Disease relevance of AP1B1

• Northern blot analysis of 70 sporadic meningiomas showed specific loss of expression in 8 tumors, suggesting inactivation of BAM22 [1].
• Based on this, we propose BAM22 as a second chromosome 22 locus important in meningioma development, after the neurofibromatosis type 2 gene [1].

High impact information on AP1B1

• This suggests that the phosphorylation of arrestin-3 does not directly regulate interaction with endocytic (clathrin, beta-adaptin) or signaling (Src) components and is in contrast to arrestin-2, where phosphorylation appears to regulate interaction with clathrin and Src [2].
• The observation that BAM22 inhibited the Leu-enkephalin-promoted cAMP inhibition in rat dorsal root ganglia neurons supports the potential physiological implication of such regulatory mechanism [3].
• Structure of the promoter and genomic organization of the human beta'-adaptin gene (BAM22) from chromosome 22q12 [4].
• As part of the genomic characterization of the BAM22 locus, we sequenced 40 kb covering exons 1-4 and 12 kb upstream from the start of gene transcription [4].
• The genomic sequencing of a 40-kb region bounded by the EWS and BAM22 genes and containing a CpG-rich region has identified two new genes in the q12 region of chromosome 22 [5].

Biological context of AP1B1

• beta-adaptin: Key molecule for microglial scavenger receptor function under oxidative stress [6].
• The BAM22 gene is located on human Chromosome (Chr) 22q12 and can be considered a candidate meningioma tumor suppressor gene [7].
• We provide 3885-bp cDNA sequence, which entirely covers the open reading frame of the adtb1, capable of encoding a protein of 943 amino acids [7].
• The adtb1 gene has been assigned to mouse Chr 11, band 11A2, which confirms the synteny between human Chr 22q12 and mouse Chr 11 [7].

Anatomical context of AP1B1

• The results indicated that LENK, MENK, and MERF (or highly similar peptides) are present in the turtle central nervous system, and that a peptide showing immunological similarity to BAM22P and PEPE also appeared to be present [8].
• At the same concentrations, leu-enkephalin, the proenkephalin fragments BAM 22 and E, and somatostatin maintained about half of the dorsal root ganglionic neurons supported by NGF, but were not effective on ciliary neurons [9].
• Differential expression experiments of beta-adaptin, alpha-adaptin, SR-AI, and SR-BI in RAW (macrophages) and EOC (microglia) cells were performed according to dosage and exposure time to amyloid-beta [6].

Associations of AP1B1 with chemical compounds

• The distributions of the immunoreactive labeling for LENK, MENK, MERF, BAM22P, and PEPE were indistinguishable, and double-label studies showed that LENK, MERF, and BAM22P were colocalized within individual neurons and fibers [8].
• Antisera against several enkephalin peptides were used: leucine-enkephalin (LENK), methionine-enkephalin (MENK), methionine-enkephalin-arg6-phe7 (MERF), methionine-enkephalin-arg6-gly7-leu8 (MERGL), Peptide E (PEPE), and BAM22P [8].
• Substantial cross-reactivity is seen with some other naturally occurring opioid peptides bearing the enkephalin sequence, such as dynorphin, alpha-neo-endorphin and BAM 22, but cross-reactivity is lacking in the case of certain synthetic enkephalin derivatives possessing a D-amino acid in position 2 [10].
• Peroxidase-catalyzed oxidation of 3,3 ,5,5 -tetramethylbenzidine (TMB) was inhibited by o-aminophenol (AP), 2-amino-4-tert-butylphenol (ATBP), 2-amino-4,6-di-tert-butylphenol (ADTBP), and 4-tert-butylpyrocatechol (TBP) [11].
• 3. Endopeptidase H2 hydrolyzes the Phe-Ser bond of peptides related to bradykinin and its activity appears to be limited to peptide chains of < or = 18 amino acid residues since it does not hydrolyze BAM 22, peptide E or kininogen [12].

Analytical, diagnostic and therapeutic context of AP1B1

• Under these conditions, RT-PCR assays show that beta-adaptin mRNA is normally synthesized, reason why protein translation or protein structure of beta-adaptin might be altered [6].

References