Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication

Spano, Furio; Raugei, Giovanni; Palla, Emanuela; Colella, C.; Melli, Marialuisa

doi:10.1016/0378-1119(90)90367-z

Cited by 39 publications

(21 citation statements)

References 36 publications

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“…Comparison of the organization of the annexin V gene with the human and mouse annexin II [23,24] and the pigeon annexin I gene [25] revealed a striking homology: although the genes vary considerably in size (mouse annexin II gene 21 kb, human annexin II gene 40 kb, and chicken annexin V gene 25 kb), the differences are due almost entirely to differences in intron length. Exon sizes are conserved, and the localization of exon borders within the cDNA sequence of chicken annexin V and annexin I and II are identical except for the untranslated regions of the cDNA and the regions coding for the unique amino ends of the proteins (Table I).…”

Section: Resultsmentioning

confidence: 99%

Organisation of the chicken annexin V gene and its correlation with the tertiary structure of the protein

et al. 1993

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Chicken annexin V (anchorin CII) is a collagen binding, membrane-associated molecule with Ca" channel activity. Here we report on the coding sequences, promotor region, size and distribution of exons, and exon-intron junctions of the chicken annexin V gene. It is about 25 kb long and codes for 13 short exons between 50 and 581 bp length. Exon sizes and locations of splice sites are almost completely homologous to those of the human and mouse annexin II or pigeon annexin I genes, although there is only SO-60% homology in the sequence of the corresponding proteins. The four repeat structure and symmetry of the armexin V as evident from sequence and X-ray analysis studies is only partially reflected in this highly conserved exon dist~bution. In the first two repeats of chicken annexin V the exons correlate with protein domains ~n~ining one, two, or three a-helices, while in the repeats 3 and 4 exon junctions and o-helical domains do not correlate. The analysis of the promotor structure revealed the absence of a typical TATA-box, but a GC-rich region which may possibly promote transcription from several start sites.

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Section: Resultsmentioning

confidence: 99%

Organisation of the chicken annexin V gene and its correlation with the tertiary structure of the protein

et al. 1993

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“…The first coding exon is 43 bp long, smaller than the corresponding exons of the annexin I and I genes, and consistent with the fact that the N-terminal sequence prior to the first protein repeat is smaller in annexin VI than in either annexins I or II. The sizes of the remaining coding exons are identical to those of the corresponding exons of the annexin I and II genes (15)(16)(17)(18)(19)(20). The exceptions to this are exon 21 that is only 18 nt and is alternatively spliced (2) and exon 26 that is 406 bp and includes the translation stop codon and 3' untranslated sequence.…”

Section: Resultsmentioning

confidence: 95%

“…Several groups have recently started to investigate the annexin I and II genes to gain insight into the determinants of specific and common patterns of gene regulation. The organization of the annexin I gene is completely conserved among humans, rats, mice, and pigeons (15)(16)(17) (although there are differences in intron sizes); likewise the human and murine annexin II genes are conserved (18,19). Most striking is the observation that the positions of the intron-exon boundaries within the core domains of the annexin I and II genes are almost exactly conserved (20).…”

mentioning

confidence: 72%

“…2 of which 10 out of 26 have split codons. The frequency of split codons in other annexin genes is similar, typically 4 of 12 (15)(16)(17)(18)(19)(20). The first coding exon is 43 bp long, smaller than the corresponding exons of the annexin I and I genes, and consistent with the fact that the N-terminal sequence prior to the first protein repeat is smaller in annexin VI than in either annexins I or II.…”

Section: Resultsmentioning

confidence: 99%

“…The boundaries of exons 4,5,7,8,9,11,13,15,20,23, and 24 were sequenced using complementary pairs of exonspecific oligonucleotides designed to lie in the middle of exons whose positions were predicted from the intron-exon organization of those annexin genes so far characterized (15)(16)(17)(18)(19)(20). Sequencing reactions were performed in the presence of Mn2+ so that sequence close to the primer could be determined, as recommended in the United States Biochemical Sequenase handbook.…”

Section: Methodsmentioning

confidence: 99%

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Structure of the human annexin VI gene.

Smith

Davies

Crumpton

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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We report the structure of the human annexin VI gene and compare the intron-exon organization with the known structures of the human annexin I and II genes. The gene is -60 kbp long and contains 26 exons. Consistent with the published annexin VI cDNA sequence, the genomic sequence at the 3' end does not contain a canonical polyadenylylation signal. The genomic sequence upstream of the transcription start site contains TATAA and CAAT motifs. The spatial organization of the exons does not reveal any obvious similarities between the two halves of the annexin VI gene. Comparison of the intron-exon boundary positions of the annexin VI gene with those of annexins I and U reveals that within the repeated domains the break points are perfectly conserved except for exon 8, which is one codon smaller in annexin H. The corresponding point in the second half of annexin VI is represented by two exons, exons 20 and 21. The latter exon is alternatively spliced, giving rise to two annexin VI isoforms that differ with respect to a 6-amino acid insertion at the start of repeat 7.

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Annexin A2 (ANX A2): An emerging biomarker and potential therapeutic target for aggressive cancers

Sharma

2018

Intl Journal of Cancer

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ANX A2 is an important member of annexin family of proteins expressed on surface of endothelial cells (ECs), macrophages, mononuclear cells and various types of cancer cells. It exhibits high affinity binding for calcium (Ca ) and phospholipids. ANX A2 plays an important role in many biological processes such as endocytosis, exocytosis, autophagy, cell-cell communications and biochemical activation of plasminogen. On the cell surface ANX A2 organizes the assembly of plasminogen (PLG) and tissue plasminogen activator (tPA) for efficient conversion of PLG to plasmin, a serine protease. Proteolytic activity of plasmin is required for activation of inactive pro-metalloproteases (pro-MMPs) and latent growth factors for their biological actions. These activation steps are critical for degradation of extracellular matrix (ECM) and basement proteins (BM) for cancer cell invasion and metastasis. Increased expression of ANX A2 protein/gene has been correlated with invasion and metastasis in a variety of human cancers. Moreover, clinical studies have positively correlated ANX A2 protein expression with aggressive cancers and with resistance to anticancer drugs, shorter disease-free survival (DFS), and worse overall survival (OS). The mechanism(s) by which ANX A2 regulates cancer invasion and metastasis are beginning to emerge. Investigators used various technologies to target ANX A2 in preclinical model of human cancers and demonstrated exciting results. In this review article, we analyzed existing literature concurrent with our own findings and provided a critical overview of ANX A2-dependent mechanism(s) of cancer invasion and metastasis.

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Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication

Cited by 39 publications

References 36 publications

Organisation of the chicken annexin V gene and its correlation with the tertiary structure of the protein

Organisation of the chicken annexin V gene and its correlation with the tertiary structure of the protein

Structure of the human annexin VI gene.

Annexin A2 (ANX A2): An emerging biomarker and potential therapeutic target for aggressive cancers

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