Complete structure of the murine p36 (annexin II) gene. Identification of mRNAs for both the murine and the human gene with alternatively spliced 5′ noncoding exons

Fey, Marianne; Moffat, Graeme J.; Vik, D P; Meisenhelder, Jill; Saris, Christiaan J. M.; Hunter, Tony; Tack, Brian F.

doi:10.1016/0167-4781(95)00238-3

Cited by 13 publications

(11 citation statements)

References 64 publications

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“…Our data on the predominance of eNOS expression from Northern blot analysis contrasts with those from previous RT‐PCR studies, (22,26,40) which collectively suggest that all three NOS isoforms are expressed in a variety of osteoblast‐like cells, cell lines, and fresh bone biopsies. Many studies have observed a similar discrepancy, where RT‐PCR detectable transcripts, presumably with very low abundance, were undetectable by either Northern blot analysis or immunocytochemistry (41–45) . This difference may be ascribed to the RT‐PCR technique which is useful for detecting particularly rare transcripts but less useful for comparing relative abundance.…”

Section: Discussionmentioning

confidence: 97%

Mechanical Strain Stimulates Nitric Oxide Production by Rapid Activation of Endothelial Nitric Oxide Synthase in Osteocytes

Zaman

Pitsillides

Rawlinson

et al. 1999

Journal of Bone and Mineral Research

226

138

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Previous studies have indicated that physiological levels of dynamic mechanical strain produce rapid increases in nitric oxide (NO) release from rat ulna explants and primary cultures of osteoblast-like cells and embryonic chick osteocytes derived from long bones. To establish the mechanism by which loading-induced NO production may be regulated, we have examined: nitric oxide synthase (NOS) isoform mRNA and protein expression, the effect of mechanical loading in vivo on NOS mRNA expression, and the effect of mechanical strain on NO production by bone cells in culture. Using Northern blot analyses, in situ hybridization, and immunocytochemistry we have established that the predominant NOS isoform expressed in rat long bone periosteal osteoblasts and in a distinct population of cortical bone osteocytes is the endothelial form of NOS (eNOS), with little or no expression of the inducible NOS or neuronal NOS isoforms. In contrast, in non-load-bearing calvariae there are no detectable levels of eNOS in osteocytes and little in osteoblasts. Consistent with these observations, ulnar explants release NO rapidly in response to loading in vitro, presumably through the activation of eNOS, whereas calvarial explants do not. The relative contribution of different bone cells to these rapid increases in strain-induced NO release was established by assessment of medium nitrite (stable NO metabolite) concentration, which showed that purified populations of osteocytes produce significantly greater quantities of NO per cell in response to mechanical strain than osteoblast-like cells derived from the same bones. Using Northern blot hybridization, we have also shown that neither a single nor five consecutive daily periods of in vivo mechanical loading produced any significant effect on different NOS isoform mRNA expression in rat ulnae. In conclusion, our results indicate that eNOS is the prevailing isoform expressed by cells of the osteoblast/osteocyte lineage and that strain produces increases in the activity of eNOS without apparently altering the levels of eNOS

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Section: Discussionmentioning

confidence: 97%

Mechanical Strain Stimulates Nitric Oxide Production by Rapid Activation of Endothelial Nitric Oxide Synthase in Osteocytes

Zaman

Pitsillides

Rawlinson

et al. 1999

Journal of Bone and Mineral Research

226

138

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“…Similarly, alternative splicing of annexin A2 transcripts in mice results in the formation of two isoforms, one of which has low abundance. The splicing occurs in the 5′-untranslated region (5′-UTR), in which a 70 nucleotide non-coding exon2 insertion between the exon 1 and exon 3 results in difference in translation and transport of the mRNA between the two isoforms [62]. In rats isoform 2 an additional 6 nucleotides between exon 3 and 4 translates into and additional serine residue in the amino-terminal region, and provides another serine phosphorylation site [63].…”

Section: Transcriptional Regulation Of Annexin A2mentioning

confidence: 99%

Annexin A2 Heterotetramer: Structure and Function

Bharadwaj

Bydoun

Holloway

et al. 2013

IJMS

249

346

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Annexin A2 is a pleiotropic calcium- and anionic phospholipid-binding protein that exists as a monomer and as a heterotetrameric complex with the plasminogen receptor protein, S100A10. Annexin A2 has been proposed to play a key role in many processes including exocytosis, endocytosis, membrane organization, ion channel conductance, and also to link F-actin cytoskeleton to the plasma membrane. Despite an impressive list of potential binding partners and regulatory activities, it was somewhat unexpected that the annexin A2-null mouse should show a relatively benign phenotype. Studies with the annexin A2-null mouse have suggested important functions for annexin A2 and the heterotetramer in fibrinolysis, in the regulation of the LDL receptor and in cellular redox regulation. However, the demonstration that depletion of annexin A2 causes the depletion of several other proteins including S100A10, fascin and affects the expression of at least sixty-one genes has confounded the reports of its function. In this review we will discuss the annexin A2 structure and function and its proposed physiological and pathological roles.

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“…This suggests that vertebrate annexins derived from at least two related but distinct progenitors and that most are likely to be mutual duplication products. Human [19,20] and mouse [21,22] annexin II thus show greatest sequence divergence from their annexin VII counterparts [23,24] but have core gene structures virtually identical to the five annexin I genes [25][26][27][28], human annexin III [29], human [30,31], chick [32,33] and rat [34] annexin V and both halves of the human annexin VI octad [35]. Fragmentary data for human annexin IV [36] and bovine XI [37] do not currently permit their association with either the annexin II or VII archetypes, but for phylogenetic reasons (see later) they and annexin VIII are expected to resemble annexin II.…”

Section: Annexin Gene Structures and Organizationmentioning

confidence: 99%

“…The TATA element of annexin II lies in a region extensively rich in G+C content and its composite core promoter may therefore use both TATA and initiator Reviews (Inr) elements. This ensures transcription initiation for important housekeeping functions and may affect alternative splicing of the recently discovered cassette exon 2 in human [20] and mouse [22] annexins II. Annexin V has also recently been found to possess a composite promoter that is split into a distal TATA-containing promoter and a proximal Inr-containing promoter 7 kb downstream [34].…”

Section: Annexin Gene Structures and Organizationmentioning

confidence: 99%

Annexin gene structures and molecular evolutionary genetics

Morgan

Fernández

1997

Cellular and Molecular Life Sciences (CMLS)

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Annexins provide an exemplary model for studying the pattern and process of molecular evolution in multigene families. Their related gene structures, broad dispersal in eukaryotic genomes and abundant coding sequences permit a phylogenetic reconstruction of their genetic history. The emerging picture is one of prolific expansion by gene duplication to more than 27 paralogous subfamilies that have undergone steady sequence divergence, speciation and differential selection. Homologous recombination via the common tetrad of internal repeats has, nevertheless, strictly preserved this core structure for over 1200 million years, implying a basic functional role. The existence of multiple annexins with unique 5' coding and regulatory regions has facilitated their adaptation to the varying ontogenetic and cell-specific needs of diverse organisms. Computational and cladistic sequence analyses have permitted the determination of original gene duplication dates and mutation rates for the ten known vertebrate annexins. Molecular genetic and evolutionary studies of annexins can help to define their structure-function relationships elucidate their individual physiological roles and ultimately link them to hereditary phenotypes.

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Complete structure of the murine p36 (annexin II) gene. Identification of mRNAs for both the murine and the human gene with alternatively spliced 5′ noncoding exons

Cited by 13 publications

References 64 publications

Mechanical Strain Stimulates Nitric Oxide Production by Rapid Activation of Endothelial Nitric Oxide Synthase in Osteocytes

Mechanical Strain Stimulates Nitric Oxide Production by Rapid Activation of Endothelial Nitric Oxide Synthase in Osteocytes

Annexin A2 Heterotetramer: Structure and Function

Annexin gene structures and molecular evolutionary genetics

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