S100A2

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Protein-coding gene in the species Homo sapiens

title: "S100A2" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["s100-proteins"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/s100-proteins" source: "https://en.wikipedia.org/wiki/S100A2" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

S100 calcium-binding protein A2 (S100A2) is a protein that in humans is encoded by the S100A2 gene and it is located on chromosome 1q21 with other S100 proteins.

Tissue and subcellular distribution

S100A2, also known as CaN19 or S100L was first isolated from bovine lung tissue. However, in human tissue it was discovered several years later, in the mammary epithelial cells. Under normal circumstances it is highly expressed in human lungs, prostate, kidneys, hair follicles and salivary and mammary glands. S100A2 is predominantly found in the nucleus, which is not very common in other S100 proteins. Moreover, it can also be found in the cytoplasm, and its distribution is rather diffuse. Its occurrence in cytoplasm is most likely dependent on calcium levels in the cell. In the extracellular environment, it can be found as a homodimer in vivo and in vitro, but it also exists in monomeric, polymeric and multimeric forms. In multimeric form, it functions as a RAGE receptor ligand.

Function

S100A2 is important in cytoskeleton organization. Also, S100A2 is induced by p53, which it interacts and participates in the transcription of p21. It also plays a role in differentiation, regeneration of tissues and healing and it was shown it attract eosinophils by chemotaxis.

Clinical significance

Its expression is reduced in many types of cancer, thereby distinguishing the cancerous expression profile of the other proteins of the S100 group. It has been reported that S100A2 is downregulated in lung, kidney, prostate cancer and melanoma. Chromosomal rearrangements and altered expression of this gene have also been implicated in breast cancer. In addition, its decline is associated with poor prognosis, disease progression, increased occurrence of metastasis and increased patient mortality. Although in most cancers it has been found in reduced levels, there are studies that show that in some cases it is overproduced.

References

References

  1. (July 1993). "Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E". Proceedings of the National Academy of Sciences of the United States of America.
  2. (February 1989). "Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution". The Journal of Cell Biology.
  3. (April 1991). "Positive selection of candidate tumor-suppressor genes by subtractive hybridization". Proceedings of the National Academy of Sciences of the United States of America.
  4. (October 2011). "S100A2 in cancerogenesis: a friend or a foe?". Amino Acids.
  5. (November 2002). "Differential responses of S100A2 to oxidative stress and increased intracellular calcium in normal, immortalized, and malignant human keratinocytes". The Journal of Investigative Dermatology.
  6. (November 1996). "Expression pattern of S100 calcium-binding proteins in human tumors". International Journal of Cancer.
  7. (August 2005). "The calcium-binding protein S100A2 interacts with p53 and modulates its transcriptional activity". The Journal of Biological Chemistry.
  8. (September 2000). "Biochemical characterization of S100A2 in human keratinocytes: subcellular localization, dimerization, and oxidative cross-linking". The Journal of Investigative Dermatology.
  9. Martonosi, Anthony N.. (1983). "The Regulation of Cytoplasmic Ca2+ Concentration in Muscle and Nonmuscle Cells". Elsevier.
  10. (May 2008). "Transcriptional activation of the tumor suppressor and differentiation gene S100A2 by a novel p63-binding site". Nucleic Acids Research.
  11. (April 2010). "Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73". Oncogene.
  12. (July 1989). "Enhancement of wound healing by topical treatment with epidermal growth factor". The New England Journal of Medicine.
  13. (March 1996). "Novel specific chemtactic receptor for S100L protein on guinea pig eosinophils". Biochemical and Biophysical Research Communications.
  14. (August 1997). "Differential expression patterns of S100A2, S100A4 and S100A6 during progression of human malignant melanoma". International Journal of Cancer.
  15. (January 2003). "Differential expression of S100A2 and S100A4 during progression of human prostate adenocarcinoma". Journal of Clinical Oncology.
  16. (December 2000). "Expression of calcium-binding protein S100A2 in breast lesions". British Journal of Cancer.
  17. "Entrez Gene: S100A2 S100 calcium binding protein A2".
  18. (December 2005). "S100A2 expression as a predictive marker for late cervical metastasis in stage I and II invasive squamous cell carcinoma of the oral cavity". Oncology Reports.
  19. (August 2005). "Overexpression of S100A2 protein as a prognostic marker for patients with stage I non small cell lung cancer". International Journal of Cancer.
  20. (March 2016). "Overexpression of the S100A2 protein as a prognostic marker for patients with stage II and III colorectal cancer". International Journal of Oncology.

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