Disease relevance of S100a1

• Expression of antisense RNA to S100A4 gene encoding an S100-related calcium-binding protein suppresses metastatic potential of high-metastatic Lewis lung carcinoma cells [1].
• Accordingly, various diseases such as cardiomyopathies, neurodegenerative and inflammatory disorders, and cancer are associated with altered S100 protein levels [2].
• Since binding of effector molecules to S100 proteins has been shown to involve the C-terminus and linker regions, these calcium-induced changes have implications for the role of Mts1 in metastasis [3].
• Immunological assays for the detection of neuroendocrine-associated peptides, hormones, and enzymes revealed that, like melanoma, the SU-CCS-1 cell line was actively producing alpha-melanotropin, S-100 antigen, and nerve growth factor [4].
• To elucidate the molecular mechanism by which the potent anticancer drug, 5-fluorouracil (5-FUra), inhibits cell proliferation, the effect of its metabolite, 5-fluorouridine triphosphate, on transcription of rat rRNA gene and processing of pre-rRNA was investigated in S-100 extract from the mouse lymphosarcoma cells [5].

Psychiatry related information on S100a1

• Characterization of social behaviors and oxytocinergic neurons in the S-100 beta overexpressing mouse model of Down Syndrome [6].
• Elevated levels of S100 beta protein have been observed in the brains of individuals with Alzheimer Disease (AD), as well as in those with Down Syndrome (DS) [7].

High impact information on S100a1

• At least one of the compensatory mechanisms preventing a more severe skin phenotype in newborn Lor(-/-) mice is an increase in the expression of other CE components, such as SPRRP2D and SPRRP2H, members of the family of "small proline rich proteins", and repetin, a member of the "fused gene" subgroup of the S100 gene family [8].
• In addition, in a cell-free system, the S-100 fraction of anti-IgM-treated WEHI-231 cells induces a caspase activation pattern different from that activated by cytochrome c and dATP [9].
• Partial amino acid sequence analysis of the purified 10-kD protein, two-dimensional polyacrylamide gel analysis and a binding experiment revealed that the 10-kD protein was identical to a calcium-binding protein derived from mRNA named pEL98 or 18A2 that is homologous to S100 protein [10].
• At the cut ends of the nerve stumps a cap developed (more at the proximal than at the distal stump) that contained S-100-negative and fibronectin-positive fibroblast-like cells [11].
• An in vitro processing system of mouse rRNA was achieved using an RNA polymerase I-specific transcription system, (S100) and recombinant plasmids consisting of mouse rRNA gene (rDNA) segments containing the transcription initiation and 5'-terminal region of 18S (or 41S) rRNA [12].

Chemical compound and disease context of S100a1

• The S-100 protein level in mouse neuroblastoma (N18TG-2 and NIE-115), rat glioma (C6, C6BU-1, and C6V-1), and hybrid (NG108-15, 140-3, 141-B, NBr10A, NBr20A, NCB20, and NX3IT) cells was determined with a sensitive enzyme immunoassay system that uses a rabbit antibody to bovine brain S-100 protein [13].
• De novo DNA methyltransferases, Dnmt3a and 3b, were purified by fractionation of S-100 extract from mouse lymphosarcoma cells through several chromatographic matrices followed by glycerol density gradient centrifugation [14].

Biological context of S100a1

• We have found that the mouse parathyroid exhibits the glial progenitor markers, p75(NTR) and S100 protein, during fetal development [15].
• We have generated mice with a targeted deletion of the S100A1 gene coding for the major cardiac isoform of the large multigenic S100 family of EF hand Ca(2+)-binding proteins [16].
• An update of the S100 nomenclature is included, because some of the recently identified S100 genes and pseudogenes had to be renamed [2].
• The mts1 gene codes for a 101 amino acid protein which belongs to the subfamily of S100 Ca(2+)-binding proteins and is overexpressed in metastatic cancers as compared to their nonmetastatic counterparts [17].
• Several of the patients undergoing open heart surgery presented measurable values in this IRMA S-100 assay, indicating cerebral effects of open heart surgery [18].

Anatomical context of S100a1

• The parathyroid maintains intense immunoreactivity for p75(NTR) and S100 protein during the migration and development in the thyroid lobe [15].
• Expression of glial progenitor markers p75(NTR) and S100 protein in the developing mouse parathyroid gland [15].
• The S100-related calcium-binding protein S100A4 (p9Ka) is expressed at a low level in rat mammary epithelial cells from normal mammary gland and benign mammary tumors [19].
• The S-100 family of proteins are acidic calcium and zinc binding low molecular weight proteins mainly present in astrocytes and in a population of oligodendrocytes of the CNS [18].
• S-100 proteins (S-100 a and S-100 b) were specifically abundant in nerve tissues [20].

Associations of S100a1 with chemical compounds

• In contrast, the number of double-labeled S100/GFAP-immnoreactive cells increased from 1 day up to 7 days after MPTP treatment [21].
• S100 proteins comprise a family of Ca(2+) binding proteins of at least 21 members [22].
• Two calcium-binding sites of the Mts1 protein, a member of S-100 protein family, were distinguished with the Fluo-3 fluorescent technique [23].
• Chemotactic protein, 10 kD (CP-10), is an S100 protein with potent chemotactic activity for myeloid cells in vitro and in vivo and is expressed in neutrophils and lipopolysaccharide (LPS)-activated macrophages [24].
• The 76-amino acid sequence, obtained by automated N-terminal microsequence analysis of native CP-10, and fragments derived from trypsin digestion and cyanogen bromide cleavage indicated no sequence identity with any known cytokine or chemotactic factor but revealed up to 55% sequence homology with S100, Ca2(+)-binding proteins [25].

Physical interactions of S100a1

• Calcyclin-like protein binds Zn2+ and forms dimers like other members of the S-100 protein family [26].

Regulatory relationships of S100a1

• In NG108-15 hybrid cells the induction of S-100 protein was also observed by forskolin as well as prostaglandin (PG) E1 plus theophylline which are known to activate adenylate cyclase of the cells [13].

Other interactions of S100a1

• In our double-labeled immunostaining, the number of S100-positive/GFAP-negative cells decreased from 1 day up to 7 days after MPTP treatment [21].
• Calcyclin is a member of the S100 family of calcium binding proteins [27].
• As a member of the S100 protein family, Mts1 is predicted to contain four alpha-helices and two calcium-binding loops, the second of which forms a canonical EF hand, while the first is a pseudo-EF hand, using two extra residues and principally backbone carbonyls rather than side chain oxygens to coordinate calcium [3].
• These results suggest that a predominant form of S100 protein in human myocardial cells is not S100a (alpha beta) or S100b (beta beta), but S100a0 (alpha alpha) [28].
• Sephacryl S-100 gel filtration chromatography analysis of the cytosolic Bax indicated that this protein is monomeric and displays an apparent molecular mass of 25 kDa [29].

Analytical, diagnostic and therapeutic context of S100a1

• The co-localization of p75(NTR) and S100 in the developing parathyroid cells has been confirmed by confocal microscopy [15].
• Systems, including knock-out animal models, should be now used with the aim of defining the correspondence between the in vitro regulatory role(s) attributed to individual members of this protein family and the in vivo function(s) of each S100 protein [30].
• The pattern of S100 mRNA expression did not change during postnatal development and cell culture of smooth muscle [31].
• We have raised mouse hybridomas that secrete monoclonal antibodies against bovine brain-specific proteins 14-3-2 and S-100, and we have characterized the antibodies by immunoperoxidase and immunofluorescence methods in sections and in tissue cultures of rat brain [32].
• A monoclonal antibody to the calcium binding protein S-100 (G12.B8) reacted strongly with bovine S-100 in an ELISA and with the major protein bands in electrophoretically separated S-100 [32].

References