LIM and Senescent Cell Antigen-Like Domains 1 (LIMS1) ELISA Kits

Human LIM and Senescent Cell Antigen-Like Domains 1 (LIMS1) interaction partners

1. We found that the LIMS1 locus appeared to encode a minor histocompatibility antigen. Genomic collision at this locus was associated with rejection of the kidney allograft and with production of anti-LIMS1 IgG2 and IgG3.

2. High LIMS1 expression is associated with Neuroblastoma.

3. focal adhesion signaling to actin cytoskeleton is implicated in human laryngeal carcinogenesis and PINCH1 has prognostic significance in the disease.

4. that PINCH-1 may be playing an important role in etiopathogenesis of both subtypes breast cancer

5. Mammalian cells have two functional PINCH proteins, PINCH1 and PINCH2. PINCH not only binds to Nck2 and engages in the signaling of growth factor receptors, but also forms a ternary complex with ILK and parvin (IPP complex).

6. our data suggest an essential role of PINCH1, ILK and ILKAP for the radioresistance of p53-wildtype glioblastoma multiforme cells

7. Data suggest that PINCH1 and Nck2 critically participate in the regulation of cellular radiosensitivity and EGFR function and downstream signaling in a cellular model of human squamous cell carcinoma.

8. Downregulation of PINCH1 is associated with metastatic breast cancer.

9. changes in CSF levels of PINCH appear to correlate with changes in blood CD4 count and with changes in CSF hyperphosphorylated Tau levels

10. two novel genes, galectin 9 and PINCH, were expressed at much higher levels in cancerous lesions than in normal tissues in all the patients with clear-cell carcinoma who were examined

11. PINCH predicts survival in rectal cancer patients with RT, but not in patients without RT. The expression of PINCH may be regulated by radiation and by environmental factors surrounding the cells.

12. PINCH is increased and binds to hp-Tau. These studies address a new mechanism by which AD and HIV may intersect and identify PINCH as a contributing factor to the accumulation of hyperphosphorylated Tau.

13. Pinch-1 mRNA and protein were significantly up-regulated in acute lymphoblastic leukemia and acute myeloid leukemia bone marrow stromal cells compared to normal bone marrow stromal cells (p<0.01).

14. PINCH protein might play an important role in the tumourigenesis and metastasis of gastric adenocarcinoma.

15. PINCH mRNA overexpression in colorectal carcinomas is correlated with VEGF and FAS mRNA expression

16. PINCH may function as a neuron-specific host-mediated response to challenge by HIV-related factors in the CNS.

17. PINCH1 can shuttle into the nucleus from cytoplasm in podocytes, wherein it interacts with WT1 and suppresses podocyte-specific gene expression.

18. Review provides an overview of the current knowledge of the molecular interactions of PINCH with other components of focal adhesions and discusses its potential implication for human heart disease.

19. data reveal how specific domains of PINCH-1 direct two independent pathways: one utilizing ILK to allow cell attachment, and the other recruiting Rsu-1 to activate Rac1 in order to promote cell spreading

20. PINCH staining at the tumour invasive margin was related to survival in poorly differentiated tumours but not in better differentiated tumours, indicating that the impact of PINCH on prognosis was dependent on differentiation status.

Mouse (Murine) LIM and Senescent Cell Antigen-Like Domains 1 (LIMS1) interaction partners

1. findings suggest that PINCH-1 regulates integrin-mediated adhesion of keratinocytes through the interactions with ILK as well as EPLIN.

2. Rsu-1 expression is dramatically decreased in PINCH double knockout mouse livers.

3. PINCH is increased and binds to hp-Tau. These studies address a new mechanism by which AD and HIV may intersect and identify PINCH as a contributing factor to the accumulation of hyperphosphorylated Tau.

4. PINCH-1 inhibits JNK-mediated apoptosis by stabilising the PINCH-1 binding protein RSU-1 and promotes Bcl-2-dependent pro-survival signalling downstream of integrins.

5. Data suggest that the adapter protein PINCH1 critically participates in the regulation of the cellular radiosensitivity of normal and malignant cells similarly under adhesion and suspension conditions.

6. PINCH1 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes.

7. These results provide important evidence for a crucial role of the PINCH-1-ILK-alpha-parvin complex in the control of podocyte adhesion, morphology, and survival.

8. LIM 5 domain of PINCH1 interacts with Rsu-1 in mammalian cells and functions, in part, by altering cell adhesion.

9. The PINCH1 is composed of 5 LIM domains, binds ILK and locates to integrin-mediated adhesion sites, and PINCH1 is for integrin function, actin organization, cell-cell adhesion and endodermal cell survival during the implanting of mouse embryos.

10. PICH1, Ilk and alpha-parvin form a complex to costameres in neonatal mouse ventricular myocytes. This complex is stimulated by fibronectins and phenylephrine, and by both by drug synergism, to regulate cardiac myocyte hypertrophy.

11. LIM1 domain only of either PINCH1 or PINCH2 can prevent ILK degradation despite their failure to localize to focal adhesions.

12. Transactivation studies and chromatin immunoprecipitation implicate Lims1 as a direct target of NF-E2 regulation

13. Pinch1 plays an essential role in neural crest development, in part through transforming growth factor-beta signaling.

14. mechanical stretch prevented vascular smooth muscle from apoptosis via a mechanism that involves alphaVbeta3 integrin expression, stabilization of PINCH-1, and remodeling of the cytoskeleton.

15. Results describe the roles of the ILK-PINCH-parvin triad proteins in the maturation of focal adhesions.

16. Absence of either PINCH1 or PINCH2 in myocardium leads to exacerbated cardiac injury and deterioration in cardiac function after myocardial infarction.