Collagenous transmembrane proteins: collagen XVII as a prototype

Franzke, Claus‐Werner; Tasanen, Kaisa; Schumann, Hauke; Bruckner‐Tuderman, Leena

doi:10.1016/s0945-053x(03)00051-9

Cited by 83 publications

(83 citation statements)

References 54 publications

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“…Transmembrane Proteins The designations of most collagenous transmembrane proteins are related to their structures or functions or to diseases caused by mutations in their genes (2). The group includes several collagens, i.e.…”

Section: Structure and Functions Of Collagenousmentioning

confidence: 99%

“…The functional consequences include diminished epidermal adhesion and skin blistering in response to minimal shearing forces. The disorder is called junctional epidermolysis bullosa (JEB), a skin disease with variable clinical phenotypes (2,35,36). Morphological characteristics of JEB are rudimentary hemidesmosomes and subepidermal tissue separation.…”

Section: Biochemical Features and Ligand Interactions-collagenmentioning

confidence: 99%

“…Its mRNA is expressed in placenta, kidney, skin, and neural cells. 2 Recombinant collagen XXIII is synthesized as a ϳ75-kDa protein, which can be released from the cell surface by furin-mediated proteolysis. The cleavage produces a 60-kDa soluble ectodomain that forms a multimeric complex, which binds heparin with low affinity (20).…”

Section: Other Collagenous Transmembrane Proteins Andmentioning

confidence: 99%

See 2 more Smart Citations

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Franzke

Brückner

Bruckner‐Tuderman

2005

Journal of Biological Chemistry

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151

138

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Section: Structure and Functions Of Collagenousmentioning

confidence: 99%

Section: Biochemical Features and Ligand Interactions-collagenmentioning

confidence: 99%

Section: Other Collagenous Transmembrane Proteins Andmentioning

confidence: 99%

See 1 more Smart Citation

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Franzke

Brückner

Bruckner‐Tuderman

2005

Journal of Biological Chemistry

Self Cite

151

138

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“…Among different types of proteolysis, the release of extracellular domains of transmembrane proteins, mainly catalyzed by proteases of a disintegrin and metalloprotease (ADAM) family, is known as ectodomain shedding (2). Ectodomain shedding is involved in functions of a variety of essential transmembrane proteins such as TNF-a, TGF-a, epidermal growth factor receptor ligands (2,3), or transmembrane collagens (4,5). All of type XIII, XVII, XXIII, and XXV collagens as well as ectodysplasin A are transmembrane proteins in type II orientation, with an intracytoplasmic N terminus and an extracellular C terminus, and their ectodomains can be shed.…”

mentioning

confidence: 99%

“…All of type XIII, XVII, XXIII, and XXV collagens as well as ectodysplasin A are transmembrane proteins in type II orientation, with an intracytoplasmic N terminus and an extracellular C terminus, and their ectodomains can be shed. The shedding occurs within juxtamembranous noncollagenous domains, and is usually mediated by furin and/or ADAMs (4,5). However, the biological significance of these processes is still unclear.…”

mentioning

confidence: 99%

Ectodomain Shedding Generates Neoepitopes on Collagen XVII, the Major Autoantigen for Bullous Pemphigoid

Nishie

Lamer

Schlösser

et al. 2010

The Journal of Immunology

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As a type II transmembrane protein in basal keratinocytes, collagen XVII provides stable adhesion between epidermis and dermis in the skin. Its ectodomain can be shed from the cell surface, and autoantibodies in certain blistering diseases preferentially recognize the shed form. Major epitopes of collagen XVII are clustered within the juxtamembranous noncollagenous 16th A domain, and ectodomain shedding occurs within this region, suggesting that cleavage generates neoepitopes. However, the candidate cleavage sites have been controversial, and the mechanism of neoepitope generation is unclear. In this study, we investigated cleavage sites in the noncollagenous 16th A domain to understand the generation of neoepitopes and their pathological role. Polyclonal Abs recognizing the stretch Leu524-Gly532 preferentially reacted with the shed ectodomain, but not with the full-length form, indicating that a neoepitope was localized at this site. The neoepitope-specific Ab fixed complement and induced granulocyte-dependent dermal-epidermal separation in cryosections of normal human skin. The physiological cleavage sites were identified using mass spectrometry. N termini were found at Asp514, Leu524, Glu525, and Gly526, among which Asp514 and Glu525 were blocked by acetylation and pyroglutaminate. In silico prediction of B cell epitopes indicated that the antigenicity of the Leu524-Gly532 region increased substantially after shedding, regardless of the cleavage sites. Correspondingly, neoepitopes were found in the skin and blister fluids of patients with bullous pemphigoid, and bullous pemphigoid sera reacted with the peptide Leu524-Gly532. Taken together, these data demonstrate that physiological shedding of collagen XVII generates neoepitopes, which may serve as a target of blister-inducing autoantibodies.

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Overview of Extracellular Matrix

2012

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The extracellular matrix provides an environment for cells. It is produced, assembled, and modified by cells and in turn, it modifies the functions and behavior of the cells it encounters. The molecules that make up the matrix are diverse in both structure and function. This well-illustrated unit provides an introduction to the structure and function of the major components of the extracellular matrix and serves as a background for the other units in the chapter, which include protocols for isolation and analysis of individual components. Curr. Protoc. Cell Biol.

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Collagenous transmembrane proteins: collagen XVII as a prototype

Cited by 83 publications

References 54 publications

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Ectodomain Shedding Generates Neoepitopes on Collagen XVII, the Major Autoantigen for Bullous Pemphigoid

Overview of Extracellular Matrix

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