Effects of collagenase-cleavage of type I collagen on alpha2beta1 integrin-mediated cell adhesion

1998 ◽  
Vol 111 (8) ◽  
pp. 1127-1135 ◽  
Author(s):  
A.J. Messent ◽  
D.S. Tuckwell ◽  
V. Knauper ◽  
M.J. Humphries ◽  
G. Murphy ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Type I Collagen ◽  
Cell Attachment ◽  
Heat Denaturation ◽  
Type I ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Triple Helices ◽  
Collagen Fragment ◽  
Cell Matrix Interactions

In this paper we show that collagenase-3 cleavage of type I collagen has a marked effect on alpha2beta1 integrin-mediated interactions with the collagen fragments generated. Isolated alpha2beta1 integrin and alpha2 integrin A-domain were found to bind to both native collagen and native 3/4 fragment and, to a lesser degree, native 1/4 fragment. Whole integrin and integrin A-domain binding were lost after heat denaturation of the collagen fragments. At physiological temperature, cell adhesion to triple-helical 3/4 fragment via alpha2beta1 integrin was still possible; however, no alpha2beta1 integrin-mediated adhesion to the 1/4 fragment was observed. Unwinding of the collagen fragment triple helices by heating to physiological temperatures prior to adsorption to plastic tissue culture plates resulted in total abrogation of HT1080 cell attachment to either fragment. These results provide significant evidence in support of a role for matrix-metalloproteinase cleavage of the extracellular matrix in modifying cell-matrix interactions.

scholarly journals Extracellular Matrix Hydrogels Promote Expression of Paxillin, a Muscle-Tendon Junction Marker

2021 ◽  
Author(s):  
Lewis S. Gaffney ◽  
Matthew B. Fisher ◽  
Donald O. Freytes
Keyword(s):  
Extracellular Matrix ◽  
Type I Collagen ◽  
Conditioned Media ◽  
Type I ◽  
Tissue Specific ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Cell Matrix Interactions ◽  
Tissue Models ◽  
Cells Cultured

AbstractMuscle and tendon injuries are prevalent and range from minor sprains and strains to traumatic, debilitating injuries. However, the interactions between these tissues during injury and recovery remain unclear. Three-dimensional tissue models that incorporate both tissues and a physiologically relevant junction between muscle and tendon may aide in understanding how the two tissues interact. Here, we use tissue specific extracellular matrix (ECM) derived from muscle and tendon to determine how cells of each tissue interact with the microenvironment of the opposite tissue resulting in junction specific features. ECM materials were derived from the achilles tendon and gastrocnemius muscle, decellularized, and processed to form tissue specific pre-hydrogel digests. C2C12 myoblasts and tendon fibroblasts were cultured in tissue-specific ECM conditioned media or encapsulated in tissue-specific ECM hydrogels to determine cell-matrix interactions and the effects on a muscle-tendon junction marker, paxillin. ECM conditioned media had only a minor effect on upregulation of paxillin in cells cultured in monolayer. However, cells cultured within ECM hydrogels had 50-70% higher paxillin expression than cells cultured in type I collagen hydrogels. Contraction of the ECM hydrogels varied by the type of ECM used. Subsequent experiments with varying density of type I collagen (and thus contraction) showed no correlation between paxillin expression and the amount of gel contraction, suggesting that a constituent of the ECM was the driver of paxillin expression in the ECM hydrogels. Using tissue specific ECM allowed for the de-construction of the cell-matrix interactions similar to muscle-tendon junctions to study the expression of MTJ specific proteins.Impact StatementThe muscle-tendon junction is an important feature of muscle-tendon units; however, despite cross-talk between the two tissue types, it is overlooked in current research. Deconstructing the cell-matrix interactions will allow the opportunity to study significant junction specific features and markers that should be included in tissue models of the muscle-tendon unit, while gaining a deeper understanding of the natural junction. This research aims to inform future methods to engineer a more relevant multi-tissue platform to study the muscle-tendon unit.

Different mechanisms in the attachment of cells to native and denatured collagen

1979 ◽  
Vol 38 (1) ◽  
pp. 267-281
Author(s):  
S.L. Schor ◽  
J. Court
Keyword(s):  
Cell Attachment ◽  
Experimental Conditions ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Independent Mechanism ◽  
Cell Matrix Interactions ◽  
Serum Dependent ◽  
Kinetics Of ◽  
Dependent Mechanism

The attachment of cells to collagen has been reported previously to require the presence of serum and the particular serum protein involved in this process, variously known as CIG, CAP or fibronectin, has been isolated. This conclusion that cell attachment to collagen requires serum (or more precisely, fibronectin) is based on experiments measuring the kinetics of cell attachment to films of collagen. We have measured the kinetics of attachment of HeLa and attachment to films of collagen-containing substrata under a variety of experimental conditions and present evidence that the serum-dependent mechanism of cell attachment described by others is actually only the case for films of denatured collagen, while cell attachment to native collagen fibres occurs by a different, serum-independent, mechanism. The possible relevance of these findings to cell-matrix interactions in vivo is discussed.

scholarly journals Oncogenic Deregulation of Cell Adhesion Molecules in Leukemia

Cancers ◽  
2019 ◽  
Vol 11 (3) ◽  
pp. 311 ◽  
Author(s):  
Roland Windisch ◽  
Nina Pirschtat ◽  
Christian Kellner ◽  
Linping Chen-Wichmann ◽  
Jörn Lausen ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Cell Adhesion ◽  
Progenitor Cells ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Gene Products ◽  
Hematopoietic Stem ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Cell Matrix Interactions

Numerous cell–cell and cell–matrix interactions within the bone marrow microenvironment enable the controlled lifelong self-renewal and progeny of hematopoietic stem and progenitor cells (HSPCs). On the cellular level, this highly mutual interaction is granted by cell adhesion molecules (CAMs) integrating differentiation, proliferation, and pro-survival signals from the surrounding microenvironment to the inner cell. However, cell–cell and cell–matrix interactions are also critically involved during malignant transformation of hematopoietic stem/progenitor cells. It has become increasingly apparent that leukemia-associated gene products, such as activated tyrosine kinases and fusion proteins resulting from chromosomal translocations, directly regulate the activation status of adhesion molecules, thereby directing the leukemic phenotype. These observations imply that interference with adhesion molecule function represents a promising treatment strategy to target pre-leukemic and leukemic lesions within the bone marrow niche. Focusing on myeloid leukemia, we provide a current overview of the mechanisms by which leukemogenic gene products hijack control of cellular adhesion to subsequently disturb normal hematopoiesis and promote leukemia development.

Alignment and Cell-Matrix Interactions of Human Corneal Endothelial Cells on Nanostructured Collagen Type I Matrices

2010 ◽  
Vol 51 (12) ◽  
pp. 6303 ◽  
Author(s):  
Rita Gruschwitz ◽  
Jens Friedrichs ◽  
Monika Valtink ◽  
Clemens M. Franz ◽  
Daniel J. Müller ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Corneal Endothelial Cells ◽  
Human Corneal Endothelial Cells ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Cell Matrix Interactions

scholarly journals Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin

2014 ◽  
Vol 2014 ◽  
pp. 1-13 ◽  
Author(s):  
Satoru Ken Nishimoto ◽  
Miyako Nishimoto
Keyword(s):  
Binding Site ◽  
Matrix Protein ◽  
Cell Attachment ◽  
Matrix Gla Protein ◽  
Extracellular Matrix Protein ◽  
Tissue Sections ◽  
Embryonic Tissues ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Cell Matrix Interactions

Background. Matrix Gla protein (MGP) is a vitamin K-dependent, extracellular matrix protein. MGP is a calcification inhibitor of arteries and cartilage. However MGP is synthesized in many tissues and is especially enriched in embryonic tissues and in cancer cells. The presence of MGP in those instances does not correlate well with the calcification inhibitory role. This study explores a potential mechanism for MGP to bind to matrix proteins and alter cell matrix interactions.Methods. To determine whether MGP influences cell behavior through interaction with fibronectin, we studied MGP binding to fibronectin, the effect of MGP on fibronectin mediated cell attachment and spreading and immunolocalized MGP and fibronectin.Results. First, MGP binds to fibronectin. The binding site for MGP is in a specific fibronectin fragment, called III1-C or anastellin. The binding site for fibronectin is in a MGP C-terminal peptide comprising amino acids 61–77. Second, MGP enhances cell attachment and cell spreading on fibronectin. MGP alone does not promote cell adhesion. Third, MGP is present in fibronectin-rich regions of tissue sections.Conclusions. MGP binds to fibronectin. The presence of MGP increased cell-fibronectin interactions.

Attachment of sponge cells to collagen substrata: effect of a collagen assembly factor

1985 ◽  
Vol 79 (1) ◽  
pp. 271-285
Author(s):  
B. Diehl-Seifert ◽  
B. Kurelec ◽  
R.K. Zahn ◽  
A. Dorn ◽  
B. Jericevic ◽  
...  
Keyword(s):  
Cell Attachment ◽  
Cell Matrix ◽  
Sequence Of Events ◽  
Matrix Interactions ◽  
Geodia Cydonium ◽  
Aggregation Factor ◽  
Assembly Factor ◽  
Electron Microscopical ◽  
Cell Matrix Interactions

Collagen, isolated from the sponge Geodia cydonium in the absence of denaturing agents, had the typical amino acid composition and was associated with the carbohydrates galactose and glucose. The resulting individual fibrils with a diameter of 23 nm, displayed a 19.5 nm periodicity with one intraperiod band. A collagen assembly factor (CAF) was identified in and partially purified from the extracellular space. The CAF reacted with antibodies against intact Geodia cells but not with antibodies against Geodia lectin and Geodia aggregation factor. In the presence of the CAF, the collagen fibrils reconstituted collagen bundles in an ordered sequence of events, which were followed by electron-microscopical and biochemical methods. Bundle formation was not dependent on the presence of the homologous lectin, glycoconjugates or aggregation factor. Homologous cells (Geodia archaeocytes) were determined to attach only to those Geodia collagen substrates that contained CAF. The attachment of these cells did not require fibronectin or Geodia lectin. Homologous glycoconjugates or NaOH-treated collagen inhibited cell attachment. Collagen from the sponge Chondrosia reniformis, even in the presence of Geodia CAF, was no appropriate substrate for Geodia cell attachment. Whether collagen is a component of cell-matrix interactions in sponge systems also in vivo is discussed.

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