| First Author | Hwang M | Year | 2003 |
| Journal | J Biol Chem | Volume | 278 |
| Issue | 48 | Pages | 47827-33 |
| PubMed ID | 12970338 | Mgi Jnum | J:86731 |
| Mgi Id | MGI:2681382 | Doi | 10.1074/jbc.M306561200 |
| Citation | Hwang M, et al. (2003) The novel murine Ca2+-binding protein, Scarf, is differentially expressed during epidermal differentiation. J Biol Chem 278(48):47827-33 |
| abstractText | Calcium (Ca2+) signaling-dependent systems, such as the epidermal differentiation process, must effectively respond to variations in Ca2+ concentration. Members of the Ca2+-binding proteins play a central function in the transduction of Ca2+ signals, exerting their roles through a Ca2+-dependent interaction with their target proteins, spatially and temporally. By performing a suppression subtractive hybridization screen we identified a novel mouse gene, Scarf (skin calmodulin-related factor), which has homology to calmodulin (CaM)-like Ca2+-binding protein genes and is exclusively expressed in differentiating keratinocytes in the epidermis. The Scarf open reading frame encodes a 148-amino acid protein that contains four conserved EF-hand motifs (predicted to be Ca2+-binding domains) and has homology to mouse CaM, human CaM-like protein, hClp, and human CaM-like skin protein, hClsp. The functionality of Scarf EF-hand domains was assayed with a radioactive Ca2+-binding method. By Southern blot and computational genome sequence analysis, a highly related gene, Scarf2, was found 15 kb downstream of Scarf on mouse chromosome 13. The functional Scarf Ca2+-binding domains suggest a role in the regulation of epidermal differentiation through the control of Ca2+-mediated signaling. |
