title: The novel murine Ca2+-binding protein, Scarf, is differentially expressed during epidermal differentiation.
abstract: 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.
authors.affiliation: Developmental Skin Biology Unit, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
authors.forename: Meeyul
authors.initials: M
authors.lastname: Hwang
authors.forename: Maria I
authors.initials: MI
authors.lastname: Morasso
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D015153:Blotting, Western; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism; D002154:Calpain; D002454:Cell Differentiation; D002478:Cells, Cultured; D003001:Cloning, Molecular; D000078404:Epidermal Cells; D004817:Epidermis / Q000378:metabolism; D005786:Gene Expression Regulation; D018507:Gene Expression Regulation, Developmental; D015723:Gene Library; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D007438:Introns; D015603:Keratinocytes / Q000166:cytology / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D016366:Open Reading Frames; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000096:biosynthesis / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D051128:Scavenger Receptors, Class F; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D014018:Tissue Distribution
chemical_list: D002135:Calcium-Binding Proteins; D002147:Calmodulin; D011956:Receptors, Cell Surface; C480165:Scarf2 protein, mouse; D051128:Scavenger Receptors, Class F; C480164:Calm4 protein, mouse; D002154:Calpain; D002118:Calcium