The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha.

Jindal, Hitesh K.; Chaney, William G.; Anderson, Christopher W.; Davis, Randall G.; Vishwanatha, Jamboor K.

doi:10.1016/s0021-9258(19)67770-7

Cited by 89 publications

(8 citation statements)

References 39 publications

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“…As a member of the primer recognition protein complex, ANXA2 monomers in nucleus stimulate DNA synthesis, cell division and proliferation of cells by promoting transition into the G1-S phase. [115][116][117] ANXA2 exists in the nucleus in low concentrations, which largely depends on the nuclear export regulation site located at the N-terminal of ANXA2 and the adjacent NES. 118 After being modified to expose NES, the site can lead to the export of ANXA2 from the nucleus.…”

Section: How Does Anxa2 Participate In Cell Proliferation and Act As ...mentioning

confidence: 99%

Annexin A2: The diversity of pathological effects in tumorigenesis and immune response

Huang

Jia

Yang

et al. 2022

Intl Journal of Cancer

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Annexin A2 (ANXA2) is widely used as a marker in a variety of tumors. By regulating multiple signal pathways, ANXA2 promotes the epithelial‐mesenchymal transition, which can cause tumorigenesis and accelerate thymus degeneration. The elevated ANXA2 heterotetramer facilitates the production of plasmin, which participates in pathophysiologic processes such as tumor cell invasion and metastasis, bleeding diseases, angiogenesis, inducing the expression of inflammatory factors. In addition, the ANXA2 on the cell membrane mediates immune response via its interaction with surface proteins of pathogens, C1q, toll‐like receptor 2, anti‐dsDNA antibodies and immunoglobulins. Nuclear ANXA2 plays a role as part of a primer recognition protein complex that enhances DNA synthesis and cells proliferation by acting on the G1‐S phase of the cell. ANXA2 reduction leads to the inhibition of invasion and metastasis in multiple tumor cells, bleeding complications in acute promyelocytic leukemia, retinal angiogenesis, autoimmunity response and tumor drug resistance. In this review, we provide an update on the pathological effects of ANXA2 in both tumorigenesis and the immune response. We highlight ANXA2 as a critical protein in numerous malignancies and the immune host response.

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Section: How Does Anxa2 Participate In Cell Proliferation and Act As ...mentioning

confidence: 99%

Annexin A2: The diversity of pathological effects in tumorigenesis and immune response

Huang

Jia

Yang

et al. 2022

Intl Journal of Cancer

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“…As a monomer, ANXA2 is found in both the cytosol and nucleus, but predominantly in the cytosol 15,16 . The function of the ANXA2 monomer in the nucleus was suggested by its purification as part of a primer recognition protein complex that enhances DNA polymerase α activity in vitro 17–19 …”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…15,16 The function of the ANXA2 monomer in the nucleus was suggested by its purification as part of a primer recognition protein complex that enhances DNA polymerase α activity in vitro. [17][18][19] Through S100A10, ANXA2 has been reported to function as a co-receptor for tissue plasminogen activator (tPA) at the cell surface. 20 In a previous report, it was shown that depletion of ANXA2 in telomerase immortalized microvascular endothelial cells led to the loss of plasminogen binding and plasmin generation similar to when S100A10 was depleted.…”

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confidence: 99%

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The association between Annexin A2 and epithelial cell adhesion molecule in breast cancer cells

et al. 2021

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Background: The epithelial cell adhesion molecule (EpCAM) is a type I transmembrane and glycosylated protein, which is overexpressed in many neoplasms. However, EpCAM has no known ligand partners and the mechanisms by which it functions are not fully understood.Aim: This study was performed to discover novel partners of EpCAM, which may provide a better understanding of its functions. Methods:The membrane fraction of the ERα + noninvasive breast cancer cell line ZR-75-1 and MCF-7 was extracted and followed by co-immunoprecipitation of EpCAM using C-10, a mouse monoclonal antibody raised against amino acids 24-93 of the EpCAM molecule. As a negative control, MDA-MB-231 and Hs578T were used since they express a negligible amount of EpCAM and are known as EpCAM À/ low ERα À/low invasive and tumorigenic breast cancer cell lines.Results: Annexin A2 (ANXA2) was found to be selectively and differentially co-immunoprecipitated with EpCAM in the ERα + breast cancer cells MCF-7 and ZR-75-1.ANXA2 is a multifunctional protein and known to act as a co-receptor for tissue plasminogen activator (tPA) on the surface of endothelial and cancer cells, thereby affecting fibrinolytic activity and neoangiogenesis as well as invasive and metastatic properties. In this study, the association between EpCAM and ANXA2 was found to affect the activity of tPA. Conclusion:This study concludes that ANXA2 co-localizes with EpCAM at the plasma membrane, and the co-localization may have functional implications. Data suggest that EpCAM supports ANXA2 to function as a co-receptor for the tPA, and that EpCAM has a regulatory function on the expression and subcellular localization of ANXA2.

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“…Annexin II (p36 ; Saris et al ., 1986 ;Huang et al ., 1986), is the dominant phosphorylated protein in Rous sarcoma virus transformed fibroblasts, leading to the suggestion that it is a substrate for the p60°-5« tyrosine kinase (Erikson and Erikson, 1980) . Monomeric annexin II and phosphoglycerate kinase have also been implicated (Jindal and Vishwanotha, 1990 ;Jindal et al ., 1991) as the two cofactors in the "primer recognition protein complex" that interacts with DNA polymerase a, the enzyme responsible for synthesizing the lagging strand of DNA during DNA replication . Annexin III is identical to inositol 1 :2 cyclic phosphate 2-phosphohydrolase (Ross et al ., 1990) and probably controls the intracellular levels of all inositol cyclic phosphates.…”

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confidence: 99%

A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin.

Wice

Gordon

1992

The Journal of Cell Biology

101

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Abstract. The human intestinal epithelium is rapidly and perpetually renewed as the descendants of multipotent stem cells located in crypts undergo proliferation, differentiation, and eventual exfoliation during a very well organized migration along the crypt to villus axis. The mechanisms that establish and maintain this balance between proliferation and differentiation are largely unknown . We have utilized HT29 cells, derived from a human colon adenocarcinoma, as a model system for identifying gene products that may regulate these processes . Proliferating HT-29 cells cultured in the absence of glucose (e.g., using inosine as the carbon source) have some of the characteristics of undifferentiated but committed crypt epithelial cells while postconfluent cells cultured in the absence of glucose resemble terminally differentiated enterocytes or goblet cells . A cDNA library, constructed from exponentially growing HT-29 cells maintained in inosine-containing media, was sequentially screened with a series of probes depleted of sequences encoding housekeeping functions and enriched for intestine-specific sequences that are expressed in proliferating committed, but not differentiated, epithelial cells. Of 100,000 recombinant phage surveyed, one was found whose cDNA was derived from an apparently gut-specific mRNA.

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The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha.

Cited by 89 publications

References 39 publications

Annexin A2: The diversity of pathological effects in tumorigenesis and immune response

Annexin A2: The diversity of pathological effects in tumorigenesis and immune response

The association between Annexin A2 and epithelial cell adhesion molecule in breast cancer cells

A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin.

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