The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Plcl1  -  phospholipase C-like 1

Mus musculus

Synonyms: C230017K02Rik, Inactive phospholipase C-like protein 1, PLC-L, PLC-L1, PLCE, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on Plcl1


Biological context of Plcl1

  • In contrast, PLC activities in brain cortex samples from PRIP-1-/- mice were not different from those in the wild type mice, indicating that the hydrolysis of Ins(1,4,5)P3 is enhanced in cells from PRIP-1-/- mice [2].
  • Together, these results suggest an essential role for PRIP-1 in controlling GABA(A) receptor activity via regulating subunit phosphorylation and thereby the efficacy of neuronal inhibition mediated by these receptors [3].
  • PRIP, a novel Ins(1,4,5)P3 binding protein, functional significance in Ca2+ signaling and extension to neuroscience and beyond [4].

Anatomical context of Plcl1

  • Histological examination of all the implants with haematoxylin and eosin staining, masson trichrome staining, SM alpha-actin antibody, and CM-DiI labeling confirmed that the regular morphology and biofunction of the SMCs seeded and the expression of the vascular smooth muscle matrices in PLCL scaffolds [5].
  • Such a high elastic property and proper biocompatibility to SMCs of PLCL scaffolds prepared in this study will be very useful to engineer SM-containing tissues such as blood vessels under mechanically dynamic environments (mechano-active tissue engineering) [6].
  • DN1-3 (Zn-alpha2-glycoprotein, vascular endothelial growth factor receptor [VEGFR]-2, and lactate dehydrogenase [LDH]) were overexpressed and DN7-8 (peroxisome proliferator-activated receptor [PPAR]-interacting protein [PRIP], unknown) were underexpressed in the KK/Ta mouse kidney [7].

Associations of Plcl1 with chemical compounds

  • PRIP-1 was isolated as a novel inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] binding protein with a domain organization similar to phospholipase C-delta1 (PLC-delta1) but lacking the enzymatic activity [2].
  • In the present study, we investigated the effects of pentylenetetrazol (PTZ), a chemical convulsant that interacts with the GABA(A) receptor, in mice lacking the phospholipase C (PLC)-related inactive protein-1 (PRIP-1) [8].
  • Finally, phosphorylation of PRIP-1 on threonine 94 facilitated the dissociation of PP1alpha-PRIP-1 complexes, providing a local mechanism for the activation of PP1alpha [3].
  • The implanted PLCL scaffolds displayed a slow degradation on time, where caprolactone units were faster degraded than lactide did [5].

Other interactions of Plcl1

  • In wild-type animals, robust phosphorylation and functional modulation of GABA(A) receptors containing beta3 subunits by cAMP-dependent protein kinase was evident, which was diminished in PRIP-1-/- mice [3].
  • Here, we examined the role for phospholipase C-related inactive protein type 1 (PRIP-1), which binds and inactivates protein phosphatase 1alpha (PP1alpha) in facilitating GABA(A) receptor phospho-dependent regulation using PRIP-1-/- mice [3].

Analytical, diagnostic and therapeutic context of Plcl1


  1. Role of phospholipase C-L2, a novel phospholipase C-like protein that lacks lipase activity, in B-cell receptor signaling. Takenaka, K., Fukami, K., Otsuki, M., Nakamura, Y., Kataoka, Y., Wada, M., Tsuji, K., Nishikawa, S., Yoshida, N., Takenawa, T. Mol. Cell. Biol. (2003) [Pubmed]
  2. Role of PRIP-1, a novel Ins(1,4,5)P3 binding protein, in Ins(1,4,5)P3-mediated Ca2+ signaling. Harada, K., Takeuchi, H., Oike, M., Matsuda, M., Kanematsu, T., Yagisawa, H., Nakayama, K.I., Maeda, K., Erneux, C., Hirata, M. J. Cell. Physiol. (2005) [Pubmed]
  3. GABAA receptor phospho-dependent modulation is regulated by phospholipase C-related inactive protein type 1, a novel protein phosphatase 1 anchoring protein. Terunuma, M., Jang, I.S., Ha, S.H., Kittler, J.T., Kanematsu, T., Jovanovic, J.N., Nakayama, K.I., Akaike, N., Ryu, S.H., Moss, S.J., Hirata, M. J. Neurosci. (2004) [Pubmed]
  4. PRIP, a novel Ins(1,4,5)P3 binding protein, functional significance in Ca2+ signaling and extension to neuroscience and beyond. Kanematsu, T., Takeuchi, H., Terunuma, M., Hirata, M. Mol. Cells (2005) [Pubmed]
  5. In vivo biocompatibilty and degradation behavior of elastic poly(L-lactide-co-epsilon-caprolactone) scaffolds. Jeong, S.I., Kim, B.S., Kang, S.W., Kwon, J.H., Lee, Y.M., Kim, S.H., Kim, Y.H. Biomaterials (2004) [Pubmed]
  6. Manufacture of elastic biodegradable PLCL scaffolds for mechano-active vascular tissue engineering. Jeong, S.I., Kim, S.H., Kim, Y.H., Jung, Y., Kwon, J.H., Kim, B.S., Lee, Y.M. Journal of biomaterials science. Polymer edition. (2004) [Pubmed]
  7. Altered mouse cholinephosphotransferase gene expression in kidneys of type 2 diabetic KK/TA mouse. Gohda, T., Tanimoto, M., Shiina, K., Ito, T., Kobayashi, M., Hagiwara, S., Kaneko, S., Makita, Y., Funabiki, K., Horikoshi, S., Tomino, Y. Metab. Clin. Exp. (2004) [Pubmed]
  8. Hypersensitivity to pentylenetetrazol-induced convulsion in mice lacking the PLC-related inactive protein-1. Yamaguchi, T., Kubota, T., Kanematsu, T., Nakayama, K., Hirata, M., Yamamoto, T. Brain Res. (2004) [Pubmed]
WikiGenes - Universities