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Review of C-type lectin-like receptor 2 (show CLEC1B Proteins) and podoplanin interactions [review]
PDPN acts as an oncogene (show RAB1A Proteins) to promote hypopharyngeal cancer cell viability, migration and invasion. miR (show MLXIP Proteins)-203 directly targets PDPN to suppress its expression, thus exerting inhibitory effects on cancer metastasis.
podoplanin expression in cancer-related fibrotic tissues is associated with a poor prognosis, especially in patients with large tumors or lymph node metastases.
Data show that podoplanin (PDPN), CD106 (VCAM-1 (show VCAM1 Proteins)) and CD248 (show CD248 Proteins) protein were increased in diseased compared to healthy tendon cells.
Increased expression of twist/podoplanin in ductal breast carcinoma was associated with shorter patient survival.
Study showed that podoplanin increases the motility of fibroblasts and facilitates their interaction with endothelial cells. This, respectively, favors movement of fibroblasts into the breast tumor stroma and affects tumor angiogenesis, what creates a favorable microenvironment for breast cancer progression.
Data suggest that podoplanin (PDPN) might be a pathogenetic determinant of malignant pleural mesothelioma (MPM) dissemination and aggressive growth and may thus be an ideal therapeutic target.
high podoplanin expression in primary brain tumors induces platelet aggregation, correlates with hypercoagulability, and is associated with increased risk of VTE
This article provides evidence supporting the implication of podoplanin expression as a marker of bad prognosis of cutaneous squamous cell carcinoma
A possible crosstalk between epithelial and stromal tumor cells in hepatocellular carcinoma tumor microenvironment may be mediated by podoplanin
these data suggest that the platelet CLEC-2 (show CLEC1B Proteins)-podoplanin signaling axis regulates the severity of lung inflammation in mice and is a possible novel target for therapeutic intervention in patients at risk of developing ARDS.
Describe a bone-specific conditional Pdpn hypomorphic knockout mouse and confirm a role for Pdpn in the attainment of fully elongated osteocyte dendrites.
In podoplanin conditional knockout mice (Wnt1 (show WNT1 Proteins)-Cre;PdpnDelta/Deltamice), the tooth and alveolar bone showed no morphological abnormalities and grow normally, indicating that podoplanin is not critical in the development of the tooth and bone.
Podoplanin expressed by lymphatic vessels prevents postnatal blood filling of the lymphatic vascular system and contributes to efficient dendritic cell migration to the lymph nodes.
Study provides evidence that podoplanin as a novel component of the neuronal machinery underlying neuritogenesis, synaptic plasticity, and hippocampus-dependent memory functions.
This study suggests that ppGalNAc-T13 (show GALNT13 Proteins) contributes to neuronal differentiation through glycosylating and stabilizing PDPN, which provides insights into the regulatory roles of O-glycosylation in mammalian neural development.
Data show that E11/glycoprotein 38(GP38) was up-regulated upon SEMA3A (show SEMA3A Proteins) stimulation, and cyclin-dependent kinase 6 (CDK6 (show CDK6 Proteins)) was down-regulated in a time-dependent manner.
this study uncovers a unique molecular mechanism of lymphangiogenesis in which galectin-8 (show LGALS8 Proteins)-dependent crosstalk among VEGF-C (show VEGFC Proteins), podoplanin and integrin pathways plays a key role.
A reciprocal interaction between CLEC-2 (show CLEC1B Proteins) on megakaryocytes and PDPN on Bone marrow (BM) Fibroblastic reticular cell-like cells contributes to the periarteriolar megakaryopoietic microenvironment in mouse BM.
Data indicate that a mechanism reliant upon blockade of proteasome-mediated E11 destabilization contributes to osteocytogenesis and that this may involve downstream targeting of RhoA (show RHOA Proteins).
These results indicated that PDPN gene plays a significant role in the proliferation and maturation of bovine Sertoli cells.
This gene encodes a type-I integral membrane glycoprotein with diverse distribution in human tissues. The physiological function of this protein may be related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor. The specific function of this protein has not been determined but it has been proposed as a marker of lung injury. Alternatively spliced transcript variants encoding different isoforms have been identified.
, PA2.26 antigen
, glycoprotein 36
, glycoprotein, 36-KD
, lung type I cell membrane associated glycoprotein
, lung type-I cell membrane-associated glycoprotein (T1A-2)
, glycoprotein 38
, transmembrane glycoprotein E11
, E11 antigen epitope
, epithelial cell surface transmembrane protein antigen
, pulmonary type I alveolar epithelial cell transmembrane differentiation marker
, type I cell 40 kDa protein
, mucin-type membrane protein gp40