Apical cell surface expression of rat dipeptidyl peptidase IV in transfected Madin-Darby canine kidney cells

Low, Seng Hui; Wong, Siew Heng; Tang, Bor Luen; Subramaniam, V.N.; Hong, Wanjin

doi:10.1016/s0021-9258(18)98852-6

Cited by 51 publications

(10 citation statements)

References 59 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…First, they confirm the remarkable flexibility of the protein sorting machinery of epithelia (23,34), since the same GPI-anchored proteins are sorted differently in different epithelial cells types. Recent work has shown that a typical apical protein, dipeptidyl peptidase IV, may reach the apical membrane via different routes in different epithelial cells, e.g., by transcytosis from the basolateral membrane in liver cells and directly from the TGN in MDCK and in FRT cells (6,20,46). Furthermore, in transgenic mice, the low density lipoprotein receptor is distributed basolaterally in liver and intestinal cells but apically in proximal tubular kidney cells (27).…”

Section: Discussionmentioning

confidence: 99%

Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells.

Zurzolo

Lisanti

Caras

et al. 1993

The Journal of Cell Biology

153

118

View full text Add to dashboard Cite

Abstract. Glycosylphosphatidylinositol (GPI) acts as an apical targeting signal in MDCK cells and other kidney and intestinal cell lines. In striking contrast with these model polarized cell lines, we show here that Fischer rat thyroid (FRT) epithelial calls do not display a preferential apical distribution of GPI-, anchored proteins. Six out of nine detectable endogenous GPI-anchored proteins were localized on the basolateral surface, whereas two others were apical and one was not polarized. Transfection of several model GPI proteins, previously shown to be apically targeted in MDCK cells, also led to unexpected results. While the ectodomain of decay accelerating factor (DAF) was apicaUy secreted, 50% of the native, GPI-anchored form, of this protein was basolateral. Addition of a GPI anchor to the ectodomain of Herpes simplex gD-1, secreted without polarity, led to basolateral localization of the fusion protein, gD1-DAE Targeting experiments demonstrated that gD1-DAF was delivered vectoriaUy from the Golgi apparatus to the basolateral surface. These results indicate that FRT cells have fundamental differences with MDCK cells with regard to the mechanisms for sorting GPI-anchored proteins: GPI is not an apical signal but, rather, it behaves as a basolateral signal. The "mutant" behavior of FRT cells may provide clues to the nature of the mechanisms that sort GPI-anchored proteins in epithelial cells.

show abstract

Section: Discussionmentioning

confidence: 99%

Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells.

Zurzolo

Lisanti

Caras

et al. 1993

The Journal of Cell Biology

153

118

View full text Add to dashboard Cite

show abstract

“…For example, dipeptidyl peptidase IV (DPP-IV) and aminopeptidase N (APN) use the transcytotic route in liver and both routes in CaCo2 cells. When transfected into MDCK cells, they mainly use the direct route from the TGN to the apical surface (39,66) . However, about 20% of both travel to the MDCK basolateral surface.…”

Section: Pathways To the Cell Surfacementioning

confidence: 99%

Plasma membrane protein sorting in polarized epithelial cells.

Mostov

Apodaca

Aroeti

et al. 1992

The Journal of Cell Biology

261

177

View full text Add to dashboard Cite

“…3 ). In MDCK cells, on the other hand, ectopically expressed DPP4 is directly transported to the apical domain but not by transcytosis ( 60 , 61 ). The indirect targeting of apical proteins such as DPP4 is thus considered to be a hallmark of the hepatocytic polarity phenotype.…”

Section: Discussionmentioning

confidence: 99%

Hepatocyte polarity establishment and apical lumen formation are organized by Par3, Cdc42, and aPKC in conjunction with Lgl

Tocan

Hayase

Kamakura

et al. 2021

Journal of Biological Chemistry

View full text Add to dashboard Cite

Hepatocytes differ from columnar epithelial cells by their multipolar organization, which follows the initial formation of central lumen-sharing clusters of polarized cells as observed during liver development and regeneration. The molecular mechanism for hepatocyte polarity establishment, however, has been comparatively less studied than those for other epithelial cell types. Here, we show that the tight junction protein Par3 organizes hepatocyte polarization via cooperating with the small GTPase Cdc42 to target atypical protein kinase C (aPKC) to a cortical site near the center of cell–cell contacts. In 3D Matrigel culture of human hepatocytic HepG2 cells, which mimics a process of liver development and regeneration, depletion of Par3, Cdc42, or aPKC results in an impaired establishment of apicobasolateral polarity and a loss of subsequent apical lumen formation. The aPKC activity is also required for bile canalicular (apical) elongation in mouse primary hepatocytes. The lateral membrane-associated proteins Lgl1 and Lgl2, major substrates of aPKC, seem to be dispensable for hepatocyte polarity establishment because Lgl-depleted HepG2 cells are able to form a single apical lumen in 3D culture. On the other hand, Lgl depletion leads to lateral invasion of aPKC, and overexpression of Lgl1 or Lgl2 prevents apical lumen formation, indicating that they maintain proper lateral integrity. Thus, hepatocyte polarity establishment and apical lumen formation are organized by Par3, Cdc42, and aPKC; Par3 cooperates with Cdc42 to recruit aPKC, which plays a crucial role in apical membrane development and regulation of the lateral maintainer Lgl.

show abstract

Apical cell surface expression of rat dipeptidyl peptidase IV in transfected Madin-Darby canine kidney cells

Cited by 51 publications

References 59 publications

Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells.

Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells.

Plasma membrane protein sorting in polarized epithelial cells.

Hepatocyte polarity establishment and apical lumen formation are organized by Par3, Cdc42, and aPKC in conjunction with Lgl

Contact Info

Product

Resources

About