Disease relevance of HERPUD1

• HERPUD1 mRNA expression predicted the occurrence of metastases almost perfectly [1].
• Samples of 21 patients with CML, the ALL-derived cell line SUP-B15, and of seven patients with Philadelphia chromosome (Ph1)-positive ALL (three of them with breakpoints within m-bcr) were examined [2].
• The human T acute lymphocytic leukemia cell line, SUP-T13, is a mosaic of TCR/CD3+ and TCR/CD3- cells [3].
• Therefore, we studied the mechanism of Herp CpG islands regulation by luciferase assays and mRNA analysis in neuronal SH-SY5Y (human neuroblastoma cell line) and HEK 293T (human embryonic kidney 293T) cells [4].
• To assess the role of these genes in other leukemia-associated translocations we mapped their locations with respect to the t(11;19)(q23;p13) and t(4;19)(q21;p13) translocation breakpoints carried by T-ALL cell lines SUP-T13 and SUP-T8a, respectively [5].

Psychiatry related information on HERPUD1

• The results raise the possibility that Tyr-MIF-1 might participate in opiate dependence and opiate abstinence syndrome [6].
• In a second, double-blind study testing MIF-1 in endogenous depressions, 5 patients met the criteria for substantial improvement out of a total of 8 receiving MIF-1 75 mg per day [7].

High impact information on HERPUD1

• We have analyzed LCK gene expression in HSB-2 and SUP-T12 cell lines [8].
• The breakpoint in SUP-T12 occurred 2 kb 5' of the type II promoter, leaving an intact LCK gene on the der(1) chromosome [8].
• In vitro experiments showed that overexpression of the stress response gene HERPUD1 rapidly induces apoptosis [1].
• We found that Herp interacts with both PS1 and PS2 [9].
• Here, we report that a high expression of Herp in cells increases the level of Abeta generation, although not in PS-deficient cells [9].

Chemical compound and disease context of HERPUD1

• It is, therefore, possible that the effects of MIF-1 in movement disorders are associated with increased melatonin secretion [10].
• Neurological effects of MIF-1, MSH, and opiate peptides in clinical studies [11].
• There is evidence to suggest that MIF-1 increases nigro-striatal dopaminergic activity, but its ability to improve symptoms in patients with Parkinson's disease, levodopa-related dyskinesias and Tardive dyskinesia cannot be explained solely on the basis of the drug's effect on striatal dopaminergic neurons [10].
• More recently, MIF-1 has been reported partially to protect against the nigro-striatal dopamine depleting effects of MPTP in mice, raising the possibility that it may exert protective effects against the development of Parkinson's disease [10].

Biological context of HERPUD1

• Here, we report the genomic structure of human Herp and the presence of a new ER stress response element, ERSE-II, in its promoter region [12].
• The gene for Herp consists of eight exons, localized to chromosome 16q12.2-13 [12].
• Treatment with the glycosylation inhibitor tunicamycin both enhances the synthesis of Mif1 mRNA and protein [13].
• The Mif1 5' flanking region contains a functional ER stress-responsive element which is sufficient for induction by tunicamycin [13].
• In addition, MIF-1, 2, and 3 share a 5-nucleotide (TTATG) internal sequence, which may account for cross-competition of these binding sites in the exonuclease protection experiment [14].

Anatomical context of HERPUD1

• Herp was originally identified as a homocysteine-responsive protein, and its expression is up-regulated by endoplasmic reticulum stress [9].
• Immunohistochemical analysis of a normal human brain section with an anti-Herp antibody revealed the exclusive staining of neurons and vascular smooth muscle cells [9].
• Taken together, Herp could be involved in Abeta accumulation, including the formation of senile plaques and vascular Abeta deposits [9].
• Consideration of the isolation, structure, localization, and behavioral effects of melanocyte stimulating hormone release inhibiting factor (MIF-1) is followed by a review of its opiate antagonistic and clinical effects [15].
• This suggestion was strengthened by the finding that only the cytosol of the RBC, not its membranes, rapidly degraded Tyr-MIF-1 to free iodine and iodotyrosine [16].

Associations of HERPUD1 with chemical compounds

• Here, we demonstrate that homocysteine induces the ER stress response and leads to the expression of a novel protein, Herp, containing a ubiquitin-like domain at the N terminus. mRNA expression of Herp was strongly up-regulated by inducers of ER stress, including mercaptoethanol, tunicamycin, A23187, and thapsigargin [17].
• MMS, on the other hand, activates Mif1 via an UPR-independent pathway [13].
• Although Tyr-melanocyte-stimulating hormone release-inhibiting factor 1 (MIF-1) (Tyr-Pro-Leu-Gly-NH2) can exert a number of biological actions in the brain and elsewhere, it has never been isolated from any tissue [18].
• MSH also seems to be working in conjunction with the hypothalamic tripeptide MIF-1 and the pineal hormone melatonin, both of which can affect the release of MSH from the pituitary [19].
• Family members MIF-1, Tyr-W-MIF-1 and Tyr-K-MIF-1 are also included [20].

Other interactions of HERPUD1

• Expression analysis of the two selected ER stress responsive genes, NDRG1 and HERPUD1 in primary CaPs revealed a significantly reduced tumor associated expression [21].
• We previously demonstrated that MIBP1 and RFX1 polypeptides associate in vivo to form a complex that binds to the MIF-1 element in the c-myc gene and the major histocompatibility complex class II X-box recognition sequence [22].
• For many peptides, such as the enkephalins, TRH, somatostatin and MIF-1, poor penetration of the blood-brain barrier was shown [23].
• In addition to our previous characterization of a 20-nucleotide binding site for MIF-1, we now have identified adjacent 20-nucleotide and 34-nucleotide binding sites for MIF-2 and MIF-3, respectively [14].
• 17 beta Estradiol-induced increase in brain dopamine D-2 receptor: antagonism by MIF-1 [24].

Analytical, diagnostic and therapeutic context of HERPUD1

• The effects of Prolyl-leucyl-glycinamide (PLG, MIF-1) and the exogenous opiate antagonist naloxone, on aggressive interactions and defeat-induced analgesia were examined in male mice [25].
• Using a combination of biochemical techniques including high-pressure gel permeation chromatography followed by reversed-phase HPLC on brain extracts and Edman degradation, we demonstrated the presence of an authentic MIF-1 peptide in leech brain [26].
• MN SUP which contained high suppressor cell-inducing activity had no effect on PPD-induced blastogenesis of PBMC from a healthy donor [27].
• Western blot analysis identified MIF1-like proteins in the murine trigeminal ganglion (TG) and immunostaining localized these proteins primarily to the cytoplasm of TG neuronal cell bodies [28].
• In situ hybridization for Mif1 transcripts confirms the selective expression of Mif1 in TG neurons [28].

References