Cloning of Partial cDNA for Mouse 180-kDa Bullous Pemphigoid Antigen (BPAG2), a Highly Conserved Collagenous Protein of the Cutaneous Basement Membrane Zone

Li, Ke-Hua.; Giudice, George J.; Tamai, Katsuto; Do, Haeyoung. Choi; Sawamura, Daisuke; Díaz, Luis A.; Uitto, Jouni

doi:10.1111/1523-1747.ep12616611

Cited by 49 publications

(11 citation statements)

References 30 publications

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“…These include the dense plaque polypeptides BP230 [Owaribe et al, 1990;Sawamura et al, 1991 [ andHD1 [Hiede et al. 1992], the plasma membrane-associated component BP 180 |Giudice et al, 1991: Li et al. 1992 and other polypeptides [Klatte et al.…”

Section: Introductionmentioning

confidence: 99%

Studies of Hemidesmosomes in Human Amnion: The Use of a Detergent Extraction Protocol for Compositional and Ultrastructural Analysis and Preparation of a Hemidesmosome-Enriched Fraction from Tissue

Behzad¹,

Jones

Ball

et al. 1995

Cells Tissues Organs

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A method is described for the sequential detergent and high ionic strength extraction of human amnion with the progressive enrichment of the intermediate filament (IF) cytoskeleton and its associated structures including hemidesmosomes (HD). TEM of the extracted epithelium in situ reveals IF bundles beneath the apical cell surface, around the nucleus and at the lateral edges of the cells where association with desmosomes occurs. IF bundles are also very prominent within basal cell processes where they loop through the cytoplasm adjacent to the HDs. A novel connecting filament network is observed running between the IFs and the hemidesmosomal dense plaque. The adjacent IF network contains both cytokeratin and vimentin, the latter revealed much more fully as a result of the extraction protocol. The hemidesmosomal plasma membrane contains integrin subunits α6 and β4 and these are quantitatively retained at the basal cell surface during extraction, while nonjunctional plasma membrane is solubilised. Integrin βl is found at the basolateral cell surface but, like actin, is extracted quantitatively and is not present in HDs. The extracted epithelial cells may be recovered by scraping and the IF network depolymerised to produce a particulate fraction containing short residual IFs, associated thin filaments and plaque material. This fraction contains immunoreactive cytokeratin and vimentin. Integrin α6β4 has been used as a biochemical criterion of the presence of HD material in the fraction. Both subunits are highly enriched. The fraction also contains the hemidesmosomal components HD1, BP230 and BP180. This method is likely to be useful in further characterisation of the HD.

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Section: Introductionmentioning

confidence: 99%

Studies of Hemidesmosomes in Human Amnion: The Use of a Detergent Extraction Protocol for Compositional and Ultrastructural Analysis and Preparation of a Hemidesmosome-Enriched Fraction from Tissue

Behzad¹,

Jones

Ball

et al. 1995

Cells Tissues Organs

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“…Work in mammalian intestinal epithelial cells, 3D cultures and short-term epithelial Box 1. Isoforms originating from splicing Differential splicing of the mammalian BPAG1 gene gives rise to several proteins, with the first BPAG1 isoforms reported being BPAG1e and BPAG1n (Li et al, 1992;Sawamura et al, 1990). Additional BPAG1e isoforms, including BPAG1eA, BPAG1eS and BPAG1eB, are found in muscle (Okumura et al, 2002).…”

Section: The Various Binding Partners Of Spektraplakinsmentioning

confidence: 99%

Spectraplakin family proteins – cytoskeletal crosslinkers with versatile roles

Zhang

Yue

2017

Journal of Cell Science

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The different cytoskeletal networks in a cell are responsible for many fundamental cellular processes. Current studies have shown that spectraplakins, cytoskeletal crosslinkers that combine features of both the spectrin and plakin families of crosslinkers, have a critical role in integrating these different cytoskeletal networks. Spectraplakin genes give rise to a variety of isoforms that have distinct functions. Importantly, all spectraplakin isoforms are uniquely able to associate with all three elements of the cytoskeleton, namely, F-actin, microtubules and intermediate filaments. In this Review, we will highlight recent studies that have unraveled their function in a wide range of different processes, from regulating cell adhesion in skin keratinocytes to neuronal cell migration. Taken together, this work has revealed a diverse and indispensable role for orchestrating the function of different cytoskeletal elements in vivo.

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“…This integrin interacts with plectin and BP230, while its extracellular domain is involved in cell‐stromal adhesion. However there is an association between α 6 β 4 integrin and the extracellular part of BP‐180, and probably autoantibodies binding BP‐180 disturb this interaction altering the adhesion of basal cells to the underlying basal lamina (Li et al , 1992; Hopkinson et al , 1995). α 6 β 4 integrin is a receptor for various laminin variants, but it binds with high affinity to laminin‐5.…”

Section: α6β4 Integrinmentioning

confidence: 99%