Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Franzke, Claus‐Werner; Brückner, Peter; Bruckner‐Tuderman, Leena

doi:10.1074/jbc.r400034200

Cited by 148 publications

(141 citation statements)

References 57 publications

(61 reference statements)

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“…Collagen XVII protein contributes to the hemidesmosomal adhesion of basal undifferentiated keratinocytes in stratified squamous epithelia [25]. In line with maturation, keratinocytes lose their collagen XVII expression, however, it can be detected as an early marker of malignant transformation in epidermal squamous cell carcinomas [26].…”

Section: Discussionmentioning

confidence: 99%

Correlations Between Prognosis and Regional Biomarker Profiles in Head and Neck Squamous Cell Carcinomas

Szentkúti

Dános

Brauswetter³

et al. 2014

Pathol. Oncol. Res.

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Head and neck squamous cell carcinomas (HNSC C) show diverse clinicopathological features and are mostly linked with poor outcome. In this study, we tested if the expression of tumor growth, cell cycle and basement membrane anchorage related biomarkers allow prognostic and clinicopathological stratification of HNSCC. Archived HNSCC samples from 226 patients included into tissue microarrays (TMA) were tested using immunohistochemistry. Histopathological evaluation and the analysis of immunostaining for EGFR, Ki67, p53, p16 ink4 and Collagen XVII proteins were carried out in digital whole slides. Statistical evaluation was carried out using Pearson's Chi-square test and Kaplan-Meier survival analysis. In the tested cohort, hypopharyngeal cancers had the least favorable, and glottic cancers had the most favorable prognosis. High Ki67 positive tumor cell fractions were associated with significantly worse prognosis and elevated rate of lymph node metastasis. Both Ki67 and EGFR expression correlated significantly with the tumor localization. Ki67 index was the highest in the hypopharyngeal region and it proved to be the lowest in the glottic region. EGFR expression was the highest in the oral cavity and the lowest in the glottic region. The survival rate of patients with p16 ink4

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Section: Discussionmentioning

confidence: 99%

Correlations Between Prognosis and Regional Biomarker Profiles in Head and Neck Squamous Cell Carcinomas

Szentkúti

Dános

Brauswetter³

et al. 2014

Pathol. Oncol. Res.

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“…Thus, in various respects, gliomedin resembles other integral transmembrane proteins containing collagen domains, which are also shed from the cell surface. These include ectodysplasin A and collagens XIII, XVII and XXV (Franzke et al, 2005). It has recently been demonstrated that gliomedin ectodomains shed from the cell surface are further processed by BMP1/TLD-like proteinases, which cleave between the collagen-like and olfactomedin domains (Maertens et al, 2007).…”

Section: Non-fibrillar Collagensmentioning

confidence: 99%

The bone morphogenetic protein 1/Tolloid-like metalloproteinases

2007

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A decade ago, bone morphogenetic protein 1 (BMP1) was shown to provide the activity necessary for proteolytic removal of the C-propeptides of procollagens I-III: precursors of the major fibrillar collagens. Subsequent studies have shown BMP1 to be the prototype of a small group of extracellular metalloproteinases that play manifold roles in regulating formation of the extracellular matrix (ECM). Soon after initial cloning of BMP1, genetic studies showed the related Drosophila proteinase Tolloid (TLD) to be necessary for formation of the dorsal-ventral axis in early embryogenesis. It is now clear that the BMP1/TLD-like proteinases, conserved in species ranging from Drosophila to humans, act in dorsal-ventral patterning via activation of transforming growth factor β (TGFβ)-like proteins BMP2, BMP4 (vertebrates) and decapentaplegic (arthropods). More recently, it has become apparent that the BMP1/TLD-like proteinases are key activators of a broader subset of the TGFβ superfamily of proteins, with implications that these proteinases may be key in orchestrating formation of ECM with growth factor activation and BMP signaling in morphogenetic processes.

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“…4,12,13 The cytoplasmic domain of collagen XVII has been reported to interact with BP230, plectin, and integrin ␤4; all of these interactions are important for stabilization of the HDs. 14,15 Thus, collagen XVII is thought to be a vital cell surface receptor that links the cytoplasmic structural components with the ECM.…”

mentioning

confidence: 99%

“…1 Interaction of cells with ECM proteins is usually mediated by cell surface receptors of the integrin or syndecan families, 1-3 but other tissue-specific receptors, such as collagen XVII, also exist. 4 A major component of epithelial basement membranes, which represent highly specialized ECM, is laminin 332, and its interactions with keratinocyte integrins ␣3␤1 and ␣6␤4 guide cell migration, differentiation, and proliferation. 5,6 In basal keratinocytes of the epidermis, the adhesion receptors are embedded in larger protein complexes, the hemidesmosomes (HDs), which can be observed as electron-dense ultrastructural components facing the basement membrane.…”

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confidence: 99%