Sorting of endogenous plasma membrane proteins occurs from two sites in cultured human intestinal epithelial cells (Caco-2)

Matter, Karl; Brauchbar, Mathis; Bucher, Kaethy; Hauri, Hans‐Peter

doi:10.1016/0092-8674(90)90594-5

Cited by 259 publications

(187 citation statements)

References 35 publications

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“…In addition, to investigate whether and how the nature of membrane anchorage may affect the transcytotic processing of resident AP proteins, we analyzed in parallel the trafficking behavior of endogenous DPPIV, an AP resident single TMD protein that has been extensively used as a model protein to study sorting mechanisms in a variety of epithelia. When transfected in MDCK cells, DPPIV is targeted directly from the TGN to the apical domain (Casanova et al, 1991;Low et al, 1991), whereas in intestinal cells, endogenous DPPIV is partly directly transported to the apical membrane, whereas the remainder travels apically via the basolateral domain (Le Matter et al, 1990). In Fisher rat thyroid cells, DPPIV sorting depends on the onset of cell differentiation, i.e., transcytosis decreases and direct apical targeting increases in more differentiated cells (Zurzolo et al, 1992).…”

Section: Gpi-gfp Traffics Along the Indirect Route To The Ap Surface mentioning

confidence: 99%

Raft-mediated Trafficking of Apical Resident Proteins Occurs in Both Direct and Transcytotic Pathways in Polarized Hepatic Cells: Role of Distinct Lipid Microdomains

Aït‐Slimane

Trugnan

IJzendoorn

et al. 2003

MBoC

126

159

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In polarized hepatic cells, pathways and molecular principles mediating the flow of resident apical bile canalicular proteins have not yet been resolved. Herein, we have investigated apical trafficking of a glycosylphosphatidylinositol-linked and two single transmembrane domain proteins on the one hand, and two polytopic proteins on the other in polarized HepG2 cells. We demonstrate that the former arrive at the bile canalicular membrane via the indirect transcytotic pathway, whereas the polytopic proteins reach the apical membrane directly, after Golgi exit. Most importantly, cholesterol-based lipid microdomains ("rafts") are operating in either pathway, and protein sorting into such domains occurs in the biosynthetic pathway, largely in the Golgi. Interestingly, rafts involved in the direct pathway are Lubrol WX insoluble but Triton X-100 soluble, whereas rafts in the indirect pathway are both Lubrol WX and Triton X-100 insoluble. Moreover, whereas cholesterol depletion alters raft-detergent insolubility in the indirect pathway without affecting apical sorting, protein missorting occurs in the direct pathway without affecting raft insolubility. The data implicate cholesterol as a traffic direction-determining parameter in the direct apical pathway. Furthermore, raft-cargo likely distinguishing single vs. multispanning membrane anchors, rather than rafts per se (co)determine the sorting pathway.

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Section: Gpi-gfp Traffics Along the Indirect Route To The Ap Surface mentioning

confidence: 99%

Raft-mediated Trafficking of Apical Resident Proteins Occurs in Both Direct and Transcytotic Pathways in Polarized Hepatic Cells: Role of Distinct Lipid Microdomains

Aït‐Slimane

Trugnan

IJzendoorn

et al. 2003

MBoC

126

159

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“…We decided to apply a biochemical procedure to measure the amount of these proteins at the cell surface, since we lacked monospecific antibodies to E2 that were not limited to a particular epitope and, in any event, immunofluorescence measurements would not be quantitative. We therefore applied the technique of surface biotinylation used extensively in studies of surface transport in epithelial cells (Br/indli & Simons, 1989;Graeve et al, 1989Graeve et al, , 1990Lisanti et al, 1988Lisanti et al, , 1989Lisanti & Rodriguez-Boulan, 1990;Matter et al, 1990;Sargiacomo et al, 1989). In this assay, cell surface proteins are detected by treatment of the cells with a membrane-impermeant amino-reactive derivative of biotin (see Methods).…”

Section: E2 and E1 Are Transported To The Surface When Co-expressedmentioning

confidence: 99%

Intracellular transport of rubella virus structural proteins expressed from cloned cDNA

Baron

Ebel

Suomalainen

1992

Journal of General Virology

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“…Different functions are associated with this mechanism, including passive immunity (Walker, 1981;Gardner, 1988), ligand transport (Papiz et al, 1986;Brown et al, 1988) and various metabolic regulation mechanisms (Gardner, 1988;Lee et al, 1990; Sanderson and Walker, 1993). Results obtained with different proteins show that protein transport through the intestinal epithelium proceeds by a major transcellular degradative pathway together with a minor intact transport route (Cornell et al, 1971;Walker et al, 1972;Walker, 1981;Stern and Walker, 1984;Gardner, 1988;Marcon-Genty ef al, 1989;Hughson and Hopkins, 1990; Le Bivic et al, 1990;Matter et al, 1990;Heymann et al, 1990;Tome, 1992, 1994;Heyman and Desjeux, 1992 (Walker, 1981;Gardner, 1988 (Shen et al, 1992).…”

mentioning

confidence: 99%

Transport of β-lactoglobulin and α-lactalbumin in enterocyte-like Caco-2 cells

Caillard¹,

Tomé²

1995

Reprod. Nutr. Dev.

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Summary ― The transport of [ 14 C]-radiolabelled p-lactoglobulin and a-iactaibumin through Caco-2 cell monolayers grown on permeable filters was studied in order to evaluate the different protein pathways through the intestinal epithelium. p-Lactoglobulin or a-lactalbumin (0.25-3 mg/ml) was introduced on the apical side of the monolayer and both the transport and the release of labelled material from the cells were measured following different incubation times. The labelled material was analysed by either trichloroacetic acid precipitation or by high pressure liquid chromatography. Despite some differences between the 2 proteins, the overall mechanism followed approximately the same pattern. Part of the intact internalized protein was either recycled (10-15%) or transported via transcytosis (about 5%). Another pathway corresponded to the intracellular degradation of the protein. The calculation of the different routes followed by the proteins indicated that the main part of the degraded fraction (about 70%) was recycled whereas approximately 30% was transported to the other side. Moreover, 5-10% of the endocytosed material was retained intracellularly. milk protein / protein absorption I intestine / Caco-2 cells Résumé ― Transport de la 5-lactoglobuline et de l'a-lactalbumine dans les cellules de type entérocytaire Caco-2. Afin de quantifier les différentes voies de transport des protéines à travers l'épithélium intestinal, nous avons étudié le transport de la p -lactoglobuline et de l â -lactalbumine, marquées au !4C, à travers des cellules Caco-2 cultivées en monocouches sur des filtres perméables. Après addition de la p-lactoglobuline ou de 1'(x-lactaibumine (0,25 à 3 mglml) dans le compartiment apical, le transport et le relargage des produits radiomarqués ont été mesurés à différents temps d'incubation. Le matériel marqué a été analysé par précipitation à l'acide trichloracétique et par chromatographie liquide haute performance. Malgré quelques différences entre les 2 protéines, leur mécanisme général de transport était comparable. Une partie des protéines intactes intemalisées a été soit recyclée (10-15%) soit «transcytosée» (environ 5%). Les protéines peuvent également être dégradées à l'intérieur des cellules. La quantification des différentes voies indique que les produits de dégrada-tion sont majoritairement recyclés (70%) alors que 30% environ sont transportés vers la face opposée. De plus, 5 à 10% du matériel internalisé est stocké dans les cellules.

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Sorting of endogenous plasma membrane proteins occurs from two sites in cultured human intestinal epithelial cells (Caco-2)

Cited by 259 publications

References 35 publications

Raft-mediated Trafficking of Apical Resident Proteins Occurs in Both Direct and Transcytotic Pathways in Polarized Hepatic Cells: Role of Distinct Lipid Microdomains

Raft-mediated Trafficking of Apical Resident Proteins Occurs in Both Direct and Transcytotic Pathways in Polarized Hepatic Cells: Role of Distinct Lipid Microdomains

Intracellular transport of rubella virus structural proteins expressed from cloned cDNA

Transport of β-lactoglobulin and α-lactalbumin in enterocyte-like Caco-2 cells

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