Structural analysis of a new highly metastatic cell line PaTu 8902 from a primary human pancreatic adenocarcinoma

Elsässer, Hans-P.; Lehr, Ursula; Agricola, Brigitte; Kern, Horst F.

doi:10.1007/bf02915113

Cited by 35 publications

(20 citation statements)

References 6 publications

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“…A similar -/-mouse enterocytes. Fixation of the tissues samples was performed as described by Elsasser et al (Elsasser et al, 1993). Antibody binding was visualised by incubation with a monoclonal anti-LPH antibody and 10 nm immunogoldconjugated goat anti-mouse IgG antibody, as indicated by arrowheads.…”

Section: Discussionmentioning

confidence: 99%

“…For electron microscopy investigations, tissue samples were cut into small pieces of about 1 mm 3 and were immersion-fixed in 2.5% paraformaldehyde, 2.5% glutaraldehyde and 0.05% picric acid in 0.067 M cacodylate buffer of pH 7.4 for 2 hours at 4°C (Elsasser et al, 1993). Standard procedures for dehydration and embedding in Epon were used.…”

Section: Electron Microscopymentioning

confidence: 99%

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Loss of galectin-3 impairs membrane polarisation of mouse enterocytes in vivo

Delacour

Koch

Ackermann

et al. 2008

Journal of Cell Science

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Epithelial cells are characterised by distinct apical and basolateral membrane domains that are separated by tight junctions. Establishment and maintenance of this polarity depend on specific gene expression and protein targeting to their correct location. Our former studies, performed with renal epithelial MDCK cells, revealed a new function for galectin-3, a member of a conserved family of lectins. There, galectin-3 is required for intracellular sorting and correct targeting of non-raft-associated glycoproteins to the apical plasma membrane. In the present study, we found transport defects of the intestinal brush border hydrolases lactase-phlorizin hydrolase (LPH) and dipeptidylpeptidase IV (DPPIV) in galectin-3-null mutant mice. We could show that, in enterocytes of wild-type mice, both glycoproteins directly interact with galectin-3 and transit through non-raft-dependent apical transport platforms. Therefore, this genetic analysis provides definitive evidence for the involvement of galectin-3 in protein intracellular trafficking in vivo. Further investigations revealed that gal3-null enterocytes also exhibit striking cytoarchitecture defects, with the presence of numerous and regular protrusions located along basolateral membranes. Moreover, β-actin and villin, two characteristic markers of brush borders, become abnormally distributed along these atypical basolateral membranes in gal3–/– mice. Taken together, our results demonstrate that, in addition to a pivotal role in apical trafficking, galectin-3 also participates in epithelial morphogenesis in mouse enterocytes.

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Section: Discussionmentioning

confidence: 99%

Section: Electron Microscopymentioning

confidence: 99%

Loss of galectin-3 impairs membrane polarisation of mouse enterocytes in vivo

Delacour

Koch

Ackermann

et al. 2008

Journal of Cell Science

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“…Pancreatic carcinoma cell lines AsPC-1 (ATCC, CRL-1682), BxPC-3 (Tan et al, 1986), MiaPaCa-2 (ATCC, CRL-1420), Panc-1 (ATCC, CRL-1469), PaTu8988t (differentiated) and PaTu8988s (undifferentiated, metastases forming) (these two lines are from the same patient (Elsasser et al, 1993)) were cultured in Dulbecco's Modified Eagle Medium with 10% FCS; Capan-1 (ATCC, HTB-79), SW850 and SW-979 in Click's RPMI Medium with 10% FCS. Cells were seeded in tissue culture dishes and cultured at 378C for 3 -5 days, harvested in sub-confluent state and lysed as described below.…”

Section: Cell Lines and Culture Conditionsmentioning

confidence: 99%

Analysis of the cytochrome c-dependent apoptosis apparatus in cells from human pancreatic carcinoma

2002

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Defects in the apoptotic system are likely to play a role in tumorigenesis. Pancreatic carcinoma cells are extremely resistant to apoptosis induction by chemotherapy suggesting that the apoptosis machinery is faulty. We investigated the integrity of the cytochrome c-dependent apoptotic apparatus in 10 human pancreatic carcinoma cell lines. Expression of Apaf-1, caspase-3, -6, -7, -8 and -9, Hsp-70 and XIAP was detected in all cell lines. The expression levels of Apaf-1 and caspase-8 were homogenous in all cell lines whereas differences in expression of other caspases were seen. In cytosolic fractions, all investigated caspases were processed in response to cytochrome c but the extent of processing varied between the cell lines. No stringent correlation between the amount of processing of caspase-9 and effector caspases was seen. Cytochrome cinduced effector caspase activity was quantitated by enzyme assay. Especially at low concentrations of added cytochrome c, this response varied greatly between the cell lines. These data demonstrate that the apoptotic system downstream of the mitochondria is qualitatively intact in pancreatic carcinoma. They further show that the response to cytochrome c can be quantitated in a cell-free system and that determinants other than mere expression of apoptotic molecules can regulate cytochrome c-induced apoptosis.

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“…The PaTu cell line is a new source of insulin-producing cells for diabetic patients that has overcome the limited availability of islets for transplantation. 11 It was derived from a human pancreatic Grade II adenocarcinoma of ductal origin.…”

Section: Introductionmentioning

confidence: 99%