Localization of the 230-kilodalton bullous pemphigoid antigen in cultured keratinocytes: Formation of a prehemidesmosome

Thacher, Scott M.; Malone, Karen L.; Davé, Kirti; Zhao, Shuai

doi:10.1016/0014-4827(91)90360-7

Cited by 21 publications

(12 citation statements)

References 42 publications

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“…4, B and C), where linkage to keratin IFs was apparent. In contrast the BP antigen was present throughout the entire plaque as reported previously (data not shown; 13,20,28,30,32,47,52) . These observations indicated that at least an epitope of the HDI molecule is to be found on the cytoplasmic side of HDs.…”

Section: Localization Of Hdi In Hemidesmosomes At the Electron Microssupporting

confidence: 86%

Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes.

Hieda

Nishizawa

Uematsu

et al. 1992

The Journal of Cell Biology

218

141

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Abstract. Hemidesmosomes (HDs) mediate cell adhesion to the extracellular matrix and have morphological association with intermediate-sized filaments (IFs) through cytoplasmic plaques . Though several proteins have been located in HDs, most of them have not been well characterized, with the exception of the 230-kD antigen of bullous pemphigoid (BP), an autoimmune skin blistering disease. Only recently we have succeeded in isolating HDs from bovine corneal epithelial cells and in identifying five major components on SDS-PAGE (Owaribe K., Y. Nishizawa, and W. W. Franke . 1991 . Exp. Cell Res . 192 :622-630) . In this study we report on immunological characterization of one of the major components, termed HDl, with an H EMIDESMOSOMES (HDs)' and focal adhesions are cell junctions that mediate adhesion to the extracellular matrix (ECM) . These two plasma membrane junction types have common ultrastructural features ; e.g., both are associated with cytoskeeeool elements through electron-dense cytoplasmic plaques. They thus provide us with models to explore the mechanisms of transmembrane connection between the ECM and the cytoskeleton. In focal adhesions associated with actin-containing microfilaments (for reviews see references 2 and 50), a number ofproteins are known to be involved, including ECM receptors of the integrin family (5,12,17,33) and plaque components such as talin (1) and vinculin (29) . Yet our knowledge about the molecular architecture of the ECM-to-microfilaments junctions is still incomplete.The HD, primarily found in the basement membrane zone (BMZ) of stratified and complex epithelia, has a complex structure: a cytoplasmic plaque associated with intermediate filaments (IFs), a subbasal dense plate with anchoring filaments in the basal lamina, and anchoring fibrils in collagenous connective tissues (6,16,39). The morphological appearance is essentially that of half of the desmosome of intercellular junctions. However, although several des- apparent molecular mass of 500 kD. Immunofluorescence microscopy showed colocalization of HDl with BP antigen at the basement membrane zone of those tissues that have typical HDs, including skin epidermis, corneal and tracheal epithelia, and myoepithelium . In cultured keratinocytes, HDl demonstrated colocalization with BP antigen in the precise way, while being absent from focal adhesions . Immunoelectron microscopy revealed that an epitope of HDl was located on the cytoplasmic side of HDs . Taking all these results together, we conclude that HDl is a new hemidesmosomal component . Interestingly, HDl also exists in endothelial and glial cells, which lack typical HDs . mosomal proteins have been identified (e.g., references 4, 26; for review see reference 35) since the establishment of appropriate isolation procedures (e.g., reference 36), none of them have been found in HDs (13, 35) . Thus, in marked contrast to other celljunctions, little information is available about the molecular components of HDs, with the exception ofthe well-characterized 230-kD antigen r...

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Section: Localization Of Hdi In Hemidesmosomes At the Electron Microssupporting

confidence: 86%

Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes.

Hieda

Nishizawa

Uematsu

et al. 1992

The Journal of Cell Biology

218

141

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“…A human autoantiserum from a bullous pemphigoid patient was kindly donated by Dr. Peter Marinkovich (Stanford University; Palo Alto, CA) (Stanley, 1993). A rabbit antiserum to human 230-KD hemidesmosomal plaque protein was from Dr. S. M. Thacher (Texas A&M College of Medicine, Houston, TX) (Thacher et al, 1991). MAbs to a 3 integrin subunit were a gift from Dr. L. J.…”

Section: Methodsmentioning

confidence: 99%

Anchoring complex components laminin-5 and type VII collagen in intestine: association with migrating and differentiating enterocytes.

Leivo¹,

Tani²,

La³

et al. 1996

J Histochem Cytochem.

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Anchoring complex component laminin-5 and its subunits laminin (Ln)-alpha3 and Ln-beta3 chains, Type VII collagen, and integrin chains alpha3, alpha6, and beta4 were studied in developing and adult human intestine and compared with findings on Ln-alpha1 and Ln-alpha2 chains. In adult human duodenum, jejunum, and ileum, Ln-5 detected with a polyclonal antiserum and Ln-alpha3 and Ln-beta3 chains, detected with monoclonal antibodies (MAbs), were restricted to the epithelial basement membranes (BMs) of villi, whereas Ln-alpha2 chain was seen only focally in crypt bottoms. In double labeling experiments, the stretch of crypt BM corresponding to the proliferative cell compartment was found to be devoid of both Ln-alpha3 and Ln-alpha2 chains. Double labeling for Ln-5 and proliferating cell nuclear antigen also showed an abrupt onset of Ln-5 expression exactly at the upper edge of the proliferative cell compartment. Type VII collagen was negligible in duodenum and showed a rising duodenal-ileal gradient localizing to villar BMs. Double labeling for Ln-5 and Type VII collagen, however, indicated only partial co-distribution in the intestine. Electron microscopy of ileum revealed both anchoring filaments and anchoring fibrils but no hemidesmosomal plaques. Our results demonstrate the expression of Ln-5 in BMs outside of stratified epithelia and indicate that Ln-5 in the intestine is associated with the compartment of migrating and differentiating enterocytes. Absence of hemidesmosomes and the presence of other anchoring complex components, such as Ln-5, Type VII collagen, and integrin chains alpha3, alpha6, and beta4, suggests unique properties for epithelial cell attachment in the intestine.

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“…One of the MAbs against the 180-kD BPA showed the deposition of immunogold particles on the outer surface of the ventral side, where the plasma mem brane appeared to be associated with keratin intermediates filaments (KIF). These sites probably correspond to prehemidesmosomes reported by Thacker et al [6],…”

Section: Introductionmentioning

confidence: 99%

“…It is now accepted that hemidesmosomes contain oc6-(34-integrin [1,2], the 180-kD bullous pemphigoid antigen (BPA) [3][4][5], the 230-kD BPA [6][7][8][9] and HD1 peptide |1()| as major components. These molecules appear to repeat the assembly and disassembly during cell movement as shown in the Ca2* switch (low to high) experiments [11].…”

Section: Introductionmentioning

confidence: 99%

A Possible Cell-Biologic Mechanism Involved in Blister Formation of Bullous Pemphigoid: Anti-180-kD BPA Antibody Is an Initiator

et al. 1994

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In this short review, we summarize the results of our recent studies on the effects of anti-bullous-pemphigoid antigen (BPA) antibodies and BP sera on the hemidesmosome in cultured keratinocytes (DJM-1 cells) as examined by immunofluorescence microscopy. The 180-kD and the 230-kD BPAs localized on the basal plasma membrane showed a homogeneously dotted pattern in cells grown with low Ca²⁺ (0.07 mM), while they formed a peculiar concentric ring or arch (ring/arch) pattern in cells grown with high Ca²⁺ (1.87 mM). In addition, the 180-kD BPA was distributed also on the lateral/apical cell membrane, and the 230-kD BPA was found in the cytoplasm. The high Ca²⁺ ring/arch arrangement of BPAs was formed within 3 h after the low-high Ca²⁺ switch. Anti-180-kD BPA monoclonal antibodies (MAbs) and BP sera, but not anti-230-kD BPA MAbs, which were added into this system, caused the internalization of the 180-kD BPA from the lateral/apical cell membrane and inhibited the formation of the ring/arch pattern. These results suggest that autoantibodies to the 180-kD, but not to the 230-kD, BPAs may directly bind to the antigen on the cell surface of the basal cells and disturb the formation of hemidesmosomes. The 180-kD BPA appears to be an initiator of blister formation.

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Localization of the 230-kilodalton bullous pemphigoid antigen in cultured keratinocytes: Formation of a prehemidesmosome

Cited by 21 publications

References 42 publications

Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes.

Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes.

Anchoring complex components laminin-5 and type VII collagen in intestine: association with migrating and differentiating enterocytes.

A Possible Cell-Biologic Mechanism Involved in Blister Formation of Bullous Pemphigoid: Anti-180-kD BPA Antibody Is an Initiator

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