Human cysteine-rich protein. A member of the LIM/double-finger family displaying coordinate serum induction with c-myc

• Published in: The Journal of biological chemistry Vol. 267; no. 13; pp. 9176 - 9184
• Main Authors: Wang, X, Lee, G, Liebhaber, S A, Cooke, N E
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 05.05.1992
• Subjects: 3T3 Cells; Amino Acid Sequence; Animals; Base Sequence; Blood; Blotting, Northern; c-myc; c-myc gene; Cell Cycle; cysteine-rich protein; DNA - genetics; fibroblasts; gene expression; Gene Expression Regulation; Genes, myc; Humans; induction; LIM Domain Proteins; man; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Multigene Family; Nuclear Proteins; Polymerase Chain Reaction; Proteins; Proto-Oncogene Proteins c-myc - genetics; Proto-Oncogene Proteins c-myc - metabolism; Restriction Mapping; RNA - genetics; RNA - metabolism; serum; Transcription, Genetic; Zinc Fingers - genetics
• DOI: 10.1016/S0021-9258(19)50405-7
• ISSN: 0021-9258

We previously reported the structure of the placentally derived human cysteine-rich (h crp) cDNA and demonstrated that it encodes a highly conserved and widely distributed zinc finger-like protein. We now report that the expression of both the mouse and human crp genes is induced as a primary response to serum in quiescent Balb/c 3T3 cells and in human fibroblasts. The profile of this primary response is remarkably parallel to that of c-myc in the Balb/c 3T3 cell line. The structure of the 23.2-kilobase h crp gene demonstrates that it is a member of a gene superfamily encoding proteins sharing a highly characteristic 52-amino acid "LIM/double-finger" motif. The evolutionarily conserved structure of cysteine-rich protein, its structural similarity to a number of developmentally critical proteins, its distinctive tissue distribution, and its primary response to early events in the cell cycle suggest that crp plays an important role in cell function.