Regulation of lysosomal and ubiquitin degradative pathways in differentiating human intestinal Caco-2 cells

Zhang, Yan; Wick, Debra A.; Haas, Arthur; Seetharam, Bellur; Dahms, Nancy M.

doi:10.1016/0167-4889(95)00027-p

Cited by 11 publications

(7 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The transcriptional control of various components of the intestinal lysosomal and ubiquitin-dependent degradative pathways have been only partially explored in several in vitro culture models (Zhang et al 1995). Lysosomal delivery of the brush border hydrolases sucrase-isomaltase and dipeptidylpeptidase IV has been described in cultured intestinal epithelial cells (Matter et al 1990).…”

Section: Cdx2 and Endo-lysosomal Functionmentioning

confidence: 99%

Cdx2 regulates endo-lysosomal function and epithelial cell polarity

Gao¹,

Kaestner²

2010

Genes Dev.

View full text Add to dashboard Cite

In contrast to our significant understanding of signaling cascades that determine cell polarity in lower eukaryotic or immortalized cells, little is known about the transcriptional program that governs mammalian epithelial polarization in vivo. Here we show, using conditional gene ablation and three-dimensional tissue culture, that the homeobox transcription factor Cdx2 controls apical-basolateral polarity in mouse enterocytes and human colonic epithelial cells. Cdx2 regulates a comprehensive gene network involved in endo-lysosomal maturation and protein transport. In the absence of Cdx2, defective protein trafficking impairs apical-basal transport and induces ectopic lumen formation. These defects are partially recapitulated by suppression of key apical transport components, Rab11a and Kif3b, which are regulated by Cdx2. Furthermore, Cdx2 deficiency affects components that control the organization of microvillus actin cytoskeleton, leading to severe microvillus atrophy. These results demonstrate that Cdx2 regulates epithelial cell polarity and morphogenesis through control of apical protein transport and endo-lysosomal function.

show abstract

Section: Cdx2 and Endo-lysosomal Functionmentioning

confidence: 99%

Cdx2 regulates endo-lysosomal function and epithelial cell polarity

Gao¹,

Kaestner²

2010

Genes Dev.

View full text Add to dashboard Cite

show abstract

“…Alkaline phosphatase is located in the brush border layer (Kozaric et al 2004) regulating lipid absorption into enterocytes, participating in bicarbonate secretion and controlling bacterial endotoxin-induced inflammation (Lalles 2010). Acid phosphatase is located in the lysosomes of enterocytes (Kozaric et al 2004) and could support intracellular digestion (Zhang et al 1995).…”

Section: Discussionmentioning

confidence: 99%

Digestive enzyme system of larvae of different freshwater teleosts and its differentiation during the initial phase of exogenous feeding

Lahnsteiner¹

2017

CZECH J ANIM SCI

View full text Add to dashboard Cite

Lahnsteiner F. (2017): Digestive enzyme system of larvae of different freshwater teleosts and its differentiation during the initial phase of exogenous feeding. Czech J. Anim. Sci., 62, 403-416.Activities of digestive enzymes and main histological characteristics of the intestine were investigated in larvae of three salmonid species (Coregonus maraena, C. atterensis, Thymallus thymallus), of burbot (Lota lota), and pikeperch (Sander lucioperca) at the onset of exogenous feeding (0 day degrees (°d)) and at 250°d thereafter. At the onset of exogenous feeding the activities of proteolytic, lipolytic, and carbohydrate splitting enzymes were detected in the intestines of all species. The enzymatic activities showed significant species specific differences indicating specializations in functionality and digestion ability. In C. atterensis and L. lota the activities of most enzymes were low in comparison to the other investigated species and therefore their digestive system was only poorly developed. In S. lucioperca it was moderately developed and in T. thymallus and C. maraena well-developed. After 250°d, the activities of the investigated enzymes changed in a very species specific way. Histologically, the intestines of the investigated species revealed no species specific differentiations at the onset of the first feeding with the exception of the absence of goblet cells in L. lota and C. atterensis. These differentiated after 250°d.

show abstract

“…The total amount of protein in the resulting cell lysate was determined using the Bradford protein assay as recommended by the manufacturer (Bio-Rad). The resulting cell lysates were subjected to quantitative Western blot analysis as described previously (51), except that, after incubation with the 86f7 monoclonal antibody, the membranes were probed with horseradish peroxidase-conjugated goat anti-mouse IgG (Pierce) and the proteins were visualized using enhanced chemiluminescence (ECL) as recommended by the manufacturer (Pierce). Bands were quantified using an Ambis radioanalytical imaging system.…”

Section: Methodsmentioning

confidence: 99%

“…Analysis of the Caco-2 cells grown on filter inserts using the iodinated 86f 7 monoclonal antibody revealed that the Ala 51 construct was similar to that of the wild-type receptor in the percent found on the cell surface, its enrichment on the basolateral surface, and in its ability to internalize the antibody from the baso- lateral surface (Table 1). In contrast, the Asp 36 construct was enriched on the apical surface to a similar extent as the Val 8 and Asn 21 constructs (Table 1).…”

Section: Polarized Surface Distribution and Internalizationmentioning

confidence: 99%

See 1 more Smart Citation

Basolateral sorting signal of the 300-kDa mannose 6-phosphate receptor

Wick

Seetharam

Dahms³

2002

American Journal of Physiology-Gastrointestinal and Liver Physi

Self Cite

View full text Add to dashboard Cite

In polarized cells, the delivery of numerous membrane proteins from the trans-Golgi network to the basolateral surface depends on specific sequences located in their cytoplasmic domain. We have previously shown that the insulin-like growth factor-II/mannose 6-phosphate receptor (IGF-II/MPR) exhibits a polarized cell surface distribution in the human colon adenocarcinoma (Caco-2) cell line in which there is a threefold enrichment on the basolateral surface. To investigate the role of residues in the cytoplasmic region of the receptor that facilitates its entry into the basolateral sorting pathway, we generated stably transfected Caco-2 cell lines expressing various mutant bovine IGF-II/MPRs. The steady-state surface distribution of mutant receptors was analyzed by subjecting filter-grown cell monolayers to incubation with iodinated IGF-II/MPR-specific antibody or to indirect immunofluorescence and visualization by confocal microscopy. Together, these results demonstrate that the sorting of the IGF-II/MPR to the basolateral cell surface depends on recognition of sequences located in its cytoplasmic region that are distinct from the Tyr-based internalization and dileucine-dependent endosomal trafficking motifs.

show abstract

Regulation of lysosomal and ubiquitin degradative pathways in differentiating human intestinal Caco-2 cells

Cited by 11 publications

References 39 publications

Cdx2 regulates endo-lysosomal function and epithelial cell polarity

Cdx2 regulates endo-lysosomal function and epithelial cell polarity

Digestive enzyme system of larvae of different freshwater teleosts and its differentiation during the initial phase of exogenous feeding

Basolateral sorting signal of the 300-kDa mannose 6-phosphate receptor

Contact Info

Product

Resources

About