scholarly journals Birbeck Granules Are Subdomains of Endosomal Recycling Compartment in Human Epidermal Langerhans Cells, Which Form Where Langerin Accumulates

2002 ◽  
Vol 13 (1) ◽  
pp. 317-335 ◽  
Author(s):  
Ray Mc Dermott ◽  
Umit Ziylan ◽  
Danièle Spehner ◽  
Huguette Bausinger ◽  
Dan Lipsker ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Langerhans Cells ◽  
Birbeck Granule ◽  
Drug Induced ◽  
Intracellular Location ◽  
Birbeck Granules ◽  
Endosomal Recycling ◽  
Endosomal Membranes ◽  
And Function ◽  
Epidermal Langerhans Cells

Birbeck granules are unusual rod-shaped structures specific to epidermal Langerhans cells, whose origin and function remain undetermined. We investigated the intracellular location and fate of Langerin, a protein implicated in Birbeck granule biogenesis, in human epidermal Langerhans cells. In the steady state, Langerin is predominantly found in the endosomal recycling compartment and in Birbeck granules. Langerin internalizes by classical receptor-mediated endocytosis and the first Birbeck granules accessible to endocytosed Langerin are those connected to recycling endosomes in the pericentriolar area, where Langerin accumulates. Drug-induced inhibition of endocytosis results in the appearance of abundant open-ended Birbeck granule-like structures appended to the plasma membrane, whereas inhibition of recycling induces Birbeck granules to merge with a tubular endosomal network. In mature Langerhans cells, Langerin traffic is abolished and the loss of internal Langerin is associated with a concomitant depletion of Birbeck granules. Our results demonstrate an exchange of Langerin between early endosomal compartments and the plasma membrane, with dynamic retention in the endosomal recycling compartment. They show that Birbeck granules are not endocytotic structures, rather they are subdomains of the endosomal recycling compartment that form where Langerin accumulates. Finally, our results implicate ADP-ribosylation factor proteins in Langerin trafficking and the exchange between Birbeck granules and other endosomal membranes.

scholarly journals Morphological Alterations and Increased S100B Expression in Epidermal Langerhans Cells Detected in Skin from Patients with Progressive Vitiligo

Life ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 579
Author(s):  
Fei Yang ◽  
Lingli Yang ◽  
Lanting Teng ◽  
Huimin Zhang ◽  
Ichiro Katayama
Keyword(s):  
Electron Microscopy ◽  
Langerhans Cells ◽  
Critical Role ◽  
Light And Electron Microscopy ◽  
Morphological Alterations ◽  
Birbeck Granules ◽  
Immuno Electron Microscopy ◽  
Skin Biopsies ◽  
Epidermal Langerhans Cells

The role of Langerhans cells (LCs) in vitiligo pathogenesis remains unclear, with published studies reporting contradictory results regarding the quantity of LCs and no data on the features of LCs in vitiligo. Here, we aimed to analyze the presence, density, and morphological features of LCs in the epidermis of patients with vitiligo. Skin biopsies were stained for LCs using anti-CD1a/anti-langerin antibodies and analyzed by immunocytochemistry with light and electron microscopy. Compared with healthy controls, we detected significantly increased numbers of epidermal LCs in lesional skin from vitiligo in the progressive state. These LCs exhibited striking morphological alterations, including an elevated number of dendrites, with increased length and more branches than dendrites from controls. Ultrastructure examination via immuno-electron microscopy revealed markedly reduced Birbeck granules (BGs) and shorter BG rods in LCs from progressive vitiligo, with higher expression of langerin. Additionally, expression of S100B, the activity biomarker of vitiligo, was increased in these LCs. This work provides new insight on the cellular composition of LCs in vitiliginous skin, revealing altered morphology and increased LC numbers, with elevated S100B expression. Our data suggest LCs might play a critical role in vitiligo pathogenesis and thus may represent a novel therapeutic target for this disease.

scholarly journals Ontogeny and function of murine epidermal Langerhans cells

2017 ◽  
Vol 18 (10) ◽  
pp. 1068-1075 ◽  
Author(s):  
Daniel H Kaplan
Keyword(s):  
Langerhans Cells ◽  
And Function ◽  
Epidermal Langerhans Cells

Functional Human Epidermal Langerhans Cells that Lack Birbeck Granules

1994 ◽  
Vol 103 (6) ◽  
pp. 807-810 ◽  
Author(s):  
Mieke Mommaas ◽  
A.a.t. Mulder ◽  
Bert Jan Vermeer ◽  
Frits Koning
Keyword(s):  
Langerhans Cells ◽  
Birbeck Granules ◽  
Epidermal Langerhans Cells

scholarly journals Disappearance of certain acidic organelles (endosomes and Langerhans cell granules) accompanies loss of antigen processing capacity upon culture of epidermal Langerhans cells.

1990 ◽  
Vol 172 (5) ◽  
pp. 1471-1482 ◽  
Author(s):  
H Stössel ◽  
F Koch ◽  
E Kämpgen ◽  
P Stöger ◽  
A Lenz ◽  
...  
Keyword(s):  
Langerhans Cells ◽  
Antigen Processing ◽  
Ultrastructural Level ◽  
Helper T Cells ◽  
Processing Capacity ◽  
Native Protein ◽  
Protein Antigens ◽  
Birbeck Granules ◽  
Acidic Organelles ◽  
Epidermal Langerhans Cells

Freshly isolated epidermal Langerhans cells (LC) can actively process native protein antigens, but are weak in sensitizing helper T cells. During culture, when LC mature into potent immunostimulatory dendritic cells, T cell sensitizing capacity develops but antigen processing capacity is downregulated. Processing of exogenous antigens for class II-restricted antigen presentation involves acidic organelles. We used the DAMP-technique to monitor acidic organelles at the ultrastructural level in fresh, as well as cultured, mouse and human LC. We observed that the loss of antigen processing capacity with culture of LC was reflected by the disappearance of certain acidic organelles, namely endosomes (particularly early ones), and the hitherto enigmatic LC granules ("Birbeck Granules"). Our findings support the notion that endosomes are critical for antigen processing and suggest that LC granules might be involved as well.

scholarly journals External antigen uptake by Langerhans cells with reorganization of epidermal tight junction barriers

2009 ◽  
Vol 206 (13) ◽  
pp. 2937-2946 ◽  
Author(s):  
Akiharu Kubo ◽  
Keisuke Nagao ◽  
Mariko Yokouchi ◽  
Hiroyuki Sasaki ◽  
Masayuki Amagai
Keyword(s):  
Tight Junction ◽  
Stratum Corneum ◽  
Tight Junctions ◽  
Langerhans Cells ◽  
Antigen Uptake ◽  
Birbeck Granules ◽  
Mammalian Skin ◽  
Gain Access ◽  
Epidermal Langerhans Cells

Outermost barriers are critical for terrestrial animals to avoid desiccation and to protect their bodies from foreign insults. Mammalian skin consists of two sets of barriers: stratum corneum (SC) and tight junctions (TJs). How acquisition of external antigens (Ags) by epidermal Langerhans cells (LCs) occur despite these barriers has remained unknown. We show that activation-induced LCs elongate their dendrites to penetrate keratinocyte (KC) TJs and survey the extra-TJ environment located outside of the TJ barrier, just beneath the SC. Penetrated dendrites uptake Ags from the tip where Ags colocalize with langerin/Birbeck granules. TJs at KC–KC contacts allow penetration of LC dendrites by dynamically forming new claudin-dependent bicellular- and tricellulin-dependent tricellular TJs at LC–KC contacts, thereby maintaining TJ integrity during Ag uptake. Thus, covertly under keratinized SC barriers, LCs and KCs demonstrate remarkable cooperation that enables LCs to gain access to external Ags that have violated the SC barrier while concomitantly retaining TJ barriers to protect intra-TJ environment.

Functional human epidermal Langerhans cells that lack birbeck granules

1993 ◽  
Vol 6 (1) ◽  
pp. 48
Author(s):  
AM Mommaas ◽  
AA Mulder ◽  
F Koning ◽  
BJ Vermeer
Keyword(s):  
Langerhans Cells ◽  
Birbeck Granules ◽  
Epidermal Langerhans Cells

scholarly journals Rab11-dependent recycling of calcium channels is mediated by auxiliary subunit α2δ-1 but not α2δ-3

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
James O. Meyer ◽  
Annette C. Dolphin
Keyword(s):  
Plasma Membrane ◽  
Calcium Channels ◽  
Dominant Negative ◽  
Calcium Currents ◽  
Dependent Manner ◽  
Auxiliary Subunit ◽  
Voltage Gated Calcium Channels ◽  
Endosomal Recycling ◽  
Recycling Pathway ◽  
And Function

AbstractN-type voltage-gated calcium channels (CaV2.2) are predominantly expressed at presynaptic terminals, and their function is regulated by auxiliary α2δ and β subunits. All four mammalian α2δ subunits enhance calcium currents through CaV1 and CaV2 channels, and this increase is attributed, in part, to increased CaV expression at the plasma membrane. In the present study we provide evidence that α2δ-1, like α2δ-2, is recycled to the plasma membrane through a Rab11a-dependent endosomal recycling pathway. Using a dominant-negative Rab11a mutant, Rab11a(S25N), we show that α2δ-1 increases plasma membrane CaV2.2 expression by increasing the rate and extent of net forward CaV2.2 trafficking in a Rab11a-dependent manner. Dominant-negative Rab11a also reduces the ability of α2δ-1 to increase CaV2.2 expression on the cell-surface of hippocampal neurites. In contrast, α2δ-3 does not enhance rapid forward CaV2.2 trafficking, regardless of whether Rab11a(S25N) is present. In addition, whole-cell CaV2.2 currents are reduced by co-expression of Rab11a(S25N) in the presence of α2δ-1, but not α2δ-3. Taken together these data suggest that α2δ subtypes participate in distinct trafficking pathways which in turn influence the localisation and function of CaV2.2.

scholarly journals Control of the differentiation state and function of human epidermal Langerhans cells by cytokines in vitro

2001 ◽  
Vol 15 (5) ◽  
pp. 433-440 ◽  
Author(s):  
F Prignano ◽  
G Gerlini ◽  
V Fossombroni ◽  
N Pimpinelli ◽  
B Giannotti ◽  
...  
Keyword(s):  
Langerhans Cells ◽  
And Function ◽  
Epidermal Langerhans Cells

Origin and Function of Epidermal Langerhans Cells

1980 ◽  
Vol 53 (1) ◽  
pp. 149-174 ◽  
Author(s):  
Georg Stingl ◽  
Kunihiko Tamaki ◽  
Stephen I. Katz
Keyword(s):  
Langerhans Cells ◽  
And Function ◽  
Epidermal Langerhans Cells
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