Disease relevance of APBB1IP

• In megakaryocyte-like human erythroleukemia HEL cells, the amount of RARP1 mRNA was high, but it was low in human T-lymphoblastoid Jurkat cells [1].

Psychiatry related information on APBB1IP

• The maximum (extremum) in depolarization (DIAM max 30, 40) and repolarization (RIAM max 35) of body surface isoarea and isointegral (RIIM max) maps was less positive (p<0.001) and the minimum (DIAM min 40) was less negative than in the controls (p<0.05) even in the period free of a panic attack [2].

High impact information on APBB1IP

• Furthermore, siRNA-mediated knockdown of RIAM blocked integrin activation [3].
• Further analysis demonstrated that proline-rich regions of RARP1 are the functional regions regulated for suppression of activator protein1 transactivation [1].
• The retinoic acid-responsive proline-rich protein is identified in promyeloleukemic HL-60 cells [1].
• These data suggest that ATRA-inducible RARP1 selectively affects signal transduction and may contribute to myeloid and megakaryocytic differentiation [1].
• A specific antibody against RARP1 recognized a 110-kDa protein, which accumulates after incubation of HL-60 cells with ATRA [1].

Biological context of APBB1IP

• Transcriptional studies showed that RARP1 expression impaired the transactivation through activator protein1 and serum response-element in all cell lines we checked, whereas it did not affect the transactivation through cAMP-response element in the same cell lines [1].
• RIAM overexpression also induced integrin activation and cell adhesion [4].

Anatomical context of APBB1IP

• In immunohistochemical experiments, strong RARP1 staining was observed in the megakaryocytes of bone marrow and spleen, and heterogeneous stain was seen in thymus [1].
• Overexpression of RIAM induced cell spreading and lamellipodia formation, changes that require actin polymerization [4].
• RIAM knockdown displaced Rap1-GTP from the plasma membrane and abrogated Rap1-induced adhesion [4].
• The repolarization maps can distinguish patients with coronary artery disease and normal echocardiography from healthy persons with a sensitivity of 85% and a specificity of 65% in the case of the isoareal map from the ST segment (RIAM) and 90% and 85%, respectively, in the case of the isointegral map from the whole ST-T segments (RIIM) [5].

Associations of APBB1IP with chemical compounds

• Short-term increases in acetic or propionic acid increased Prel, but were always offset by corresponding changes in Pup to yield the same net P removal as the control reactor [6].
• This minimized Rap-RIAM module was sufficient to target talin to the plasma membrane and to mediate integrin activation, even in the absence of Rap1 activity [7].

Other interactions of APBB1IP

• Thus, RIAM links Rap1 to integrin activation and plays a role in regulating actin dynamics [4].

References