scholarly journals Matrilin-2 interacts with itself and with other extracellular matrix proteins

2002 ◽  
Vol 367 (3) ◽  
pp. 715-721 ◽  
Author(s):  
Dorothea PIECHA ◽  
Charlotte WIBERG ◽  
Matthias MÖRGELIN ◽  
Dieter P. REINHARDT ◽  
Ferenc DEÁK ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Extracellular Matrix Proteins ◽  
Collagen I ◽  
Matrix Proteins ◽  
Hek 293 ◽  
Protein Ligands ◽  
293 Cells ◽  
Physiological Relevance ◽  
Kd Values

Matrilin-2 is a component of extracellular filamentous networks. To study the interactions by which it can be integrated into such assemblies, full-length and truncated forms of matrilin-2 were recombinantly expressed in HEK-293 cells and purified from conditioned medium. The recombinant proteins, when used in interaction assays, showed affinity to matrilin-2 itself, but also to other collagenous and non-collagenous extracellular matrix proteins. The interaction between matrilin-2 and collagen I was studied in greater detail and could be shown to occur at distinct sites on the collagen I molecule and to have a KD of about 3×10-8M. Interactions with some non-collagenous protein ligands were even stronger, with matrilin-2 binding to fibrillin-2, fibronectin and laminin-1—nidogen-1 complexes, with KD values in the range of 10-8—10-11M. Co-localization of matrilin-2 with these ligands in the dermal-epidermal basement membrane, in the microfibrils extending from the basement membrane into the dermis, and in the dermal extracellular matrix, indicates a physiological relevance of the interactions in the assembly of supramolecular extracellular matrix structures.

scholarly journals Skin basement membrane and extracellular matrix proteins characterization and quantification by real time RT-PCR

Biomaterials ◽  
2006 ◽  
Vol 27 (29) ◽  
pp. 5059-5068 ◽  
Author(s):  
Tzu-Wei Wang ◽  
Jui-Sheng Sun ◽  
Yi-Chau Huang ◽  
Hsi-Chin Wu ◽  
Li-Tin Chen ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Real Time ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Rt Pcr

Interaction of Plasmodium gallinaceum ookinetes and oocysts with extracellular matrix proteins

Parasitology ◽  
1999 ◽  
Vol 119 (4) ◽  
pp. 331-336 ◽  
Author(s):  
A. ADINI ◽  
A. WARBURG
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Specific Antigen ◽  
Growth Factor Receptor ◽  
Extracellular Matrix Proteins ◽  
Growth Period ◽  
Collagen Iv ◽  
Matrix Proteins ◽  
Collagen Type Iv ◽  
Plasmodium Gallinaceum

Plasmodium ookinetes are elongate, motile and invasive while inside the mosquito gut but promptly metamorphose into spherical immobile oocysts upon coming in contact with the basement membrane surrounding the midgut. There they begin a prolonged growth period characterized by massive DNA synthesis for the production of sporozoites. Living Plasmodium gallinaceum ookinetes attached avidly to the murine extracellular matrix proteins, laminin and collagen type IV. In ELISA-type assays, the main ookinete surface protein, Pgs28 was implicated as a mediator of parasite attachment to these basement membrane constituents. Laminin and collagen IV adhered to ookinete and oocyst lysates spotted onto nitrocellulose membranes. Receptor–ligand blot assays demonstrated that Pgs28 and an oocyst-specific antigen recognized by the mAb 10D6 interact with murine collagen IV and laminin. 10D6 antigen was also recognized by monospecific antiserum against the human epidermal growth factor receptor. Mosquito-derived laminin was incorporated into oocyst capsules of P. gallinaceum growing in Aedes aegypti. We hypothesize that contact with the mosquito basement membrane triggers the transformation of ookinetes into oocysts. Coalescence of basement membrane proteins onto the capsules masks developing oocysts from the mosquito's immune system and facilitates their prolonged extracellular development in the mosquito body cavity.

scholarly journals Association of endometriosis in horses with differentiation of periglandular myofibroblasts and changes of extracellular matrix proteins

Reproduction ◽  
2001 ◽  
pp. 581-586 ◽  
Author(s):  
I Walter ◽  
J Handler ◽  
M Reifinger ◽  
C Aurich
Keyword(s):  
Extracellular Matrix ◽  
Smooth Muscle Actin ◽  
Extracellular Matrix Proteins ◽  
Collagen Type I ◽  
Collagen I ◽  
Matrix Proteins ◽  
Type I ◽  
Malignant Tumours ◽  
Normal Endometrium ◽  
Collagen Iii

Periglandular fibrosis and cystic dilation of uterine glands are associated with equine endometriosis. The presence of extracellular matrix proteins (collagen type I, III and IV, laminin and fibronectin) in healthy and endometriotic specimens was demonstrated by immunohistochemistry. The distribution of collagen I, but not collagen III, was dependent on the stage of the oestrous cycle. The arrangement of collagen I and collagen III in endometriotic specimens was similar to that in normal endometrium. In periglandular fibrosis, collagen IV, laminin and fibronectin deposition outside the basement membrane was observed. In these regions, stromal cells were characterized immunohistochemically as myofibroblasts because of their expression of a-smooth muscle actin, and occasionally tropomyosin and desmin. Periglandular differentiation of contractile cells could be interpreted as a reaction to support the extrusion of secretions in cystic dilated glands. Moreover, the changes of extracellular matrix proteins are characteristic for neoplastic lesions, although further development of endometriosis to benign or malignant tumours is not known in horses. Knowledge of the factors responsible for these fibroblastic modulations may be the key to explaining the pathogenesis of endometriosis.

Extracellular matrix proteins control the growth of cerebellar medulloblastoma cells

2004 ◽  
Vol 216 (03) ◽  
Author(s):  
U Schüller ◽  
W Hartmann ◽  
A Koch ◽  
K Schilling ◽  
OD Wiestler ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Cerebellar Medulloblastoma
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