Complex formation and submembranous localization of annexin 2 and S100A10 in live HepG2 cells

Zobiack, Nicole; Gerke, Volker; Rescher, Ursula

doi:10.1016/s0014-5793(01)02604-7

Cited by 48 publications

(40 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Taken together, S100A10 and annexin II formed a complex on the outer surface of RCC10RGB9 cells, as reported in other cultured cancer cells. (5)(6)(7) Exactly the same result was obtained with TUHR14TKB cells (data not shown).…”

Section: Resultssupporting

confidence: 78%

“…(5)(6)(7) In the present study, we estimated the gene expression of S100A10 and annexin II by reverse transcription-polymerase chain reaction (RT-PCR) in a larger number of surgically resected RCC samples (n = 47) after standardization for the expression of β-actin in each sample. Then we immunohistochemically investigated the expression of S100A10 and annexin II in RCC and normal kidney tissues (n = 13).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Evaluation of S100A10, annexin II and B‐FABP expression as markers for renal cell carcinoma

et al. 2006

View full text Add to dashboard Cite

This study aimed to analyze expression of S100A10, annexin II and B-FABP genes in renal cell carcinoma (RCC) and their potential value as tumor markers. Furthermore, any correlation between the gene expression and prognostic indicators of RCC was analyzed. Expression of each gene was estimated by RT-PCR in the nonneoplastic (normal) and tumorous parts of resected kidney samples. Also, each antigen was immunostained in RCC and normal kidney tissues. Expression of the S100A10 gene averaged 2.5-fold higher in the tumor than that in the normal tissues (n = 47), after standardization against that of β β β β-actin. However, expression of annexin II, a natural ligand of S100A10, was only 1.64-fold higher. In the tissue sections of RCC, S100A10 and annexin II were immunostained in membranes. In the normal renal epithelia, however, both antigens were stained in the Bowman's capsule and the tubules from Henle's loop through the collecting duct system, but not in the proximal tubules, from where most RCC are derived. In contrast, expression of the B-FABP gene was 20-fold higher in the tumor. No B-FABP was immunohistochemically detected in normal kidney sections, but it was stained in the cytoplasm of RCC tissue sections. S100A10 and B-FABP genes were overexpressed regardless of nuclear grade and stage of RCC. Immunopositivity in RCC tissues (n = 13) was 100% for S100A10 and annexin II, and 70% for B-FABP; however, no clear relationship was observed in either antigen with nuclear grade and stage. It was found that all three performed well as RCC markers. B-FABP was most specific to RCC, as it was expressed little in normal kidney tissues. (Cancer Sci 2007; 98: 77-82) W e have previously described the overexpression of S100A10 in renal cell carcinoma (RCC) cells compared with the normal human kidney cDNA library.(1) Such overexpression has been confirmed in RCC and non-neoplastic (normal) tissues in surgically resected kidneys (n = 7).(1,2) S100A10 is a member of the S100 family of proteins that are small acidic calcium-binding proteins with two helix-loop-helix EF-hand motifs. Twenty human S100 family members are expressed in a cell-and tissue-specific manner, and are responsible for a variety of cellular processes including cell proliferation and differentiation.(3,4) Sixteen of their genes (designated S100A1-S100A16) are clustered on the chromosome 1q21 region, where a number of chromosomal abnormalities occur with neoplasias.(4) S100A10 forms a heterotetramer with annexin II (S100A10) 2 (annexin II) 2 , and the complex localizes in the extracellular membrane of various cancer cells. In the present study, we estimated the gene expression of S100A10 and annexin II by reverse transcription-polymerase chain reaction (RT-PCR) in a larger number of surgically resected RCC samples (n = 47) after standardization for the expression of β-actin in each sample. Then we immunohistochemically investigated the expression of S100A10 and annexin II in RCC and normal kidney tissues (n = 13). The extracellular S100A10/ annexin II complex f...

show abstract

Section: Resultssupporting

confidence: 78%

mentioning

confidence: 99%

Evaluation of S100A10, annexin II and B‐FABP expression as markers for renal cell carcinoma

et al. 2006

View full text Add to dashboard Cite

show abstract

“…A quantitative analysis detected the subplasmalemmal localization of annexin II in B60% of the NHP2 cells, whereas 100% of the NHP2 cells showed cytoplasmic staining of annexin II (Table 1). The submembranous distribution of annexin II, previously also observed in other cells (Huang et al, 1986;Ma and Ozers, 1996;Zobiak et al, 2001), suggests potential annexin IImembrane interactions. Interestingly, annexin II may also be exported outside of cells and the extracellular annexin II has been identified as both soluble and membrane-bound (Hajjar et al, 1994).…”

Section: Reduced As Well As Altered Expression Patterns Of Annexin IIsupporting

confidence: 64%

“…Exactly how the re-expressed annexin II inhibits the migratory ability of prostate cancer cells remains to be determined. It is possible that these annexin II molecules may form complexes with p11 underneath plasma membrane and bind to cytoskeletal molecules, and the II 2 -p11 2 complexes then stabilize cytoskeleton and inhibit cell migration (Thiel et al, 1992;Bianchi et al, 1995;Zobiak et al, 2001). The II 2 -p11 2 complexes may also regulate or stabilize, through unknown mechanisms, the intermediate filament, a major cytoskeletal component that helps to maintain the mechanical stability of cells and serves as attachment sites for cell organelles and cytoplasmic molecules, which in turn limits cell migration (Ikebuchi and Waisman, 1990;Bianchi et al, 1995).…”

Section: Annexin II Inhibits Migration Of Prostate Cancer Cellsmentioning

confidence: 99%

Annexin II expression is reduced or lost in prostate cancer cells and its re-expression inhibits prostate cancer cell migration

et al. 2003

View full text Add to dashboard Cite

While studying Bim, a BH3-only proapoptotic protein, we identified an B36 kDa protein, which was abundantly expressed in all five strains of primary normal human prostate (NHP) epithelial cells but significantly reduced or lost in seven prostate cancer cell lines. The B36 kDa protein was subsequently identified as annexin II by proteomic approach and confirmed by Western blotting using an annexin II-specific antibody. Conventional and 2D SDS-PAGE, together with Western blotting, also revealed reduced or lost expression of annexin I in prostate cancer cells. Subcellular localization studies revealed that in NHP cells, annexin II was distributed both in the cytosol and underneath the plasma membrane, but not on the cell surface. Prostate cancer cells showed reduced levels as well as altered expression patterns of annexin II. Since annexins play important roles in maintaining Ca 2+ homeostasis and regulating the cytoskeleton and cell motility, we hypothesized that the reduced or lost expression of annexin I/II might promote certain aggressive phenotypes of prostate cancer cells. In subsequent experiments, we indeed observed that restoration of annexin II expression inhibited the migration of the transfected prostate cancer cells without affecting cell proliferation or apoptosis. Hence, our results suggest that annexin II, and, likely, annexin I, may be endogenous suppressors of prostate cancer cell migration and their reduced or lost expression may contribute to prostate cancer development and progression.

show abstract

“…Annexin A2 associates with lipid raft microdomains (both caveolar and non-caveolar, shown previously in smooth muscle) (14), whereas annexin A1 binds to nonraft regions. The annexins also exist as both monomeric and heterotetrameric forms with their binding partners S100A10 (with annexin A2) and S100A11 (with annexin A1) (37). b, a disruption of the sarcolemmal membrane results in the influx of Ca 2ϩ that activates the patch fusion process.…”

Section: Figmentioning

confidence: 99%

Dysferlin Interacts with Annexins A1 and A2 and Mediates Sarcolemmal Wound-healing

Lennon¹,

Kho

Bacskai

et al. 2003

Journal of Biological Chemistry

355

371

View full text Add to dashboard Cite

Mutations in the dysferlin gene cause limb girdle muscular dystrophy type 2B and Miyoshi myopathy. We report here the results of expression profile analyses and in vitro investigations that point to an interaction between dysferlin and the Ca 2؉ and lipid-binding proteins, annexins A1 and A2, and define a role for dysferlin in Ca 2؉ -dependent repair of sarcolemmal injury through a process of vesicle fusion. Expression profiling identified a network of genes that are co-regulated in dysferlinopathic mice. Co-immunofluorescence, co-immunoprecipitation, and fluorescence lifetime imaging microscopy revealed that dysferlin normally associates with both annexins A1 and A2 in a Ca 2؉ and membrane injurydependent manner. The distribution of the annexins and the efficiency of sarcolemmal wound-healing are significantly disrupted in dysferlin-deficient muscle. We propose a model of muscle membrane healing mediated by dysferlin that is relevant to both normal and dystrophic muscle and defines the annexins as potential muscular dystrophy genes.

show abstract

Complex formation and submembranous localization of annexin 2 and S100A10 in live HepG2 cells

Cited by 48 publications

References 22 publications

Evaluation of S100A10, annexin II and B‐FABP expression as markers for renal cell carcinoma

Evaluation of S100A10, annexin II and B‐FABP expression as markers for renal cell carcinoma

Annexin II expression is reduced or lost in prostate cancer cells and its re-expression inhibits prostate cancer cell migration

Dysferlin Interacts with Annexins A1 and A2 and Mediates Sarcolemmal Wound-healing

Contact Info

Product

Resources

About