Search results for "CD98"

showing 4 items of 4 documents

The receptor protein tyrosine phosphatase PTPRJ negatively modulates the CD98hc oncoprotein in lung cancer cells.

2018

PTPRJ, a receptor protein tyrosine phosphatase strongly downregulated in human cancer, displays tumor suppressor activity by negatively modulating several proteins involved in proliferating signals. Here, through a proteomic-based approach, we identified a list of potential PTPRJ-interacting proteins and among them we focused on CD98hc, a type II glycosylated integral membrane protein encoded by SLC3A2, corresponding to the heavy chain of a heterodimeric transmembrane amino-acid transporter, including LAT1. CD98hc is widely overexpressed in several types of cancers and contributes to the process of tumorigenesis by interfering with cell proliferation, adhesion, and migration. We first valid…

0301 basic medicineCD98hcChemistryCell growthCellPTPRJProtein tyrosine phosphatasemedicine.disease_causeProtein tyrosine phosphatase03 medical and health scienceschemistry.chemical_compound030104 developmental biologymedicine.anatomical_structureProteasomal degradationOncologyMG132Cancer cellCancer researchmedicineProteasome inhibitorGene silencingLung cancerCarcinogenesismedicine.drugResearch Paper
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CATs and HATs: the SLC7 family of amino acid transporters

2004

The SLC7 family is divided into two subgroups, the cationic amino acid transporters (the CAT family, SLC7A1-4) and the glycoprotein-associated amino acid transporters (the gpaAT family, SLC7A5-11), also called light chains or catalytic chains of the hetero(di)meric amino acid transporters (HAT). The associated glycoproteins (heavy chains) 4F2hc (CD98) or rBAT (D2, NBAT) form the SLC3 family. Members of the CAT family transport essentially cationic amino acids by facilitated diffusion with differential trans-stimulation by intracellular substrates. In some cells, they may regulate the rate of NO synthesis by controlling the uptake of l-arginine as the substrate for nitric oxide synthase (NOS…

CD98Amino Acid Transport System y+PhysiologyStereochemistryClinical Biochemistry610 Medicine & healthLarge Neutral Amino Acid-Transporter 11308 Clinical BiochemistryImmunoglobulin light chain142-005 142-0052737 Physiology (medical)CationsPhysiology (medical)medicineAnimalsHumansAmino Acidschemistry.chemical_classificationbiologySystem LBiological TransportTransporter1314 Physiologymedicine.diseaseLysinuric protein intoleranceAmino acidchemistryBiochemistryMultigene Familybiology.protein570 Life sciences; biologyCotransporterPfl�gers Archiv European Journal of Physiology
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O44. Inhibition of CD98-associated amino acid transporters by dinitrosyl iron complexes

2008

chemistry.chemical_classificationCancer ResearchCD98BiochemistrybiologyPhysiologyChemistryClinical Biochemistrybiology.proteinTransporterBiochemistryAmino acidNitric Oxide
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Human endometrial CD98 is essential for blastocyst adhesion.

2010

Background Understanding the molecular basis of embryonic implantation is of great clinical and biological relevance. Little is currently known about the adhesion receptors that determine endometrial receptivity for embryonic implantation in humans. Methods and Principal Findings Using two human endometrial cell lines characterized by low and high receptivity, we identified the membrane receptor CD98 as a novel molecule selectively and significantly associated with the receptive phenotype. In human endometrial samples, CD98 was the only molecule studied whose expression was restricted to the implantation window in human endometrial tissue. CD98 expression was restricted to the apical surfac…

medicine.medical_specialtyCD98ScienceWomen's Health/Female Subfertility and Gynecological EndocrinologyIntegrinFusion Regulatory Protein-1EndometriumEndometriumInternal medicineCell AdhesionmedicineHumansBlastocystCell adhesionMultidisciplinarybiologyQRAdhesionOvum implantationEmbryonic stem cellEpitheliumPhysiology/Reproductive PhysiologyCell biologyCell Biology/Cell AdhesionBlastocystEndocrinologymedicine.anatomical_structureembryonic structuresbiology.proteinMedicineFemaleEndometriResearch ArticleImplantació de l'ou
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