Asset Details
Do you wish to reserve the book?
S100 proteins in cancer
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
S100 proteins in cancer
Do you wish to request the book?
S100 proteins in cancer
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
S100 proteins in cancer
2015
Overview
Key Points
The S100 protein family is composed of 21 members that exhibit a high degree of structural similarity, but are not functionally interchangeable.
S100 family members function as intracellular Ca
2+
sensors and extracellular factors.
Chromosomal alterations, mutations and/or translocations in
S100
genes are rare in human cancers. Nonetheless, dysregulation of multiple S100 proteins is a common occurrence in individual human cancers and most often involves upregulation.
Each human cancer exhibits a distinctive S100 protein profile that can be both stage-specific and subtype-specific, as well as facilitate diagnosis, prognosis and/or drug response.
The modulation of S100 expression is a common downstream event in S100 signalling cascades, resulting in feedback loops that can sustain and exacerbate tumour progression.
The most common strategies for inhibiting S100 proteins exploit small molecules that block the hydrophobic cleft required for S100 proteins to interact with targets and elicit biological effects.
Inhibitors of two family members, S100B and S100A9, are in clinical trials for melanoma and prostate cancer, respectively.
The S100 family of proteins modulates cellular responses by acting both as intracellular Ca
2+
sensors and as extracellular factors. Expression of several members of this family is dysregulated in cancer, and each cancer shows a unique S100 protein profile or signature. In this Review, Anne Bresnick and colleagues highlight new findings regarding the role of S100 proteins in cancer diagnosis and treatment.
In humans, the S100 protein family is composed of 21 members that exhibit a high degree of structural similarity, but are not functionally interchangeable. This family of proteins modulates cellular responses by functioning both as intracellular Ca
2+
sensors and as extracellular factors. Dysregulated expression of multiple members of the S100 family is a common feature of human cancers, with each type of cancer showing a unique S100 protein profile or signature. Emerging
in vivo
evidence indicates that the biology of most S100 proteins is complex and multifactorial, and that these proteins actively contribute to tumorigenic processes such as cell proliferation, metastasis, angiogenesis and immune evasion. Drug discovery efforts have identified leads for inhibiting several S100 family members, and two of the identified inhibitors have progressed to clinical trials in patients with cancer. This Review highlights new findings regarding the role of S100 family members in cancer diagnosis and treatment, the contribution of S100 signalling to tumour biology, and the discovery and development of S100 inhibitors for treating cancer.
