Imaging of collagen type III in fluid by atomic force microscopy

Taatjes, Douglas J.; Quinn, Anthony S.; Bovill, Edwin G.

doi:10.1002/(sici)1097-0029(19990301)44:5<347::aid-jemt5>3.0.co;2-2

Cited by 19 publications

(10 citation statements)

References 26 publications

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“…Collagen monomers usually assemble to form cable-like structures with varying diameters between 10–500 nm. An enlarged view of the network showed individual monomer filaments with an average diameter of approximately 431.2 nm, complying with standard findings [35].…”

Section: Resultssupporting

confidence: 88%

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Ubiquitin-Like Protein from Human Placental Extract Exhibits Collagenase Activity

Chakraborty

Mitra

et al. 2013

PLoS ONE

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An aqueous extract of human placenta exhibits strong gelatinase/collagenase activity in zymography. 2-D gel electrophoresis of the extract with gelatin zymography in the second dimension displayed a single spot, identified as ubiquitin-like component upon MALDI/TOF MS/MS analysis. Immunoblot indicated presence of ubiquitin and absence of collagenase in the extract. Collagenase activity of the ubiquitin-like component was confirmed from the change in solubility of collagen in aqueous buffer, degradation of collagen by size-exclusion HPLC and atomic force microscopy. Quantification with DQ-gelatin showed that the extract contains 0.04 U/ml of collagenase activity that was inhibited up to 95% by ubiquitin antibody. Ubiquitin from bovine erythrocytes demonstrated mild collagenase activity. Bioinformatics studies suggest that placental ubiquitin and collagenase follow structurally divergent evolution. This thermostable intrinsic collagenase activity of placental extract might have wide physiological relevance in degrading and remodeling collagen as it is used as a drug for wound healing and pelvic inflammatory diseases.

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Section: Resultssupporting

confidence: 88%

“…Control collagen incubated at 37°C for 48 h when imaged in liquid mode exhibited intact monomeric filament of 82 nm, as evident from the cross-section (Figure 3A) [35]. Image of collagen treated with collagenase indicated gradual loss in integrity of the fibril.…”

Section: Resultsmentioning

confidence: 88%

Ubiquitin-Like Protein from Human Placental Extract Exhibits Collagenase Activity

Chakraborty

Mitra

et al. 2013

PLoS ONE

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“…It was used for example to investigate the interaction of basement membrane macromolecules, (89) the surface ultrastructure of collagen fibrils and their association in human cornea and sclera, (90) the assembly mechanism of fibrous long-spacing collagen, (91) the substructure of native hydrated rat tail tendon ECM (92) and imaging of collagen III polymerization in solution. (93) Among a variety of other applications, AFM was used to examine the structure of single collagen XVI molecules on mica. (94) AFM of normal human skin basement membrane preparations (95) displays the structural diversity of different fibrillar networks and the close-meshed underlying laminin-collagen IV net.…”

Section: Multiphoton Microscopy and Second Harmonic Generationmentioning

confidence: 99%

Local proteolytic activity in tumor cell invasion and metastasis

Ludwig¹

2005

BioEssays

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Proteolytic cleavage of extracellular matrix (ECM) is a critical regulator of many physiological and pathological events. It affects fundamental processes such as cell growth, differentiation, apoptosis and migration. Most proteases are produced as inactive proenzymes that undergo proteolytic cleavage for activation. Proteolytic activity is additionally modified by endogenous inhibitors. Mechanisms that localize and concentrate protease activity in the pericellular microenvironment of cells are prerequisites for processes like angiogenesis, bone development, inflammation and tumor cell invasion. Methods that enable real-time, high-resolution imaging and precise quantification of local proteolytic activity in vitro and in vivo remain major challenges. These methods will play an important role in the understanding of basic principles e.g. in cancer cell invasion, the identification of new therapeutical targets and hence drug design. This review highlights mechanisms and functions of local proteolytic activity with special emphasis on tumor cell invasion and metastasis, and focuses on techniques for the investigation of this process.

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“…CM is the original AFM imaging mode and can be implemented in both air [39][40] and fluid [41][42][43]. Direct monitoring of cantilever deflection without feedback varying of the sample-to-cantilever height is usually not used since the larger forces occurring with large cantilever deflections can damage the surface [44].…”

Section: Afm Operating Modesmentioning

confidence: 99%

Imaging Proteins with Atomic Force Microscopy: An Overview

Silva

2005

CPPS

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Atomic force microscopy (AFM) has become a common tool for biophysical studies of proteins; mainly due its property to perform characterizations near physiological conditions. The tertiary and quaternary structures, forces driving folding-unfolding processes, and secondary structure elements can be studied in their native environments allowing high resolution level associated with small distortions. This review outlines the operational principles and applications of AFM for protein biophysics.

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Imaging of collagen type III in fluid by atomic force microscopy

Cited by 19 publications

References 26 publications

Ubiquitin-Like Protein from Human Placental Extract Exhibits Collagenase Activity

Ubiquitin-Like Protein from Human Placental Extract Exhibits Collagenase Activity

Local proteolytic activity in tumor cell invasion and metastasis

Imaging Proteins with Atomic Force Microscopy: An Overview

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