S100
S100 protein is a family of low molecular weight proteins found in vertebrates characterized by two calcium binding sites of the helix-loop-helix ("EF-hand type") conformation. There are at least 21 different types of S100 proteins. The name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. The largest amount of S100 proteins is found in the brain, where they are only present in glial cells and certain neurons. Also, S100 proteins are present in the melanocytes, Langerhans cells, histiocytes, myoepithelial cells, and chondrocytes.
Function[edit | edit source]
S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response.
Clinical significance[edit | edit source]
Several members of the S100 protein family are useful as markers for certain tumors and epidermal differentiation. It can also be a marker for certain neurons.
See also[edit | edit source]
- S100A1
- S100A2
- S100A3
- S100A4
- S100A5
- S100A6
- S100A7
- S100A8
- S100A9
- S100A10
- S100A11
- S100A12
- S100A13
- S100A14
- S100A15
- S100A16
- S100B
- S100P
- S100Z
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD