with the much more restricted expression of the related gene Plxdc1 and with members of the Wnt family (Wnt3a, Wnt5a and Wnt8b) that show a striking overlap with Plxdc2 expression in certain areas. - Source: PubMed
Publication date: 2006/12/16
Miller Suzanne F CSummerhurst KristenRünker Annette EKerjan GéraldineFriedel Roland HChédotal AlainMurphy PaulaMitchell Kevin J - ARHGAP family genes, such as FNBP2, SRGAP1/ARHGAP13, SRGAP2/ARHGAP14, ARHGAP4 and AHRGAP20/KIAA1391, encode GTPase activating proteins for Rho family proteins (RhoGAPs). Here, we identified and characterized the ARHGAP23 gene by using bioinformatics. KIAA1501 (AB040934.1) was a 5'-truncated partial cDNA derived from the ARHGAP23 gene. Complete coding sequence of human ARHGAP23 cDNA was determined by assembling BM806021 EST, BQ718622 EST, KIAA1501 partial cDNA, and AC115090.8 genome sequence corresponding to exons 7 and 25. ARHGAP23 gene encoded 1491-aa isoform 1 (without exon 23) and 1144-aa isoform 2 (with exon 23) due to alternative splicing. Isoform 2 was C-terminally truncated due to frame-shift within 23-bp exon 23. ARHGAP23 mRNA was expressed in placenta, prostate, hippocampus, brain medulla as well as in brain tumor, salivary gland tumor, head and neck tumor. Mouse 4933428G20 (NM_021493.1) was a 5'-truncated partial cDNA derived from Arhgap23 gene at mouse chromosome 11D. Human ARHGAP23, ARHGAP21 and Xenopus rGAP shared the common domain structure consisting of PDZ, Pleckstrin homology (PH), and RhoGAP domains. ARHGAP23-KIAA1684-MLLT6-RNF110-PIP5K2B-LASP1-PLXDC1-CACNB1 locus at human chromosome 17q12 and CACNB2-PLXDC2-LASP2-MLLT10-BMI1-PIP5K2A-KIAA1217-ARHGAP21 locus at human chromosome 10p12 were paralogous regions (paralogons) with internal inversion. MLLT6, MLLT10 and LASP1 genes are fusion partners of MLL gene in hematological malignancies, while RNF110, PIP5K2B, LASP1 and BMI1 genes are amplified in human tumors. Evolutionary recombination hotspots and oncogenomic recombination hotspots were co-localized around the ARHGAP23-CACNB1 locus and the ARHGAP21-CACNB2 locus. - Source: PubMed
Katoh MasukoKatoh Masaru