Disease relevance of SPAG5

• The Range of Tumor Extension Should Have Precedence over the Location of the Deepest Tumor Center in Determining the Regional Lymph Node Grouping for Widely Extending Esophageal Carcinomas [1].
• When pathological AFV changes are present, especially if the examination is performed by a not so expert sonographer, biometric measurements (Single Deepest Pocket, Amniotic Fluid Index, Two-Diameter Pocket) with their respective reference ranges might be helpful in confirming the diagnosis of oligohydramnios or hydramnios [2].

High impact information on SPAG5

• Astrin associates with spindle microtubules as early as prophase where it concentrates at spindle poles [3].
• Astrin also localizes to kinetochores but only on those chromosomes that have congressed [3].
• 1,25-Dihydroxyvitamin D3 (1,25-(OH)2D3) regulates the expression of c-myc protooncogene in HL-60 promyelocytic leukemia cells (Reitzma, P. H., Rothberg, P. G., Astrin, S. M., Trial, J., Barshavit, Z., Hall, A., Teitelbaum, S. U., and Kahn, A. J. (1983) Nature 306, 492-494) [4].
• Silencing of astrin in HeLa cells by RNA interference resulted in growth arrest, with formation of multipolar and highly disordered spindles [5].
• Cells depleted of astrin were normal during interphase but were unable to progress through mitosis and finally ended in apoptotic cell death [5].

Biological context of SPAG5

• The mitotic-spindle-associated protein astrin is essential for progression through mitosis [5].
• Western blotting assays of rat somatic cells and male germ cells at different stages of development using anti-Spag5 antibodies demonstrated that the protein expression pattern changes during spermatogenesis and that sperm tails contain a 58 kDa Spag5 protein [6].
• These findings suggest that the silencing of astrin induce a p53-dependent apoptosis and has an additive effect on paclitaxel treatment [7].
• We silenced the expression of astrin protein and tested the cell viability in response to paclitaxel treatment in paclitaxel-sensitive and paclitaxel-resistant cells [7].
• Astrin is a microtubule-associated protein and localizes with mitotic spindles in the M-phase [7].

Anatomical context of SPAG5

• Astrin is a mitotic-spindle-associated protein expressed in most human cell lines and tissues [5].
• Multiple tissue Northern blot analysis showed that hMAP126 was abundantly expressed in the testis [8].
• Our data demonstrate that Spag5 has different localization in somatic versus male germ cells suggesting the possibility of different function [6].
• Use of affinity-purified anti-Spag5 antibodies in immuno electron microscopy shows that in rat elongated spermatids and epididymal sperm the Spag5 protein associates with ODF, but not with the axonemal MTs [6].
• RT PCR assays indicated expression of Spag5 in various tissues and in somatic cells Spag5 localizes to endoplasmic reticulum and microtubules, as expected for an Astrin orthologue [6].

Associations of SPAG5 with chemical compounds

• All the experiments were conducted with a blood sample of the common 1-1 phenotype [Astrin, K. H., Bishop, D. F., Wetmur, J. G., Kaul, B., Davidow, B. & Desnick, R. J. (1987) Ann. NY Acad. Sci. 514, 23-29] [9].

Analytical, diagnostic and therapeutic context of SPAG5

• Sequence analysis revealed that astrin has an N-terminal globular domain and an extended coiled-coil domain [5].
• Recombinant astrin was purified and characterized by CD spectroscopy and electron microscopy [5].
• One novel gene product, hMAP126, was demonstrated to interact with p29 in the yeast two-hybrid assay [8].
• These findings suggested that the Spag5 is essential for testis development in rats and that the hgn/hgn rat is a unique animal model for studying the function of Spag5 [10].

References