Cell-type specific proteins

Induction ofmRNA for pS2 and secretion of cell-type-specific proteins. pS2 was measured in the culture medium of MCF7 cells with the ELSA-pS2 immunoradiometric assay (CIS Bio International, Gif-sur-Yvette, France). Cells were subcultured in 24-well plates for 144 h in 10% CDHuS. The culture medium was centrifuged at 1200g for 10 min to eliminate floating and detached cells. Results are expressed as ng of secreted protein per million cells. The relative-induced protein potency (RIPP) was calculated as 100 X the ratio between the dose of E2 and that of the chemical needed to produce maximal expression of cell-type-specific proteins (pS2). 

Intermediate filaments are present in most animal cells. They are composed of more than 50 proteins which are expressed in a cell-type specific manner. Their diameter is about 10 nm and thus between those of the larger microtubules and the smaller F-actin. They form scaffolds and networks in the cyto- and nucleoplasm. 

Syndecans are transmembrane proteins, which are modified by the addition of heparan sulphate glycos-aminoglycan (GAG) chains and other sugars. Syndecans bind a wide variety of different ligands via their heparan sulphate chains. Binding specificities may vary depending on cell-type specific modifications of the heparan sulphate chains. 

Specific transcription factors bind to enhancer regions or, in a few cases, to silencers and mod-ciate the formation of the initiation complex, thus regulating the rate of initiation of transcription. Each gene contains a variety of enhancer or silencer sequences in its regulatory region. The exact combination of specific transcription factors available (and active) in a particular cell at a particular time determines which genes will be transcribed at what rates, because specific transcription factors are proteins, their expression can be cell-type specific.. Additionally, hormones may regulate the activity of some specific transcription factors. Examples include steroid receptors and the CREB protein. 

Shih, M., and Malbon, C. C. (1994) Oligodeoxynucleotides antisense to mRNA encoding protein kinase A, protein kinase C, and beta-adrenergic receptor kinase reveal distinctive cell-type-specific roles in agonist-induced desensitization. Proc. Natl. Acad. Sci. U. S. A. 91, 12193-12197. 

The adenoviruses contain at least three protein moieties, and certain types are capable of inducing one or more new host antigens, such as tumor (T) antigens, the chemistry of which is presently unknown. The viial proteins can be separated by gel diffusion and correlated with results obtained by complement fixation. One moiety is the toxic protein that causes the host cell to degenerate. Another corresponds to the group antigen common to all 31 types of adenoviruses and the third is the type-specific protein. 

Wettschureck, N., and Offermanns, S. (2005). Mammalian G proteins and their cell type specific functions. Physiol. Rev. 85, 1159-1204. 

The cortical region of many cells is enriched in actin and associated actin-binding proteins, which function in motility, cell shape maintenance, and membrane protein distribution in polarized cells. In some cases, discrete structures anchor actin to the membrane, as is the case for intercellular adherens junctions and cell-substrate focal contacts. In certain special cell types, the fundamental blueprint for an adherens junction is taken to a new structural level, serving as scaffolding for cell-type specific complexes, such as the dystrophin-associated protein complex (DPC) in striated muscle. Although for years morphological studies have described a close association with IF with the actin-rich cortex, recent advances in methods to study protein-protein interactions have provided new insight into the intimate structural and functional relationship between IFs and these membrane domains. 

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