High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV

Brittingham, Raymond; Uitto, Jouni; Fertala, Andrzej

doi:10.1016/j.bbrc.2006.03.034

Cited by 72 publications

(50 citation statements)

References 36 publications

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“…Further observations indicated that strong interactions did occur between collagen VII in anchoring fibrils and collagen IV or laminin 332 present in the dermo-epidermal basement membrane (14,15) but not between collagen VII and the major component of banded fibrils of the papillary dermis, i.e. collagen I (3,14). However, others reported direct but weak interactions between collagens I and VII (13).…”

Section: Discussionmentioning

confidence: 94%

“…This finding was surprising since earlier reports indicated that anchoring fibrils interacted with banded dermal collagen fibrils solely by unspecific mechanical entanglement (5). Further observations indicated that strong interactions did occur between collagen VII in anchoring fibrils and collagen IV or laminin 332 present in the dermo-epidermal basement membrane (14,15) but not between collagen VII and the major component of banded fibrils of the papillary dermis, i.e. collagen I (3,14).…”

Section: Discussionmentioning

confidence: 99%

“…However, this model has been contested because anchoring plaques are relatively rare (4). Thus, there is the possibility that anchoring fibrils directly interact with collagen I-containing dermal fibrils and, indeed, weak in vitro-binding of collagen VII to monomolecular collagen I has been reported (14). However, when organized into fibrils, collagen I may offer multiple, possibly cooperative, binding sites for collagen VII, which may strengthen substantially the interaction between the two proteins.…”

mentioning

confidence: 99%

“…Previous studies addressing interactions between collagen VII and unpolymerized basement membrane molecules demonstrated that the amino-terminal, non-collagen-like domain 1 of collagen VII (NC-1(VII)) interacts with collagen IV and laminin 332 (13), components (14) of the basement membrane and of anchoring filaments, respectively (15).…”

mentioning

confidence: 99%

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Supramolecular Interactions in the Dermo-epidermal Junction Zone

Villone

Fritsch

Koch

et al. 2008

Journal of Biological Chemistry

110

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The dermis and the epidermis of normal human skin are functionally separated by a basement membrane but, together, form a stable structural continuum. Anchoring fibrils reinforce this connection by insertion into the basement membrane and by intercalation with banded collagen fibrils of the papillary dermis. Structural abnormalities in collagen VII, the major molecular constituent of anchoring fibrils, lead to a congenital skin fragility condition, dystrophic epidermolysis bullosa, associated with skin blistering. Here, we characterized the molecular basis of the interactions between anchoring fibrils and banded collagen fibrils. Suprastructural fragments of the dermo-epidermal junction zone were generated by mechanical disruption and by separation with magnetic Immunobeads. Anchoring fibrils were tightly attached to banded collagen fibrils. In vitro binding studies demonstrated that a von Willebrand factor A-like motif in collagen VII was essential for binding of anchoring fibrils to reconstituted collagen I fibrils. Since collagen I and VII molecules reportedly undergo only weak interactions, the attachment of anchoring fibrils to collagen fibrils depends on supramolecular organization of their constituents. This complex is stabilized in situ and resists dissociation by strong denaturants.The functions and homeostasis of skin critically depend on the stable organization and cohesion between the epidermis and the dermis. These tissue layers are confined and interconnected by the dermo-epidermal junction zone (DEJZ) 4 , which comprises the basal keratinocytes, the dermo-epidermal basement membrane, and the uppermost, i.e. the papillary dermis.The suprastructural entity affording pivotal mechanical stability of the DEJZ is the anchoring complex, which sequentially consists of the hemidesmosomes at the basal surface of the keratinocytes, the anchoring filaments linking the hemidesmosomes to the basement membrane, and the anchoring fibrils connecting the basement membrane with the underlying dermal stroma (1). Anchoring fibrils are centro-symmetrically banded structures that originate in the basement membrane and either end in the papillary dermis or loop back into the basement membrane (2-4). Their calculated length is 785 nm (5), but they appear shorter in the tissue due to their insertion into the lamina densa (3, 6).The quantitatively major molecular constituent of anchoring fibrils is collagen VII (7). The major component of D-periodically banded, dermal collagen fibrils, collagen I, copolymerizes with minor quantities of collagens III, V, XII, and XIV to form macromolecular alloys that vary in their composition and, because of this, also in their supramolecular organization. Therefore, the latter collagens may contribute only small mass fractions, yet critically determine the structural and functional properties of the fibrils (8 -10).Structural abnormalities of the anchoring complex lead to skin fragility, the landmark of epidermolysis bullosa, a group of heritable blistering skin diseases (11). The absenc...

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Supramolecular Interactions in the Dermo-epidermal Junction Zone

Villone

Fritsch

Koch

et al. 2008

Journal of Biological Chemistry

110

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“…It is therefore possible that hepsin cleavage may release domain VI of ␤3. It has been reported that Ln-332 interacts with collagen VII via domain VI of the ␤3 chain (49,50). Therefore, release of domain VI by hepsin could disrupt the interaction of Ln-332 with collagen VII.…”

Section: Discussionmentioning

confidence: 99%

Proteolytic Processing of Laminin-332 by Hepsin and Matriptase and Its Role in Prostate Cancer Progression

Tripathi¹

2010

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Public reporting burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for reducing this burden to Department of Defense, Washington Headquarters Services, Directorate for Information Operations and Reports (0704-0188), 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-4302. Respondents should be aware that notwithstanding any other provision of law, no person shall be subject to any penalty for failing to comply with a collection of information if it does not display a currently valid OMB control number. PLEASE DO NOT RETURN YOUR FORM TO THE ABOVE ADDRESS. (From -To) 15 REPORT DATE (DD-MM-YYYY) 01-09-2010 REPORT TYPE Annual Summary DATES COVERED PERFORMING ORGANIZATION NAME(S) AND ADDRESS(ES) AND ADDRESS(ES) PERFORMING ORGANIZATION REPORT NUMBERThe Vanderbilt University Nashville, TN 37203 SPONSORING / MONITORING AGENCY NAME(S) AND ADDRESS(ES) 10. SPONSOR/MONITOR'S ACRONYM(S) U.S. Army Medical Research and Materiel Command Fort Detrick, Maryland 21702-5012 SPONSOR/MONITOR'S REPORT NUMBER(S) DISTRIBUTION / AVAILABILITY STATEMENTApproved for Public Release; Distribution Unlimited SUPPLEMENTARY NOTES ABSTRACTLaminin-332 is lost in prostate cancer progression. Laminin-332 is known to be cleaved by various cell surface proteases, including MMPs, and this cleavage facilitates migration of cancer cells. We have found that Laminin-332 is individually cleaved by two serine proteases, hepsin and matriptase, and that this cleavage enhances migration of human prostate cancer cells in vitro. Hepsin is over-expressed in more than 90% prostate cancer cases. Similarly, matriptase is over-expressed in human prostate cancer cases and expression of both proteases correlates with tumor progression. However, the mechanism(s) by which these two serine proteases play a role in prostate cancer is unknown. We found that Hepsin/matriptase overexpressing prostate cancer cells, LNCaP show significantly increased migration on Ln-332. This project aims to define the role played by the cleavage of Laminin-332 by hepsin and matriptase in prostate cancer. were incubated with appropriate primary antibodies for 1 h, followed by secondary antibodies and/or fluorescent phalloidin for 1 h at room temperature. Images were captured using a Zeiss LSM510Meta with a ×60 Plan-NeoFluar 1.3 NA objective confocal microscope. We looked for Invadopodia as actin puncta that would also positive for cortactin and we also tried to localize degradation area or dark area on fluorescent matrix. We did not find any invadopodia formation in our PC3 cells. Figure 1 is a representative image of our trial attempts. Figure 1 is immunofluorescence staining of PC3 cells plated on FITC-Fibronectin (green), actin is blue an...

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Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites

et al. 2020

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Type VII collagen is an extracellular matrix protein, which is important for skin stability; however, detailed information at the molecular level is scarce. The second vWFA (von Willebrand factor type A) domain of type VII collagen mediates important interactions, and immunization of mice induces skin blistering in certain strains. To understand vWFA2 function and the pathophysiological mechanisms leading to skin blistering, we structurally characterized this domain by X‐ray crystallography and NMR spectroscopy. Cell adhesion assays identified two new interactions: one with β1 integrin via its RGD motif and one with laminin‐332. The latter interaction was confirmed by surface plasmon resonance with a KD of about 1 mm. These data show that vWFA2 has additional functions in the extracellular matrix besides interacting with type I collagen.

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High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV

Cited by 72 publications

References 36 publications

Supramolecular Interactions in the Dermo-epidermal Junction Zone

Supramolecular Interactions in the Dermo-epidermal Junction Zone

Proteolytic Processing of Laminin-332 by Hepsin and Matriptase and Its Role in Prostate Cancer Progression

Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites

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