Disease relevance of ANXA4

• Comparison of the expression of native and mutant bovine annexin IV in Escherichia coli using four different expression systems [1].

High impact information on ANXA4

• Partial amino acid sequences of p33/41 are highly homologous to those of calcium/phospholipid-binding annexin protein, annexin IV (endonexin), p33/41 exhibited similar calcium/phospholipid-binding activity (Kojima, K., Ogawa, H., Seno, N., Yamamoto, K., Irimura, T., Osawa, T., and Matsumoto, I. (1993) J. Biol. Chem. 267, 20536-20539) [2].
• The deduced amino acid sequence was identical to that of bovine annexin IV except for one amino acid substitution [2].
• Phosphorylation mutants elucidate the mechanism of annexin IV-mediated membrane aggregation [3].
• The propensity of several annexins to generate similar trimeric arrays supports the hypothesis that trimeric complexes of such annexins, including annexin IV, may represent the functional units that interact with membranes [4].
• SP-A bound to annexin IV under conditions where contaminated lipid was removed [5].

Biological context of ANXA4

• Combinatorial mutagenesis of the four domains of annexin IV: effects on chromaffin granule binding and aggregating activities [6].
• The study shows that while bovine brain PAPII shares many of the characteristics of PAPII from other mammalian tissues, its substrate specificity is not as narrow as previously reported [7].

Anatomical context of ANXA4

• In immunoblot, annexin IV purified from bovine rod outer segments cross-reacted with antibodies against annexin IV from bovine liver [8].
• Highly polarized expression of carbohydrate-binding protein p33/41 (annexin IV) on the apical plasma membrane of epithelial cells in renal proximal tubules [9].

Associations of ANXA4 with chemical compounds

• Site-directed mutagenesis was used to change the conserved acidic residues (D/E) in these sequences to alanine residues in each of the four domains of bovine annexin IV, singly or in combinations [6].
• Site-directed mutants that either mimic (Thr6Asp, T6D) or prevent (Thr6Ala, T6A) phosphorylation of threonine 6 were produced for these studies and compared with wild-type annexin IV [3].
• These fluorimetric assays offer expeditious alternatives to the existing radiolabeled thyrotropin-releasing hormone assays for the determination of PAPII activity [10].
• The isolated proteins (PAP I-a, PAP I-b and PAP II) were homogeneous in various methods including 7.5% and 20% gel electrophoresis or gel chromatography, and share, in the extract, 85% of the total of the acidic proteins that migrate with the bromophenol blue marker in 7.5% gels [11].

Other interactions of ANXA4

• However, the augmentation of aggregation of the lung lamellar bodies by annexin IV was attenuated when the lamellar bodies were preincubated with polyclonal anti-SP-A antibodies [5].

Analytical, diagnostic and therapeutic context of ANXA4

• Site-directed mutagenesis, electron microscopy, and X-ray crystallography were used to probe the structural basis of annexin IV-induced membrane aggregation and the inhibition of this property by protein kinase C phosphorylation [3].

References