Calcyclin as a marker of human epithelial cells and fibroblasts

Kuźnicki, Jacek; Kordowska, Jolanta; Puzianowska, Monika; Woźniewicz, B

doi:10.1016/0014-4827(92)90191-a

Cited by 73 publications

(57 citation statements)

References 10 publications

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“…S100A6 was originally identified in Ehrlich ascites tumor (EAT) 1 cells (16,17). It was later established that S100A6 is mainly present in epithelial cells and fibroblasts (18). We found that in EAT cells of epithelial origin, S100A6 bound a protein with a molecular mass of about 30 kDa in a Ca 2ϩ -dependent manner (19).…”

mentioning

confidence: 93%

CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

Filipek¹,

Jastrzębska²,

Nowotny³

et al. 2002

Journal of Biological Chemistry

135

107

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Recently, a human ortholog of mouse calcyclin (S100A6)-binding protein (CacyBP) called SIP (Siah-1-interacting protein) was shown to be a component of a novel ubiquitinylation pathway regulating ␤-catenin degradation (Matsuzawa, S., and Reed, J. C. (2001) Mol. Cell 7, 915-926). In murine brain, CacyBP/SIP is expressed at a high level, but S100A6 is expressed at a very low level. Consequently we carried out experiments to determine if CacyBP/SIP binds to other S100 proteins in this tissue. Using CacyBP/SIP affinity chromatography, we found that S100B from the brain extract binds to CacyBP/SIP in a Ca 2؉ -dependent manner. Using a nitrocellulose overlay assay with 125 I-CacyBP/SIP and CacyBP/SIP affinity chromatography, we found that this protein binds purified S100A1, S100A6, S100A12, S100B, and S100P but not S100A4, calbindin D 9k , parvalbumin, and calmodulin.

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mentioning

confidence: 93%

CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

Filipek¹,

Jastrzębska²,

Nowotny³

et al. 2002

Journal of Biological Chemistry

135

107

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“…S100A6 was additionally identified and purified from murine Ehrlich ascites tumor cells (18) and Gou et al (19) described a correlation between the expression of S100A6 and the metastatic behavior of Ras-transformed NIH 3T3 fibroblasts. In benign tissues, S100A6 is expressed predominantly in fibroblasts and epithelial cells (20) but is also present in neuronal and smooth muscle cells. To elucidate the in vivo function(s) of S100A6 recent efforts focused on the identification of cellular binding partners and the metal-binding characteristics (21).…”

mentioning

confidence: 99%

“…The localization of S100A6 has been also studied in transformed (15,29) or normal tissues (20,30), and in cultured smooth muscle cells (31) using a polyclonal antibody. In this study we have reinvestigated the Ca 2ϩ -dependent subcellular localization of S100A6 using a novel highly specific monoclonal antibody and show that the protein localizes to the plasma * This work was supported by the Austrian Science Foundation (P-11845).…”

mentioning

confidence: 99%

Ca2+-dependent Association of S100A6 (Calcyclin) with the Plasma Membrane and the Nuclear Envelope

Stradal

Gimona

1999

Journal of Biological Chemistry

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Expression of S100A6 (Calcyclin), a member of the S100 family and of Zn 2؉ -binding proteins is elevated in a number of malignant tumors. In vitro the protein associates with several actin-binding proteins and annexins in a Ca 2؉ -dependent manner. We have now studied the subcellular localization of S100A6 using a new, specific monoclonal antibody. Immunofluorescence microscopy of unfixed, ultrathin, frozen sections demonstrated a dual localization of S100A6 at the nuclear envelope and the plasma membrane of porcine smooth muscle only in the presence of Ca 2؉ . The same localization was found by immunofluorescence and immunogold electron microscopy as well as by confocal laser scanning microscopy with cultured, fixed, human CaKi-2 and porcine ST interphase cells. Upon cell division, however, S100A6 was found exclusively in the cytoplasm. Cell fractionation studies showed that S100A6 was present in the microsomal fraction in the presence of Ca 2؉ and was released from this fraction by the addition of EGTA/ EDTA but not by Triton X-100. The data demonstrate that S100A6 is localized both at the plasma membrane and the nuclear envelope in vivo and suggest a Ca 2؉ -dependent interaction with annexins or other components of the nuclear envelope.

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“…S100A6 was identified from melanoma tissue samples by comparing melanocytic lesions from normal nevi [214]. S100A6 is most abundant in epithelial cells and fibroblasts but is also found, in smaller amounts, in other cell-types such as neurons, glial cells, smooth muscle cells, cardiac myocytes, platelets and lymphocytes [215,216](reviewed in [217]). S100A6 has been found elevated in a large number of cancer types which include colorectal cancer, pancreatic, hepato-cellular carcinoma, melanoma, lung cancer and gastric cancer [165,[218][219][220][221][222][223][224](reviewed in [217]).…”

Section: S100a6mentioning

confidence: 99%

RAGE and Its Ligands in Melanoma

Leclerc¹

2015

Melanoma - Current Clinical Management and Future Therapeutics

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Calcyclin as a marker of human epithelial cells and fibroblasts

Cited by 73 publications

References 10 publications

CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

Ca2+-dependent Association of S100A6 (Calcyclin) with the Plasma Membrane and the Nuclear Envelope

RAGE and Its Ligands in Melanoma

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