The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Anxa3  -  annexin A3

Rattus norvegicus

Synonyms: 35-alpha calcimedin, Annexin A3, Annexin III, Annexin-3, Anx3, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Anxa3

  • Expression levels were similar in pancreas, where PAP III mRNA concentration increased within 6 h following induction of pancreatitis, reached maximal levels (> 200 times control values) at 24-48 h, and decreased thereafter [1].

High impact information on Anxa3

  • LC3 is present in greater amounts in ductus compared with aorta cells, and overexpression of LC3 in aortic cells by transfection enhances fibronectin mRNA translation to levels observed in ductus cells [2].
  • Immunoelectron microscopy on LC3 revealed specific labelling of autophagosome membranes in addition to the cytoplasmic labelling [3].
  • The deduced amino acid sequence of LC3 is highly conserved between rat and mouse [4].
  • Our anti-LC3 antiserum shows that LC3 is abundant only in neurons and that the majority of LC3 in brain co-purifies with microtubules [4].
  • Consistent with this, overexpression of LC3 decreased the level of active GTP-bound Rac1 in COS cells [5].

Biological context of Anxa3

  • Interestingly, two binding sites exist in LC3 for caldendrin from which only one exhibits a strict Ca(2+)-dependency for the interaction to take place but both require the presence of the first two EF-hands of caldendrin [6].
  • The PAP III coding sequence spanned over six exons [1].
  • Moreover, the rat PAP III gene was mapped to chromosome 4 using mouse-rat hybrid cells, a localization which coincides with that of the PAP I and II genes [1].
  • The autophagy induced in mitotic cells was inhibited by amino acids, and the resulting autophagosomes contained proteins LC3 and Lamp1, known to be associated with autophagosomes in interphase cells [7].
  • The structure of LC3, which is similar to those of Golgi-associated ATPase enhancer of 16 kDa (GATE-16) and GABAA receptor-associated protein (GABARAP), contains a ubiquitin core with two alpha helices, alpha1 and alpha2, attached at its N-terminus [8].

Anatomical context of Anxa3


Associations of Anxa3 with chemical compounds


Other interactions of Anxa3

  • In the intestinal tract, where PAP II is not expressed, the pattern of PAP III expression was comparable with that of PAP I; fasting induced a decrease in its mRNA concentration by more than 80%, which could be reversed within 6 h upon feeding [1].
  • PAP III belongs to the family of pancreatitis-associated proteins, recently characterized as pancreatic secretory proteins structurally related to C-type lectins, and whose expression is induced during the acute phase of pancreatitis [1].

Analytical, diagnostic and therapeutic context of Anxa3

  • Furthermore, LC3 was colocalized with Sos1 in cells, as determined by immunohistochemistry [5].
  • LC3 protein expression measured by quantitiative immunoblotting is twice as high in postnatal brain as in embryonic and adult brain [14].
  • A polyclonal antibody was raised against PAP III, and a Western blotting analysis using this antibody confirmed an increased level of PAP III protein in the injured nerve [15].
  • The RNA extracts were used for RT-PCR differential display to detect PAP-III gene expression in the stimulated ovarian tissue [11].
  • The molecular form of LC3 was mainly LC3-II, a membrane-bound form, during reperfusion, especially at 30 min of the phase [16].


  1. Cloning, expression and chromosomal localization of the rat pancreatitis-associated protein III gene. Dusetti, N.J., Frigerio, J.M., Szpirer, C., Dagorn, J.C., Iovanna, J.L. Biochem. J. (1995) [Pubmed]
  2. Microtubule-associated protein 1 light chain 3 is a fibronectin mRNA-binding protein linked to mRNA translation in lamb vascular smooth muscle cells. Zhou, B., Boudreau, N., Coulber, C., Hammarback, J., Rabinovitch, M. J. Clin. Invest. (1997) [Pubmed]
  3. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., Yoshimori, T. EMBO J. (2000) [Pubmed]
  4. Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B. Mann, S.S., Hammarback, J.A. J. Biol. Chem. (1994) [Pubmed]
  5. Light Chain 3 associates with a Sos1 guanine nucleotide exchange factor: its significance in the Sos1-mediated Rac1 signaling leading to membrane ruffling. Furuta, S., Miura, K., Copeland, T., Shang, W.H., Oshima, A., Kamata, T. Oncogene (2002) [Pubmed]
  6. Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an association with the microtubule cytoskeleton highlighting exclusive binding partners for neuronal Ca(2+)-sensor proteins. Seidenbecher, C.I., Landwehr, M., Smalla, K.H., Kreutz, M., Dieterich, D.C., Zuschratter, W., Reissner, C., Hammarback, J.A., Böckers, T.M., Gundelfinger, E.D., Kreutz, M.R. J. Mol. Biol. (2004) [Pubmed]
  7. Inhibition of autophagy in mitotic animal cells. Eskelinen, E.L., Prescott, A.R., Cooper, J., Brachmann, S.M., Wang, L., Tang, X., Backer, J.M., Lucocq, J.M. Traffic (2002) [Pubmed]
  8. The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8. Sugawara, K., Suzuki, N.N., Fujioka, Y., Mizushima, N., Ohsumi, Y., Inagaki, F. Genes Cells (2004) [Pubmed]
  9. Differential expression of annexins I-VI in the rat dorsal root ganglia and spinal cord. Naciff, J.M., Kaetzel, M.A., Behbehani, M.M., Dedman, J.R. J. Comp. Neurol. (1996) [Pubmed]
  10. Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes an autophagy-related protein (APG9-like2) highly expressed in trophoblast. Yamada, T., Carson, A.R., Caniggia, I., Umebayashi, K., Yoshimori, T., Nakabayashi, K., Scherer, S.W. J. Biol. Chem. (2005) [Pubmed]
  11. Gonadotropin-induced expression of pancreatitis-associated protein-III mRNA in the rat ovary at the time of ovulation. Yoshioka, S., Fujii, S., Richards, J.S., Espey, L.L. J. Endocrinol. (2002) [Pubmed]
  12. Induced expressions of Rab24 GTPase and LC3 in nerve-injured motor neurons. Egami, Y., Kiryu-Seo, S., Yoshimori, T., Kiyama, H. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  13. The first molecular evidence that autophagy relates rimmed vacuole formation in chloroquine myopathy. Suzuki, T., Nakagawa, M., Yoshikawa, A., Sasagawa, N., Yoshimori, T., Ohsumi, Y., Nishino, I., Ishiura, S., Nonaka, I. J. Biochem. (2002) [Pubmed]
  14. Gene localization and developmental expression of light chain 3: a common subunit of microtubule-associated protein 1A(MAP1A) and MAP1B. Mann, S.S., Hammarback, J.A. J. Neurosci. Res. (1996) [Pubmed]
  15. Expression of Reg/PAP family members during motor nerve regeneration in rat. Namikawa, K., Fukushima, M., Murakami, K., Suzuki, A., Takasawa, S., Okamoto, H., Kiyama, H. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  16. Participation of autophagy in the degeneration process of rat hepatocytes after transplantation following prolonged cold preservation. Lu, Z., Dono, K., Gotoh, K., Shibata, M., Koike, M., Marubashi, S., Miyamoto, A., Takeda, Y., Nagano, H., Umeshita, K., Uchiyama, Y., Monden, M. Arch. Histol. Cytol. (2005) [Pubmed]
WikiGenes - Universities