Distribution of VLA-5 and VLA-4 fibronectin receptors in human monocytes demonstrated by immunofluorescence, immunocytochemistry, and autoradiography

1993 ◽  
Vol 51 ◽  
pp. 306-307
Author(s):  
Robert Williams ◽  
Che-Hung Lee ◽  
Sara E. Quella ◽  
David M. Harlan ◽  
Yuan-Hsu Kang
Keyword(s):  
Present Report ◽  
Matrix Proteins ◽  
Extracellular Matrices ◽  
Human Monocytes ◽  
Integrin Receptors ◽  
Morphological Evaluation ◽  
The Matrix ◽  
Specific Receptors ◽  
Cytokine Stimulation ◽  
Monocyte Adherence

Monocyte adherence to endothelial or extracellular matrices plays an important role in triggering monocyte activation in extravascular sites of infection, chronic inflammatory disorders, and tissue damage. Migration of monocytes in the tissues involves the response to a chemoattractant and movement by a series of attachments and detachments to the extracellular matrices which are regulated by expression and distribution of specific receptors for the matrix proteins such as fibronectin (FN). The VSAs (very late antigens or beta integrins), a subfamily of the transmembrane heterodimeric integrin receptors, have been thought to play a major role in monocyte adherence to the extracellular matrices and cells. In this subfamily, VLA-5 and VLA-4 are believed to be the most essential integrins mediating monocyte adherence to FN. In the present report, we have established and compared different procedures for morphological evaluation of the expression and distribution of the FN receptors on human monocytes in order to investigate their response to endotoxin or cytokine stimulation.

Altered Expression of Extra-Cellular Matrix Proteins and Integrin Receptors in Discoid Lupus Erythematosus

2004 ◽  
Vol 1 (4) ◽  
pp. 368-371
Author(s):  
Gianluigi Giannelli ◽  
Concetta Sgarra ◽  
Caterina Foti ◽  
Carlo Bergamini ◽  
Carmela Coviello ◽  
...  
Keyword(s):  
Lupus Erythematosus ◽  
Extra Cellular Matrix ◽  
Matrix Proteins ◽  
Discoid Lupus Erythematosus ◽  
Integrin Receptors ◽  
Altered Expression ◽  
Cellular Matrix

scholarly journals Functional relationship between the matrix proteins of feline and simian immunodeficiency viruses

Virology ◽  
2004 ◽  
Vol 329 (1) ◽  
pp. 157-167 ◽  
Author(s):  
Mariana L. Manrique ◽  
Silvia A. González ◽  
José L. Affranchino
Keyword(s):  
Functional Relationship ◽  
Matrix Proteins ◽  
The Matrix

scholarly journals Interactions of the matrix attachment region of DNA with the matrix proteins from the copper preincubated liver nuclei.

1995 ◽  
Vol 42 (2) ◽  
pp. 205-210 ◽  
Author(s):  
P Widłak ◽  
J Rogoliński ◽  
J Rzeszowska-Wolny
Keyword(s):  
Rat Liver ◽  
Copper Ions ◽  
Specific Interaction ◽  
Protein Composition ◽  
Matrix Proteins ◽  
Matrix Attachment Region ◽  
The Matrix ◽  
Attachment Region ◽  
Liver Nuclei ◽  
The Stability

Preincubation of rat liver nuclei with copper ions influenced the stability and protein composition of the nuclear matrices isolated by a "high salt" method. Also the specific interaction between matrix proteins and the kappa Ig matrix attachment region of DNA was affected.

Melanocyte Movement In Vitro: Role of Matrix Proteins and Integrin Receptors

1993 ◽  
Vol 101 (4) ◽  
pp. 605-608 ◽  
Author(s):  
Joseph G Morelli ◽  
Joseph J Yohn ◽  
Tamara Zekman ◽  
David A Norris
Keyword(s):  
Matrix Proteins ◽  
Integrin Receptors

Independent deposition of collagen types II and IX at epithelial-mesenchymal interfaces

Development ◽  
1989 ◽  
Vol 105 (1) ◽  
pp. 85-95 ◽  
Author(s):  
J.M. Fitch ◽  
A. Mentzer ◽  
R. Mayne ◽  
T.F. Linsenmayer
Keyword(s):  
Collagen Type ◽  
Immunohistochemical Study ◽  
Type Ii Collagen ◽  
The Other ◽  
Extracellular Matrices ◽  
Type Ii ◽  
Collagen Deposition ◽  
Collagen Types ◽  
Hind Limbs ◽  
The Matrix

Previous studies have demonstrated the presence of type II collagen (in mature chickens predominantly a ‘cartilage-specific’ collagen) in a variety of embryonic extracellular matrices that separate epithelia from mesenchyme. In an immunohistochemical study using collagen type-specific monoclonal antibodies, we asked whether type IX collagen, another ‘cartilage-specific’ collagen, is coexpressed along with type II at such interfaces. We confirmed that, in the matrix underlying a variety of cranial ectodermal derivatives and along the ventrolateral surfaces of neuroepithelia, type II collagen is codistributed with collagen types I and IV. Type IX collagen, however, was undetectable at those sites. We observed immunoreactivity for type IX collagen only within the notochordal sheath, where it first appeared at a later stage than did collagen types I and II. We also observed type II collagen (without type IX) beneath the dorsolateral ectoderm at stage 16; this correlates with the period during which limb ectoderm has been reported to induce the mesoderm to become chondrogenic. Finally, in older hind limbs we observed subepithelial type II collagen that was not associated with subsequent chondrogenesis, but appeared to parallel the formation of feathers and scales in the developing limb. These observations suggest that the deposition of collagen types II and IX into interfacial matrices is regulated independently, and that induction of mesenchymal chondrogenesis by such matrices does not involve type IX collagen. Subepithelial type IX collagen deposition, on the other hand, correlates with the assembly of a thick multilaminar fibrillar matrix, as present in the notochordal sheath and, as shown previously, in the corneal primary stroma.

scholarly journals Synergistic Modulation of Cellular Contractility by Mixed Extracellular Matrices

2012 ◽  
Vol 2012 ◽  
pp. 1-13 ◽  
Author(s):  
Aastha Kapoor ◽  
Shamik Sen
Keyword(s):  
Mixed Ligand ◽  
Matrix Proteins ◽  
Extracellular Matrices ◽  
Cell Behavior ◽  
Dependent Manner ◽  
Cell Contractility ◽  
Synergistic Modulation ◽  
Coated Surfaces ◽  
Collective Influence

The extracellular matrix (ECM) is known to provide various physicochemical cues in directing cell behavior including composition, topography, and dimensionality. Physical remodeling of the ECM has been documented in a variety of cancers. In breast cancer, the increased deposition of matrix proteins, their crosslinking, and alignment create a stiffer microenvironment that activates cell contractility and promotes cancer invasion. In this paper, we sought to study the collective influence of ECM composition and density on the contractile mechanics of human MDA-MB-231 cells making use of the recently established trypsin deadhesion assay. Using collagen and fibronectin-coated surfaces of varying density, we show that cell contractility is tuned in a density-dependent manner, with faster deadhesion on fibronectin-coated surfaces compared to collagen-coated surfaces under identical coating densities. The deadhesion responses are significantly delayed when cells are treated with the myosin inhibitor blebbistatin. By combining collagen and fibronectin at two different densities, we show that mixed ligand surfaces synergistically modulate cell contractility. Finally, we show that on fibroblast-derived 3D matrices that closely mimicin vivomatrices, cells are strongly polarized and exhibit faster deadhesion compared to the mixed ligand surfaces. Together, our results demonstrate that ECM composition, density, and 3D organization collectively regulate cell contractility.

scholarly journals The matrix proteins aggrecan and fibulin-1 play a key role in determining aortic stiffness

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Yasmin ◽  
Raya Al Maskari ◽  
Carmel M. McEniery ◽  
Sarah E. Cleary ◽  
Ye Li ◽  
...  
Keyword(s):  
Aortic Stiffness ◽  
Matrix Proteins ◽  
The Matrix

Mediation of endothelial injury following neutrophil adherence to extracellular matrix

1993 ◽  
Vol 264 (4) ◽  
pp. L401-L405 ◽  
Author(s):  
R. A. Kaslovsky ◽  
L. Lai ◽  
K. Parker ◽  
A. B. Malik
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Monoclonal Antibodies ◽  
Endothelial Permeability ◽  
Endothelial Injury ◽  
Matrix Proteins ◽  
Extracellular Matrix Components ◽  
The Matrix ◽  
Neutrophil Adherence ◽  
Permeability Increase

Since polymorphonuclear leukocytes (PMN) rapidly migrate across the endothelial barrier and attach to extracellular matrix components, we tested the hypothesis that adhesion of PMN to matrix proteins can mediate endothelial injury following PMN activation. Studies were made using gelatin- and fibronectin-coated polycarbonate microporous filters (10 microns thick) on which confluent monolayers of bovine pulmonary microvessel endothelial cells were grown. PMN were layered either directly onto endothelial cells (at a ratio of 10:1) (“upright system”) or onto gelatin- and fibronectin-coated filters with the endothelial monolayer grown on the underside of the filter without contact between PMN and endothelial cells (“inverted system”). PMN were activated with phorbol 12-myristate 13-acetate (PMA; 5 x 10(-9) M) in both systems. PMN activation increased endothelial permeability to 125I-labeled albumin in upright as well as inverted systems. Pretreatment of PMN with anti-CD18 monoclonal antibodies IB4 or R15.7, which inhibited PMN adherence to matrix constituents as well as to endothelial cells, prevented the permeability increase in both configurations. This effect of anti-CD18 monoclonal antibodies (mAbs) was not ascribed to a reduction in PMN activation, since PMA-induced superoxide generation was unaffected. We conclude that activation of PMN adherent to extracellular matrix proteins increases endothelial permeability to albumin and that this response is dependent on PMN adhesion to the matrix. The results support the concept that PMN-mediated increase in endothelial permeability is the result of “targeted” release of PMN products independent of whether the PMN are adherent to the extracellular matrix or the endothelium.

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