Expression, regulation, and function of the SPR family of proteins
- 1 June 1999
- journal article
- review article
- Published by Springer Nature in Cell Biochemistry and Biophysics
- Vol. 30 (2) , 243-265
- https://doi.org/10.1007/bf02738069
Abstract
The small, proline-rich (SPR) genes consist of three subclasses closely linked on human chromosome 1, a region referred to as the epidermal differentiation complex. SPR genes consist of two exons, with the second exon containing the entire open reading frame. SPRs are expressed in all squamous tissues of the skin, scalp, foot pad, vaginal epithelia, and most of the epithelial lining of the digestive tract, including the lip, tongue, esophagus, and forestomach. Although SPR1 is absent in normal mucociliary epithelium of the respiratory tract, epithelia that undergo squamous differentiation in response to vitamin-A deficiency or to injury owing to exposure to environmental toxicants express SPR1. High levels of SPR1 are detected in various diseases and cancers of the skin or respiratory epithelia and in nonkeratinizing papillary adenocarcinomas. SPR expression can be regulated by transcriptional factors, by posttranscriptional factors, or by factors that affect SPR1 mRNA translation or protein turnover. Furthermore, regulation can be affected by the state of cell proliferation. The presence of SPR1 in most of these epithelia, and the absence of SPR3 in normal skin, suggest that these subclasses have distinct functions. Various approaches to the study of the cross-linked envelope (CE) components in identifying SPR1 and SPR2 and in suggesting that SPRs are one of the precursor proteins of the CE. However, expression of SPR1 in nonsquamous tissues and cell lines indicates a function not associated with squamous differentiation. Several studies have demonstrated that SPR1 antibodies react with nuclear proteins and that SPR1 is expressed in cells before entering the G0 phase of the cell cycle. Future studies should clarify the role of SPRs by modifying their contents in CE, and should identify SPR-associated proteins to clariy the cell growth-related role of SPR1.Keywords
This publication has 40 references indexed in Scilit:
- Genes Encoding Structural Proteins of Epidermal Cornification and S100 Calcium-Binding Proteins Form a Gene Complex (“Epidermal Differentiation Complex”) on Human Chromosome 1q21Journal of Investigative Dermatology, 1996
- Differentiation-associated localization of small prolne-rich rotein in normal and diseased human skinBritish Journal of Dermatology, 1996
- Cloning and Regulation of Cornifin β, a New Member of the Cornifin/spr FamilyPublished by Elsevier ,1996
- Molecular Characterization and Evolution of the SPRR Family of Keratinocyte Differentiation Markers Encoding Small Proline-Rich ProteinsGenomics, 1993
- Cornifin, a cross-linked envelope precursor in keratinocytes that is down-regulated by retinoids.Proceedings of the National Academy of Sciences, 1992
- A common origin for cornified envelope proteins?Nature Genetics, 1992
- An Unusual Expression of a Squamous Cell Marker, Small Proline-rich Protein Gene, in Tracheobronchial Epithelium: Differential Regulation and Gene MappingAmerican Journal of Respiratory Cell and Molecular Biology, 1992
- Induction in the expression of an unusual proline-rich protein by pig tracheal surface epithelial cells maintained in primary cultureBiochemical and Biophysical Research Communications, 1990
- Isolation, characterization, and UV-stimulated expression of two families of genes encoding polypeptides of related structure in human epidermal keratinocytes.Molecular and Cellular Biology, 1988
- Molecular cloning of gene sequences regulated during squamous differentiation of tracheal epithelial cells and controlled by retinoic acid.Molecular and Cellular Biology, 1987