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Journal articles on the topic 'S100 proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Zimmer, Danna B., and David J. Weber. "The Calcium-Dependent Interaction of S100B with Its Protein Targets." Cardiovascular Psychiatry and Neurology 2010 (August 17, 2010): 1–17. http://dx.doi.org/10.1155/2010/728052.

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S100B is a calcium signaling protein that is a member of the S100 protein family. An important feature of S100B and most other S100 proteins (S100s) is that they often bind Ca2+ ions relatively weakly in the absence of a protein target; upon binding their target proteins, Ca2+-binding then increases by as much as from 200- to 400-fold. This manuscript reviews the structural basis and physiological significance of increased Ca2+-binding affinity in the presence of protein targets. New information regarding redundancy among family members and the structural domains that mediate the interaction o

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2

Kazakov, Alexey S., Alexander D. Sofin, Nadezhda V. Avkhacheva, et al. "Interferon Beta Activity Is Modulated via Binding of Specific S100 Proteins." International Journal of Molecular Sciences 21, no. 24 (2020): 9473. http://dx.doi.org/10.3390/ijms21249473.

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Interferon-β (IFN-β) is a pleiotropic cytokine used for therapy of multiple sclerosis, which is also effective in suppression of viral and bacterial infections and cancer. Recently, we reported a highly specific interaction between IFN-β and S100P lowering IFN-β cytotoxicity to cancer cells (Int J Biol Macromol. 2020; 143: 633–639). S100P is a member of large family of multifunctional Ca2+-binding proteins with cytokine-like activities. To probe selectivity of IFN-β—S100 interaction with respect to S100 proteins, we used surface plasmon resonance spectroscopy, chemical crosslinking, and crysta

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3

Zeng, Meng-Lu, Xian-Jin Zhu, Jin Liu, et al. "An Integrated Bioinformatic Analysis of the S100 Gene Family for the Prognosis of Colorectal Cancer." BioMed Research International 2020 (November 26, 2020): 1–15. http://dx.doi.org/10.1155/2020/4746929.

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Background. S100 family genes exclusively encode at least 20 calcium-binding proteins, which possess a wide spectrum of intracellular and extracellular functions in vertebrates. Multiple lines of evidences suggest that dysregulated S100 proteins are associated with human malignancies including colorectal cancer (CRC). However, the diverse expression patterns and prognostic roles of distinct S100 genes in CRC have not been fully elucidated. Methods. In the current study, we analyzed the mRNA expression levels of S100 family genes and proteins and their associations with the survival of CRC pati

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Verma, Rachna, Priyanka Verma, Snehil Budhwar, and Kiran Singh. "S100 proteins." Indian Journal of Medical Research 148, Suppl 1 (2018): S100—S106. https://doi.org/10.4103/ijmr.ijmr_494_18.

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S100 proteins are calcium (Ca2+)-binding proteins and these have an important function in progression, manifestation and therapeutic aspects of various inflammatory, metabolic and neurodegenerative disorders. Based on their involvement in intracellular or extracellular regulatory effects, S100 proteins are classified into three subgroups: one subgroup is specialized in exerting only intracellular effects, other performs both intracellular and extracellular functions and the third subgroup members only display extracellular regulatory effects. S100 proteins are expressed particularly in vertebr

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Kazakov, Alexey S., Evgenia I. Deryusheva, Maria E. Permyakova, et al. "Calcium-Bound S100P Protein Is a Promiscuous Binding Partner of the Four-Helical Cytokines." International Journal of Molecular Sciences 23, no. 19 (2022): 12000. http://dx.doi.org/10.3390/ijms231912000.

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S100 proteins are multifunctional calcium-binding proteins of vertebrates that act intracellularly, extracellularly, or both, and are engaged in the progression of many socially significant diseases. Their extracellular action is typically mediated by the recognition of specific receptor proteins. Recent studies indicate the ability of some S100 proteins to affect cytokine signaling through direct interaction with cytokines. S100P was shown to be the S100 protein most actively involved in interactions with some four-helical cytokines. To assess the selectivity of the S100P protein binding to f

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Kazakov, Alexey S., Evgenia I. Deryusheva, Andrey S. Sokolov, et al. "Erythropoietin Interacts with Specific S100 Proteins." Biomolecules 12, no. 1 (2022): 120. http://dx.doi.org/10.3390/biom12010120.

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Erythropoietin (EPO) is a clinically significant four-helical cytokine, exhibiting erythropoietic, cytoprotective, immunomodulatory, and cancer-promoting activities. Despite vast knowledge on its signaling pathways and physiological effects, extracellular factors regulating EPO activity remain underexplored. Here we show by surface plasmon resonance spectroscopy, that among eighteen members of Ca2+-binding proteins of the S100 protein family studied, only S100A2, S100A6 and S100P proteins specifically recognize EPO with equilibrium dissociation constants ranging from 81 nM to 0.5 µM. The inter

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Kazakov, Alexey S., Evgenia I. Deryusheva, Victoria A. Rastrygina, et al. "Interaction of S100A6 Protein with the Four-Helical Cytokines." Biomolecules 13, no. 9 (2023): 1345. http://dx.doi.org/10.3390/biom13091345.

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S100 is a family of over 20 structurally homologous, but functionally diverse regulatory (calcium/zinc)-binding proteins of vertebrates. The involvement of S100 proteins in numerous vital (patho)physiological processes is mediated by their interaction with various (intra/extra)cellular protein partners, including cell surface receptors. Furthermore, recent studies have revealed the ability of specific S100 proteins to modulate cell signaling via direct interaction with cytokines. Previously, we revealed the binding of ca. 71% of the four-helical cytokines via the S100P protein, due to the pres

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Melville, Zephan, Ehson Aligholizadeh, Laura E. McKnight, Dylan J. Weber, Edwin Pozharski, and David J. Weber. "X-ray crystal structure of human calcium-bound S100A1." Acta Crystallographica Section F Structural Biology Communications 73, no. 4 (2017): 215–21. http://dx.doi.org/10.1107/s2053230x17003983.

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S100A1 is a member of the S100 family of Ca2+-binding proteins and regulates several cellular processes, including those involved in Ca2+signaling and cardiac and skeletal muscle function. In Alzheimer's disease, brain S100A1 is overexpressed and gives rise to disease pathologies, making it a potential therapeutic target. The 2.25 Å resolution crystal structure of Ca2+-S100A1 is solved here and is compared with the structures of other S100 proteins, most notably S100B, which is a highly homologous S100-family member that is implicated in the progression of malignant melanoma. The observed stru

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Koltzscher, Max, Claudia Neumann, Simone König, and Volker Gerke. "Ca2+-dependent Binding and Activation of Dormant Ezrin by Dimeric S100P." Molecular Biology of the Cell 14, no. 6 (2003): 2372–84. http://dx.doi.org/10.1091/mbc.e02-09-0553.

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S100 proteins are EF hand type Ca2+ binding proteins thought to function in stimulus-response coupling by binding to and thereby regulating cellular targets in a Ca2+-dependent manner. To isolate such target(s) of the S100P protein we devised an affinity chromatography approach that selects for S100 protein ligands requiring the biologically active S100 dimer for interaction. Hereby we identify ezrin, a membrane/F-actin cross-linking protein, as a dimer-specific S100P ligand. S100P-ezrin complex formation is Ca2+ dependent and most likely occurs within cells because both proteins colocalize at

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Mandarino, Angelo, Swetha Thiyagarajan, Allana C. F. Martins, Roberto da Silva Gomes, Stefan W. Vetter, and Estelle Leclerc. "S100s and HMGB1 Crosstalk in Pancreatic Cancer Tumors." Biomolecules 13, no. 8 (2023): 1175. http://dx.doi.org/10.3390/biom13081175.

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Pancreatic cancer remains a disease that is very difficult to treat. S100 proteins are small calcium binding proteins with diverse intra- and extracellular functions that modulate different aspects of tumorigenesis, including tumor growth and metastasis. High mobility group box 1 (HMGB1) protein is a multifaceted protein that also actively influences the development and progression of tumors. In this study, we investigate the possible correlations, at the transcript level, between S100s and HMGB1 in pancreatic cancer. For this purpose, we calculated Pearson’s correlations between the transcrip

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Fuh, Kenneth F., Jessica Withell, Robert D. Shepherd, and Kristina D. Rinker. "Fluid Flow Stimulation Modulates Expression of S100 Genes in Normal Breast Epithelium and Breast Cancer." Cellular and Molecular Bioengineering 15, no. 1 (2021): 115–27. http://dx.doi.org/10.1007/s12195-021-00704-w.

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Abstract Introduction S100 proteins are intracellular calcium ion sensors that participate in cellular processes, some of which are involved in normal breast functioning and breast cancer development. Despite several S100 genes being overexpressed in breast cancer, their roles during disease development remain elusive. Human mammary epithelial cells (HMECs) can be exposed to fluid shear stresses and implications of such interactions have not been previously studied. The goal of this study was to analyze expression profiles of S100 genes upon exposing HMECs to fluid flow. Methods HMECs and brea

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Makino, Yurika, Shinya Munakata, Takae Ueyama, et al. "Effects of Receptor for Advanced Glycation End-Products (RAGE) Signaling on Intestinal Ischemic Damage in Mice." European Surgical Research 60, no. 5-6 (2019): 239–47. http://dx.doi.org/10.1159/000504751.

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Objective: Superior mesenteric artery ischemia and nonocclusive mesenteric ischemia are representative diseases of the vascular emergency known as irreversible transmural intestinal necrosis (ITIN). The receptor for advanced glycation end-products (RAGE) belongs to the immunoglobulin superfamily of extracellular ligands, which also includes high-mobility group box 1 (HMGB-1) and proteins of the S100 family. The HMGB-1 ligands have been implicated in the pathogenesis of various inflammatory disorders. This study was designed to investigate the relation between RAGE and ITIN in a murine acute in

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Kazakov, Alexey S., Alexander D. Sofin, Nadezhda V. Avkhacheva та ін. "Interferon-β Activity Is Affected by S100B Protein". International Journal of Molecular Sciences 23, № 4 (2022): 1997. http://dx.doi.org/10.3390/ijms23041997.

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Interferon-β (IFN-β) is a pleiotropic cytokine secreted in response to various pathological conditions and is clinically used for therapy of multiple sclerosis. Its application for treatment of cancer, infections and pulmonary diseases is limited by incomplete understanding of regulatory mechanisms of its functioning. Recently, we reported that IFN-β activity is affected by interactions with S100A1, S100A4, S100A6, and S100P proteins, which are members of the S100 protein family of multifunctional Ca2+-binding proteins possessing cytokine-like activities (Int J Mol Sci. 2020;21(24):9473). Here

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Smith, Steven P., and Gary S. Shaw. "A change-in-hand mechanism for S100 signalling." Biochemistry and Cell Biology 76, no. 2-3 (1998): 324–33. http://dx.doi.org/10.1139/o98-062.

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S100 proteins are a group of small dimeric calcium-binding proteins making up a large subclass of the EF-hand family of calcium-binding proteins. Members of this family of proteins have been proposed to act as intracellular calcium modulatory proteins in a fashion analogous to that of the EF-hand sensor proteins troponin-C and calmodulin. Recently, NMR spectroscopy has provided the three-dimensional structures of the S100 family members S100A6 and S100B in both the apo- and calcium-bound forms. These structures have allowed for the identification of a novel calcium-induced conformational chang

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15

Zimmer, D. B., and L. J. Van Eldik. "Tissue distribution of rat S100 alpha and S100 beta and S100-binding proteins." American Journal of Physiology-Cell Physiology 252, no. 3 (1987): C285—C289. http://dx.doi.org/10.1152/ajpcell.1987.252.3.c285.

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To understand the physiological role of the calcium-binding proteins S100 alpha and S100 beta, it is necessary to determine the distribution of these proteins and detect their intracellular targets in various tissues. The distribution of immunoreactive S100 alpha and S100 beta in various rat tissues was examined by radioimmunoassay. All tissues examined contained detectable S100, but the S100 beta/S100 alpha ratio in each tissue differed. Brain, adipose, and testes contained 18- to 40-fold more S100 beta than S100 alpha; skin and liver contained approximately equivalent amounts and kidney, spl

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16

Emberley, Ethan D., Leigh C. Murphy, and Peter H. Watson. "S100 proteins and their influence on pro-survival pathways in cancer." Biochemistry and Cell Biology 82, no. 4 (2004): 508–15. http://dx.doi.org/10.1139/o04-052.

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The S100 gene family is composed of at least 20 members that share a common structure defined in part by the Ca2+ binding EF-hand motif. These genes which are expressed in a discriminate fashion in specific cells and tissues, have been described to have either an intracellular or extracellular function, or both. S100 proteins are implicated in the immune response, differentiation, cytoskeleton dynamics, enzyme activity, Ca2+ homeostasis and growth. A potential role for S100 proteins in neoplasia stems from these activities and from the observation that several S100 proteins have altered levels

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Donato, R., B. R. Cannon, G. Sorci, et al. "Functions of S100 Proteins." Current Molecular Medicine 13, no. 1 (2013): 24–57. http://dx.doi.org/10.2174/156652413804486214.

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Donato, R., B. R. Cannon, G. Sorci, et al. "Functions of S100 Proteins." Current Molecular Medicine 13, no. 1 (2012): 24–57. http://dx.doi.org/10.2174/1566524011307010024.

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Manev, Hari, and Radmila Manev. "Olanzapine and S100 Proteins." Neuropsychopharmacology 31, no. 11 (2006): 2567. http://dx.doi.org/10.1038/sj.npp.1301186.

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20

石, 梦瑶. "S100 Proteins in Cancer." Advances in Clinical Medicine 14, no. 09 (2024): 71–78. http://dx.doi.org/10.12677/acm.2024.1492430.

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21

Bresnick, Anne R., David J. Weber, and Danna B. Zimmer. "S100 proteins in cancer." Nature Reviews Cancer 15, no. 2 (2015): 96–109. http://dx.doi.org/10.1038/nrc3893.

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22

Xiao, Xuan, Chen Yang, Shun-Lin Qu, et al. "S100 proteins in atherosclerosis." Clinica Chimica Acta 502 (March 2020): 293–304. http://dx.doi.org/10.1016/j.cca.2019.11.019.

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23

Allgöwer, Chantal, Anna-Laura Kretz, Silvia von Karstedt, Mathias Wittau, Doris Henne-Bruns, and Johannes Lemke. "Friend or Foe: S100 Proteins in Cancer." Cancers 12, no. 8 (2020): 2037. http://dx.doi.org/10.3390/cancers12082037.

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S100 proteins are widely expressed small molecular EF-hand calcium-binding proteins of vertebrates, which are involved in numerous cellular processes, such as Ca2+ homeostasis, proliferation, apoptosis, differentiation, and inflammation. Although the complex network of S100 signalling is by far not fully deciphered, several S100 family members could be linked to a variety of diseases, such as inflammatory disorders, neurological diseases, and also cancer. The research of the past decades revealed that S100 proteins play a crucial role in the development and progression of many cancer types, su

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Zimmer, D. B., and L. J. Van Eldik. "Analysis of the calcium-modulated proteins, S100 and calmodulin, and their target proteins during C6 glioma cell differentiation." Journal of Cell Biology 108, no. 1 (1989): 141–51. http://dx.doi.org/10.1083/jcb.108.1.141.

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We have analyzed the levels, subcellular distribution, and target proteins of two calcium-modulated proteins, S100 and calmodulin, in differentiated and undifferentiated rat C6 glioma cells. Undifferentiated and differentiated C6 cells express primarily the S100 beta polypeptide, and the S100 beta levels are four-fold higher in differentiated compared to undifferentiated cells. Double fluorescent labeling studies of undifferentiated cells demonstrated that S100 beta staining localized to a small region of the perinuclear cytoplasm and colocalized with the microtubule organizing center and Golg

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Santamaria-Kisiel, Liliana, Anne C. Rintala-Dempsey, and Gary S. Shaw. "Calcium-dependent and -independent interactions of the S100 protein family." Biochemical Journal 396, no. 2 (2006): 201–14. http://dx.doi.org/10.1042/bj20060195.

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The S100 proteins comprise at least 25 members, forming the largest group of EF-hand signalling proteins in humans. Although the proteins are expressed in many tissues, each S100 protein has generally been shown to have a preference for expression in one particular tissue or cell type. Three-dimensional structures of several S100 family members have shown that the proteins assume a dimeric structure consisting of two EF-hand motifs per monomer. Calcium binding to these S100 proteins, with the exception of S100A10, results in an approx. 40° alteration in the position of helix III, exposing a br

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Moravkova, Paula, Darina Kohoutova, Stanislav Rejchrt, Jiri Cyrany, and Jan Bures. "Role of S100 Proteins in Colorectal Carcinogenesis." Gastroenterology Research and Practice 2016 (2016): 1–7. http://dx.doi.org/10.1155/2016/2632703.

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The family of S100 proteins represents 25 relatively small (9–13 kD) calcium binding proteins. These proteins possess a broad spectrum of important intracellular and extracellular functions. Colorectal cancer is the third most common cancer in men (after lung and prostate cancer) and the second most frequent cancer in women (after breast cancer) worldwide. S100 proteins are involved in the colorectal carcinogenesis through different mechanisms: they enable proliferation, invasion, and migration of the tumour cells; furthermore, S100 proteins increase angiogenesis and activate NF-κβsignaling pa

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Liang, Jie, Guanhong Luo, Xiaoxuan Ning, et al. "Differential expression of calcium-related genes in gastric cancer cells transfected with cellular prion protein." Biochemistry and Cell Biology 85, no. 3 (2007): 375–83. http://dx.doi.org/10.1139/o07-052.

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The prion protein (PrPC) has a primary role in the pathogenesis of transmissible spongiform encephalopathies, which causes prion disorders partially due to Ca2+ dysregulation. In our previous work, we found that overexpressed PrPC in gastric cancer was involved in apoptosis, cell proliferation, and metastasis of gastric cancer. To better understand how PrPC acts in gastric cancer, a human microarray was performed to select differentially regulated genes that correlate with the biological function of PrPC. The microarray data were analyzed and revealed 3798 genes whose expression increased at l

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Liu, Ying, Jian Cui, Yun-Liang Tang, Liang Huang, Cong-Yang Zhou, and Ji-Xiong Xu. "Prognostic Roles of mRNA Expression of S100 in Non-Small-Cell Lung Cancer." BioMed Research International 2018 (2018): 1–11. http://dx.doi.org/10.1155/2018/9815806.

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The S100 protein family is involved in cancer cell invasion and metastasis, but its prognostic value in non-small-cell lung cancer (NSCLC) has not been elucidated. In the present study we investigated the prognostic role of mRNA expression of each individual S100 in NSCLC patients through the Kaplan–Meier plotter (KM plotter) database. Expression of 14 members of the S100 family correlated with overall survival (OS) for all NSCLC patients; 18 members were associated with OS in adenocarcinoma, but none were associated with OS in squamous cell carcinoma. In particular, high mRNA expression level

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Glenney, J. R., M. S. Kindy, and L. Zokas. "Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution." Journal of Cell Biology 108, no. 2 (1989): 569–78. http://dx.doi.org/10.1083/jcb.108.2.569.

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A low molecular mass protein which we term S100L was isolated from bovine lung. S100L possesses many of the properties of brain S100 such as self association, Ca++-binding (2 sites per subunit) with moderate affinity, and exposure of a hydrophobic site upon Ca++-saturation. Antibodies to brain S100 proteins, however, do not cross react with S100L. Tryptic peptides derived from S100L were sequenced revealing similarity to other members of the S100 family. Oligonucleotide probes based on these sequences were used to screen a cDNA library derived from a bovine kidney cell line (MDBK). A 562-nucle

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Permyakov, Sergei E., Ramis G. Ismailov, Bin Xue, Alexander I. Denesyuk, Vladimir N. Uversky, and Eugene A. Permyakov. "Intrinsic disorder in S100 proteins." Molecular BioSystems 7, no. 7 (2011): 2164. http://dx.doi.org/10.1039/c0mb00305k.

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Austermann, Judith, Christoph Spiekermann, and Johannes Roth. "S100 proteins in rheumatic diseases." Nature Reviews Rheumatology 14, no. 9 (2018): 528–41. http://dx.doi.org/10.1038/s41584-018-0058-9.

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Bresnick, Anne R. "S100 proteins as therapeutic targets." Biophysical Reviews 10, no. 6 (2018): 1617–29. http://dx.doi.org/10.1007/s12551-018-0471-y.

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Eckert, Richard L., Ann-Marie Broome, Monica Ruse, Nancy Robinson, David Ryan, and Kathleen Lee. "S100 Proteins in the Epidermis." Journal of Investigative Dermatology 123, no. 1 (2004): 23–33. http://dx.doi.org/10.1111/j.0022-202x.2004.22719.x.

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Peterova, Eva, Jan Bures, Paula Moravkova, and Darina Kohoutova. "Tissue mRNA for S100A4, S100A6, S100A8, S100A9, S100A11 and S100P Proteins in Colorectal Neoplasia: A Pilot Study." Molecules 26, no. 2 (2021): 402. http://dx.doi.org/10.3390/molecules26020402.

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S100 proteins are involved in the pathogenesis of sporadic colorectal carcinoma through different mechanisms. The aim of our study was to assess tissue mRNA encoding S100 proteins in patients with non-advanced and advanced colorectal adenoma. Mucosal biopsies were taken from the caecum, transverse colon and rectum during diagnostic and/or therapeutic colonoscopy. Another biopsy was obtained from adenomatous tissue in the advanced adenoma group. The tissue mRNA for each S100 protein (S100A4, S100A6, S100A8, S100A9, S100A11 and S100P) was investigated. Eighteen biopsies were obtained from the he

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Weisz, Judith, and Vladimir N. Uversky. "Zooming into the Dark Side of Human Annexin-S100 Complexes: Dynamic Alliance of Flexible Partners." International Journal of Molecular Sciences 21, no. 16 (2020): 5879. http://dx.doi.org/10.3390/ijms21165879.

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Annexins and S100 proteins form two large families of Ca2+-binding proteins. They are quite different both structurally and functionally, with S100 proteins being small (10–12 kDa) acidic regulatory proteins from the EF-hand superfamily of Ca2+-binding proteins, and with annexins being at least three-fold larger (329 ± 12 versus 98 ± 7 residues) and using non-EF-hand-based mechanism for calcium binding. Members of both families have multiple biological roles, being able to bind to a large cohort of partners and possessing a multitude of functions. Furthermore, annexins and S100 proteins can in

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Sugino, Hitomi, and Yu Sawada. "Influence of S100A2 in Human Diseases." Diagnostics 12, no. 7 (2022): 1756. http://dx.doi.org/10.3390/diagnostics12071756.

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S100 proteins are a family of low-molecular-weight proteins characterized by two calcium-binding sites with a helix-loop-helix (“EF-hand-type”) domain. The S100 family of proteins is distributed across various organs and can interact with diverse molecules. Among the proteins of the S100 family, S100 calcium-binding protein A2 (S100A2) has been identified in mammary epithelial cells, glands, lungs, kidneys, and prostate gland, exhibiting various physiological and pathological actions in human disorders, such as inflammatory diseases and malignant tumors. In this review, we introduce basic know

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Calaf, Gloria M., Luis N. Ardiles, and Leodan A. Crispin. "Role of Calcium in an Experimental Breast Cancer Model Induced by Radiation and Estrogen." Biomedicines 12, no. 11 (2024): 2432. http://dx.doi.org/10.3390/biomedicines12112432.

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Background: Breast cancer, a global health challenge, significantly impacts women worldwide, causing morbidity, disability, and mortality. Objectives: To analyze the role of genes encoding S100 calcium-binding proteins and their relationship with radiation as possible markers in breast carcinogenesis. Methods: The normal MCF-10F cell line was used to study the role of ionizing radiation and estrogen to induce distinct stages of malignancy giving rise to an in vitro experimental breast cancer model. Results: Analysis of an Affymetrix system revealed that the gene expression levels of the S100 c

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Cristóvão, Joana S., Mariana A. Romão, Rodrigo Gallardo, Joost Schymkowitz, Frederic Rousseau, and Cláudio M. Gomes. "Targeting S100B with Peptides Encoding Intrinsic Aggregation-Prone Sequence Segments." Molecules 26, no. 2 (2021): 440. http://dx.doi.org/10.3390/molecules26020440.

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S100 proteins assume a diversity of oligomeric states including large order self-assemblies, with an impact on protein structure and function. Previous work has uncovered that S100 proteins, including S100B, are prone to undergo β-aggregation under destabilizing conditions. This propensity is encoded in aggregation-prone regions (APR) mainly located in segments at the homodimer interface, and which are therefore mostly shielded from the solvent and from deleterious interactions, under native conditions. As in other systems, this characteristic may be used to develop peptides with pharmacologic

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SEEMANN, Joachim, Klaus WEBER, and Volker GERKE. "Structural requirements for annexin I-S100C complex-formation." Biochemical Journal 319, no. 1 (1996): 123–29. http://dx.doi.org/10.1042/bj3190123.

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S100C is a member of the S100 family of EF-hand-type Ca2+-binding proteins which are thought to bind to and thereby regulate the activity of cellular target proteins in a Ca2+-dependent manner. An intracellular ligand for S100C is the Ca2+/phospholipid-binding protein annexin I and we show here that complex-formation is mediated through unique domains within S100C and annexin I. Using a proteolytically truncated annexin I derivative as well as a number of N-terminal annexin I peptides in liposome co-pelleting and ligand-blotting assays we map the S100C-binding site to the N-terminal 13 residue

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Mandinova, A., D. Atar, B. W. Schafer, M. Spiess, U. Aebi, and C. W. Heizmann. "Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium." Journal of Cell Science 111, no. 14 (1998): 2043–54. http://dx.doi.org/10.1242/jcs.111.14.2043.

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Changes in cytosolic Ca2+ concentration control a wide range of cellular responses, and intracellular Ca2+-binding proteins are the key molecules to transduce Ca2+ signaling via interactions with different types of target proteins. Among these, S100 Ca2+-binding proteins, characterized by a common structural motif, the EF-hand, have recently attracted major interest due to their cell- and tissue-specific expression pattern and involvement in various pathological processes. The aim of our study was to identify the subcellular localization of S100 proteins in vascular smooth muscle cell lines de

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Saito-Sasaki, Natsuko, and Yu Sawada. "S100 Proteins in the Pathogenesis of Psoriasis and Atopic Dermatitis." Diagnostics 13, no. 20 (2023): 3167. http://dx.doi.org/10.3390/diagnostics13203167.

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The skin, the outermost layer of the human body, is exposed to various external stimuli that cause inflammatory skin reactions. These external stimulants trigger external epithelial cell damage and the release of intracellular substances. Following cellular damage or death, intracellular molecules are released that enhance tissue inflammation. As an important substance released from damaged cells, the S100 protein is a low-molecular-weight acidic protein with two calcium-binding sites and EF-hand motif domains. S100 proteins are widely present in systemic organs and interact with other protein

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Heizmann, Claus, W. "S100 proteins: structure, functions and pathology." Frontiers in Bioscience 7, no. 1-3 (2002): d1356. http://dx.doi.org/10.2741/heizmann.

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Brenner, Annette K., and Øystein Bruserud. "S100 Proteins in Acute Myeloid Leukemia." Neoplasia 20, no. 12 (2018): 1175–86. http://dx.doi.org/10.1016/j.neo.2018.09.007.

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Riuzzi, Francesca, Sara Chiappalupi, Cataldo Arcuri, Ileana Giambanco, Guglielmo Sorci, and Rosario Donato. "S100 proteins in obesity: liaisons dangereuses." Cellular and Molecular Life Sciences 77, no. 1 (2019): 129–47. http://dx.doi.org/10.1007/s00018-019-03257-4.

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Pietzsch, Jens. "S100 proteins in health and disease." Amino Acids 41, no. 4 (2010): 755–60. http://dx.doi.org/10.1007/s00726-010-0816-8.

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Heizmann, Claus W. "S100 proteins structure functions and pathology." Frontiers in Bioscience 7, no. 4 (2002): d1356–1368. http://dx.doi.org/10.2741/a846.

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Singh, Parul, and Syed Azmal Ali. "Multifunctional Role of S100 Protein Family in the Immune System: An Update." Cells 11, no. 15 (2022): 2274. http://dx.doi.org/10.3390/cells11152274.

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S100 is a broad subfamily of low-molecular weight calcium-binding proteins (9–14 kDa) with structural similarity and functional discrepancy. It is required for inflammation and cellular homeostasis, and can work extracellularly, intracellularly, or both. S100 members participate in a variety of activities in a healthy cell, including calcium storage and transport (calcium homeostasis). S100 isoforms that have previously been shown to play important roles in the immune system as alarmins (DAMPs), antimicrobial peptides, pro-inflammation stimulators, chemo-attractants, and metal scavengers durin

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Okazaki, K., N. H. Obata, S. Inoue та H. Hidaka. "S100β is a target protein of neurocalcin δ, an abundant isoform in glial cells". Biochemical Journal 306, № 2 (1995): 551–55. http://dx.doi.org/10.1042/bj3060551.

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To clarify the function of neurocalcin delta, an isoform found abundantly in glial cells, we attempted to find its target proteins by using neurocalcin delta-affinity chromatography and the 125I-neurocalcin delta gel-overlay method. The 10, 14, 27, 36 and 50 kDa bands found on SDS/PAGE bound to 125I-neurocalcin delta, and 10, 11, 19, 24, 26, 50 and 70 kDa proteins were eluted from a neurocalcin delta-affinity column in a Ca(2+)-dependent manner. Sequence analysis of proteolytic peptides revealed the following identities: S100 beta (10 kDa), S100 alpha (11 kDa), myelin basic protein (19 kDa), g

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Harpio, Riikka, and Roland Einarsson. "S100 proteins as cancer biomarkers with focus on S100B in malignant melanoma." Clinical Biochemistry 37, no. 7 (2004): 512–18. http://dx.doi.org/10.1016/j.clinbiochem.2004.05.012.

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Hsieh, Hsiao-Ling, Beat W. Schäfer, Jos A. Cox, and Claus W. Heizmann. "S100A13 and S100A6 exhibit distinct translocation pathways in endothelial cells." Journal of Cell Science 115, no. 15 (2002): 3149–58. http://dx.doi.org/10.1242/jcs.115.15.3149.

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S100 proteins have attracted great interest in recent years because of their cell- and tissue-specific expression and association with various human pathologies. Most S100 proteins are small acidic proteins with calcium-binding domains — the EF hands. It is thought that this group of proteins carry out their cellular functions by interacting with specific target proteins, an interaction that is mainly dependent on exposure of hydrophobic patches, which result from calcium binding. S100A13, one of the most recently identified members of the S100 family, is expressed in various tissues. Interest

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