High impact information on HBB

• Cells were transfected with reporter gene constructs containing deletion mutations of the 5'-flanking region of the bovine CYP11A gene linked to the minimal beta-globin gene [1].
• We have examined the transcriptional activity of four cis-elements, Ad1(CRE), Ad2, Ad3, and Ad4, that are present in the promoter of the bovine CYP11B (11 beta-hydroxylase P-450) gene using beta-globin reporter gene constructs and transient transfection into steroidogenic and nonsteroidogenic cell types [2].
• Southern blot analysis indicated that both lagans appeared twice within the cow haploid genome, with the second copies lying outside the cow beta-globin locus [3].
• The 12-member beta-globin gene locus of the goat contains three beta(adult)-type pseudogenes, one in each of three four-gene subsets of the locus [4].
• In this developing cohort, a tightly programmed sequence of gene expression was observed, and maximal expression of c-kit, EPO receptor, and beta-globin transcripts occurred at 72, 96, and 120 hours post-TAP withdrawal, respectively [5].

Biological context of HBB

• Physical mapping of ADCY2, FSHB and HBB to bovine chromosome 15 by FISH of bovine bacterial artificial chromosome clones [6].
• In order to identify regulatory sequences within the 5' flanking region of the bovine CYP11A gene, chimeric DNA constructs comprizing regions of the CYP11A gene fused to a beta-globin-derived reporter gene were transfected into granulosa cells in primary culture.(ABSTRACT TRUNCATED AT 250 WORDS)[7]

Anatomical context of HBB

• Isolated beta-globin chains reproduce, in normal red cell membranes, the defective binding of spectrin to alpha-thalassaemic membranes [8].
• Spectrin-depleted inside-out membrane vesicles (IOVs) derived from membranes incubated with beta-globin chains bound only 9 +/- 3% as much spectrin as IOVs from control membranes incubated with bovine serum albumin [8].
• Collagen alpha 1 type XII, collagen alpha 2 type I, collagen alpha 2 type V, epsilon 4 beta-globin, osteonectin, and uroplakin were expressed at significantly greater levels in ovine Day 17 allantois compared to Day 13 conceptuses [9].
• The amount of beta-globin which was synthesized by calf liver cells varied from 0.3 to 3.5% of the non-alpha globin chains and remained at a low level for all the fetuses which were studied [10].
• Fingerprint analysis of peptides obtained by trypsinolysis of radioactive beta-globin chains revealed that its structure was closely related to that of beta-globin, isolated from cow bone marrow cells [10].

Associations of HBB with chemical compounds

• A radioactive beta-globin fraction was isolated by chromatography on carboxymethyl-cellulose from hemolysates, which were first fractionated on Sephadex G-100 [10].
• We replaced the residues proline beta5(A2), arginine beta104(G6), and tyrosine beta130(H8) of human Hb by the residues present in bovine beta-globin, namely alanine, lysine, and phenylalanine, respectively [11].

Other interactions of HBB

• These studies show that isolated beta-globin chains (but not alpha-globin chains) can produce a spectrin-binding defect in normal red cell membranes similar to that seen in alpha thalassaemia [8].
• Significant deviations from Hardy-Weinberg equilibrium occurred in some populations at the HBB and TF loci [12].

References