Disease relevance of CSN1S1

• Activation of a tumor-associated protein kinase (p40TAK) and casein kinase 2 in human squamous cell carcinomas and adenocarcinomas of the lung [1].
• The human VRK1 protein is a new kinase related to a poxvirus kinase, and more distantly to the casein kinase 1 family [2].
• Murine model for human secondary amyloidosis: genetic variability of the acute-phase serum protein SAA response to endotoxins and casein [3].
• At 8 weeks, they were given injections sc of 10 mg BOP/kg body weight and placed on a control diet [9 g corn oil (medium fat) and 18 g casein (medium protein)/385 kcal] [4].
• Production of casein and the presence of estrogen receptors in human breast cancer [5].

Psychiatry related information on CSN1S1

• Locomotor activity of T cells with receptors for IgM and IgG, T cells without receptors for IgM or IgG, and T and non-T cells from human peripheral blood and human tonsils towards the chemoattractant casein was examined in modified Boyden chambers [6].
• Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain [7].
• A missense variation in human casein kinase I epsilon gene that induces functional alteration and shows an inverse association with circadian rhythm sleep disorders [8].
• Twenty-eight elderly patients with dementia and in many cases also depression received daily treatment with either L-tryptophan (3g in the evening) or casein (control substance) for 1 month each, using a crossover design and double-blind procedures [9].
• Manduca sexta larvae exhibited altered food selection over a 2- or 3-day feeding period when parasitized by Cotesia congregata, and offered a choice of two chemically defined diets, one containing casein without sucrose and a second with sucrose but no casein [10].

High impact information on CSN1S1

• Particular emphasis is put on milk proteins such as lactoferrin, casein, and whey proteins, but phytate in soy formula is also discussed [11].
• Monopolar attachment of sister kinetochores at meiosis I requires casein kinase 1 [12].
• In this issue of Cell, report that casein kinase 1 contributes to this process by promoting the attachment of both kinetochores of a homolog to only one pole of the meiotic spindle in budding yeast [13].
• Casein kinase Ialpha directly binds and phosphorylates NF-AT4, resulting in the inhibiton of NF-AT4 nuclear translocation [14].
• Serine 366 comprises a casein kinase II phosphorylation site that resides within a conserved region in the La proteins from several species [15].

Chemical compound and disease context of CSN1S1

• A tyrosine-based motif and a casein kinase II phosphorylation site regulate the intracellular trafficking of the varicella-zoster virus glycoprotein I, a protein localized in the trans-Golgi network [16].
• We produced moderately severe, inactive micronodular cirrhosis in rats using CCl4 and measured the urea cycle enzyme activities in liver after feeding a 15% casein diet for 1 week and again after a 60% casein diet for 1 week [17].
• The MYCN protein of human neuroblastoma cells is phosphorylated by casein kinase II in the central region and at serine 367 [18].
• When results of all four experiments were averaged, 57.5 +/- 3.6% of hamsters fed casein exhibited cholesterol gallstones whereas only 14.0 +/- 1.3% of soy protein-fed hamsters had gallstones [19].
• We have used both biochemical and genetic approaches to show that this 496-residue (496R) protein of adenovirus type 5 is phosphorylated at serine and threonine residues near the carboxy terminus within sequences characteristic of substrates of casein kinase II [20].

Biological context of CSN1S1

• From qPCR data, the four casein transcripts appeared to be present approximately at the same level of abundance (ca. 25%, except for defective genotypes at the CSN1S1 locus, in the goat) whereas the amounts of the corresponding proteins in milk were ranging between 9 and 38% of the whole casein fraction [21].
• In addition, two cryptic exons were localized in the bovine alpha s1-casein gene [22].
• The casein gene family was localized to chromosome 4q21.1 by FISH analysis [23].
• Five yeast artificial chromosome (YAC) clones containing the human casein gene family were isolated and characterized to study the control mechanisms for the expression of these genes [23].
• Amino acid sequence analysis of the closely spaced bands all resulted in the same N-terminal sequence which was found to be homologous with alpha s1-casein from other species [24].

Anatomical context of CSN1S1

• Human alpha s1-casein has been reported to exist naturally as a multimer in complex with kappa-casein in mature human milk, thereby being unique among alpha s1-caseins [Rasmussen, Due and Petersen (1995) Comp. Biochem. Physiol., in the press] [22].
• GC kinase immunoprecipitated from transfected COS cells phosphorylated the substrates casein and myelin basic protein [25].
• Casein kinase II activity does not change during oocyte maturation, and therefore, cannot be responsible for the activation of translation [26].
• Two-hundred twenty subjects provided a semen sample for computer-aided sperm analysis (CASA) and a urine sample for measurement of phthalate monoesters, monoethyl (MEP), monobenzyl (MBzP), mono-n-butyl (MBP), mono-2-ethylhexyl (MEHP), and monomethyl (MMP) [27].
• Pre-treatment of human neutrophils with myelin basic protein selectively inhibits the formyl-peptide-induced chemotaxis, without affecting chemotaxis evoked by casein and activated serum [28].

Associations of CSN1S1 with chemical compounds

• The second peak was identified as casein kinase 2, based upon immunoreactivity to casein kinase 2-specific antipeptide antibodies and its sensitivity to inhibition by heparin sulfate [1].
• Sequence analysis of a major radiolabelled tryptic peptide from purified 14C-carboxymethylated alpha s1-casein demonstrated that the protein contains at least two cysteine residues [24].
• Like the GC kinase, rab8ip has protein kinase activity manifested by autophosphorylation and phosphorylation of the classical serine/threonine protein kinase substrates, myelin basic protein and casein [29].
• 1. TTBK1 is a serine/threonine/tyrosine kinase that is conserved among species and belongs to the casein kinase 1 superfamily [30].
• The catalytic domains of LAR and LAR-PTP2 prepared by bacterial expression were active in dephosphorylating a variety of phosphotyrosyl substrates but did not hydrolyse phosphoserine or phosphothreonine residues of labelled casein [31].

Physical interactions of CSN1S1

• Casein kinase I phosphorylates and destabilizes the beta-catenin degradation complex [32].
• Loss of phosphorylation at Ser(421) and Ser(423) due to mutation to alanine or disruption of the casein kinase 2 consensus sequence directing phosphorylation reduced the enzymatic activity and complex formation of HDAC1 [33].
• Alterations in C3 activation and binding caused by phosphorylation by a casein kinase released from activated human platelets [34].
• Casein kinase II is a negative regulator of c-Jun DNA binding and AP-1 activity [35].
• Consistent with this finding, phosphorylation of p15 by casein kinase II inhibits binding to double-stranded DNA and the activity of p15 [36].

Enzymatic interactions of CSN1S1

• Here, we report that BACE can be phosphorylated within its cytoplasmic domain at serine residue 498 by casein kinase 1 [37].
• In this report, we demonstrate that mammalian Cdc37 is phosphorylated on Ser13 in situ in rabbit reticulocyte lysate and in cultured K562 cells and that casein kinase II is capable of quantitatively phosphorylating recombinant Cdc37 at this site [38].
• These results demonstrate that the hER is phosphorylated on serine 167 by casein kinase II in a hormone-dependent manner [39].
• The human 1,25-dihydroxyvitamin D3 receptor (hVDR) has been recently shown to be phosphorylated in vitro by casein kinase-II [40].
• Furthermore, human casein enhanced t-PA-catalyzed plasminogen activation, comparable to the enhancing effect obtained with fibrinogen fragments [41].

Co-localisations of CSN1S1

• Casein autography of isolated platelets revealed a approximately 90 kDa band of activity which comigrated with plasma prekallikrein (PK)/kallikrein, a known activator of pro-UK [42].

Regulatory relationships of CSN1S1

• The results showed that yak casein hydrolysate had lymphoproliferation activity on murine splenocytes and induced their cell cycle from the G1 to the S phase [43].
• Sensitization of tumor cells to Apo2 ligand/TRAIL-induced apoptosis by inhibition of casein kinase II [44].
• Furthermore, although high concentrations of casein kinase II strongly inhibits DNA ligase I activity, it does not affect the ability of 9-1-1 to stimulate [45].
• Prolactin stabilizes and promotes transcription of casein mRNA; may stimulate synthesis of alpha-lactalbumin, the regulatory protein of the lactose synthetase enzyme system; and increases lipoprotein lipase activity in the mammary gland [46].
• HPV-16 E7 and adenovirus E1a complex formation with TATA box binding protein is enhanced by casein kinase II phosphorylation [47].

Other interactions of CSN1S1

• Myelin basic protein, casein, and a ribosomal S6-1 COOH-terminus peptide were efficient substrates for protein kinases that exhibited elevated phosphotransferase activity in the tumor extracts when compared to extracts derived from the adjacent nonneoplastic lung or from the lung parenchyma from patients with nonneoplastic lung disorders [1].
• Casein and histone were very poor substrates for this EGF-stimulated MAP2 kinase activity [48].
• In contrast to phosphorylation by casein kinase II or the cAMP-dependent protein kinase catalytic subunit, phosphorylation of RII beta by mitotic kinases impaired its interaction with a well-known RII-anchoring protein, the neuronal microtubule-associated protein 2 [49].
• Phosphorylation of CD45 by casein kinase 2. Modulation of activity and mutational analysis [50].
• ATX possesses no detectable protein kinase activity toward histone, myelin basic protein, or casein [51].

Analytical, diagnostic and therapeutic context of CSN1S1

• Here we report the molecular cloning and sequencing of three types of human alpha s1-casein transcripts and present evidence indicating that exon skipping is responsible for deleted mRNA transcripts [22].
• Tissue-specific expression of human alpha s1-casein was indicated by Northern-blot analysis [22].
• Partial restriction analysis in conjunction with the chromosomal fragmentation method and fluorescence in situ hybridization (FISH) analysis were performed to construct a detailed physical map of the casein gene family and to determine the chromosomal localization of these genes [23].
• The relative proportions of each specific messenger (% of casein mRNA) were compared to the relative amounts of the corresponding caseins (% of whole casein) in milks sampled from the same animals, determined after fractionation by reverse phase HPLC and integration of the corresponding peak areas [21].
• The human counterpart of alpha s1-casein has been purified by a combination of gel-filtration and ion-exchange chromatography under denaturing conditions [24].

References