Hemidesmosomes and their unique transmembrane protein BP180

Hirako, Yoshiaki; Owaribe, Katsushi

doi:10.1002/(sici)1097-0029(19981101)43:3<207::aid-jemt2>3.0.co;2-z

Cited by 25 publications

(20 citation statements)

References 97 publications

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“…The lamina densa is a sheet‐like structure, which is mainly composed of type IV collagen. The lamina lucida is a region between the lamina densa and the basal surface of basal keratinocytes, which form electron‐dense plaques, hemidesmosomes, that contain at least two transmembrane proteins, α6β4 integrin and BP180 (3).…”

Section: Introductionmentioning

confidence: 99%

Key role of heparan sulfate chains in assembly of anchoring complex at the dermal-epidermal junction

Iriyama

Tsunenaga

Amano

et al. 2011

Experimental Dermatology

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Epidermal basement membrane forms anchoring complex composed of hemidesmosomes, anchoring filaments, lamina densa and anchoring fibrils to link epidermis to dermis. However, the anchoring complex is rarely formed in skin equivalent models, probably because of degradation of extracellular matrix (ECM) proteins and heparan sulfate chains by matrix metalloproteinases (MMPs) and heparanase, respectively. To explore the roles of ECM proteins and heparan sulfate in anchoring complex assembly, we used specific inhibitors of MMPs and heparanase, and the formation of anchoring complex was analysed in terms of polarized deposition of collagen VII, BP180 and b4 integrin at the dermal-epidermal junction (DEJ) by means of immunohistochemistry and transmission electron microscopy (TEM). The deposition of collagen VII was polarized to the basal side by the addition of MMP inhibitor, and the staining intensity was increased by combined treatment with MMP inhibitor and heparanase inhibitor, which enhanced anchoring fibril formation as observed by TEM. BP180 was polarized to the basal side by heparanase inhibitor, which protects HS chains, but not by MMP inhibitor. MMP inhibitor improved the polarization of b4 integrin. Hemidesmosomes were formed in the presence of each inhibitor, as observed by TEM, and formation was greatly enhanced by the combined treatment. These findings suggest that heparan sulfate chains, in addition to ECM proteins at the DEJ, play an important role in the assembly of anchoring complex, especially hemidesmosomes and anchoring fibrils.

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Section: Introductionmentioning

confidence: 99%

Key role of heparan sulfate chains in assembly of anchoring complex at the dermal-epidermal junction

Iriyama

Tsunenaga

Amano

et al. 2011

Experimental Dermatology

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“…Early immunoelectron microscopic distribution studies of laminin-5 in the skin showed that it is a component of an anchoring filament, a thin filament connecting the lamina densa, an electron-dense layer of the basement membrane, to the adjacent hemidesmosome (Rousselle et al 1991). The hemidesmosome is an ultrastructurally defined subcellular adhesion device which connects cells to the surrounding basement membrane (for review, see Burgeson and Christiano 1997;Hirako and Owaribe 1998). The predicted molecular organization of the hemidesmosome is as follows.…”

Section: Introductionmentioning

confidence: 99%

Localization of laminin-5, HD1/plectin, and BP230 in the submandibular glands of developing and adult mice

Kadoya

Yamashina

1999

Histochemistry and Cell Biology

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We studied the distributions of laminin-5 and hemidesmosome components, HD1/plectin and BP230, in the submandibular glands of adult and developing mice. In adult mice, laminin-5 was expressed in the basement membranes of both the myoepithelial cells and excretory ducts. The former expression was predictable because laminin-5 is a ligand for hemidesmosomes, which appear in myoepithelial cells and stratified epithelium. However, the latter expression pattern suggested that the non-stratified epithelium of the excretory duct might also be associated with hemidesmosomes. During fetal development, laminin-5 was found in the basement membrane of developing ducts but not epithelial end buds in which future lobules are formed by epithelial branching. The expression of HD1/plectin but not BP230 was noted in the developing duct at early embryonic stages, indicating the presence of type II hemidesmosomes. Expression of BP230 appeared in the excretory duct epithelium at around the day of birth. At this stage, the typical hemidesmosome was observed in the duct epithelium. Our results suggest that laminin-5 is involved in duct development rather than epithelial branching. The results also suggest that the developing duct epithelium interacts with laminin-5 through the type II hemidesmosome, which later matures into a typical hemidesmosome upon the onset of expression of BP230.

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“…The 97 kD LAD antigen is now thought to be identical to an extracellular portion of BPAG2 [37]. Indeed, it was reported that the extracellular domain of BPAG2 was cleaved by a protease and the fragment was identified in the BMZ [38]. Cleavage of BPAG2 that directly connects the basal keratinocytes to the lamina densa allows the basal keratinocytes to detach from the basement membrane.…”

Section: Kd Bullous Pemphigoid Antigen (Bpag2 Type XVII Collagen)mentioning

confidence: 99%

“…Cleavage of BPAG2 that directly connects the basal keratinocytes to the lamina densa allows the basal keratinocytes to detach from the basement membrane. This process is thought to be essential in differentiation of epidermal keratinocytes and in wound healing [38]. However, the physiological roles of the BPAG2 fragment and of BPAG2 itself remain to be clarified.…”

Section: Kd Bullous Pemphigoid Antigen (Bpag2 Type XVII Collagen)mentioning

confidence: 99%

Epidermal Basement Membrane: Its Molecular Organization and Blistering Disorders

Masunaga

2006

Connective Tissue Research

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The epidermal basement membrane is a specialized structure localized between the epidermis and the dermis. Recent studies have elucidated the biological roles of the basement membrane and its pathophysiological involvement in bullous diseases. To understand the functions of the basement membrane, it is essential to have clear and precise information regarding the ultrastructural molecular organization of the epidermal basement membrane. Immunoelectron microscopy is a powerful technique and the only method available for the clarification of the ultrastructural localization or orientation of molecules. This review summarizes the latest information regarding the molecular organization of the epidermal basement membrane as determined by immunoelectron microscopy as well as the blistering diseases that occur in the epidermal basement membrane zone.

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Hemidesmosomes and their unique transmembrane protein BP180

Cited by 25 publications

References 97 publications

Key role of heparan sulfate chains in assembly of anchoring complex at the dermal-epidermal junction

Key role of heparan sulfate chains in assembly of anchoring complex at the dermal-epidermal junction

Localization of laminin-5, HD1/plectin, and BP230 in the submandibular glands of developing and adult mice

Epidermal Basement Membrane: Its Molecular Organization and Blistering Disorders

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