Expression of the Extracellular Matrix Proteins Collagen I, Collagen III and Fibronectin and Matrix Metalloproteinase-1 and -13 in the Skin of Patients with Inguinal Hernia

1999 ◽  
Vol 31 (6) ◽  
pp. 480-490 ◽  
Author(s):  
U. Klinge ◽  
H. Zheng ◽  
Z. Si ◽  
V. Schumpelick ◽  
R.S. Bhardwaj ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Inguinal Hernia ◽  
Matrix Metalloproteinase ◽  
Extracellular Matrix Proteins ◽  
Collagen I ◽  
Matrix Proteins ◽  
Matrix Metalloproteinase 1 ◽  
Collagen Iii

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.

scholarly journals Immunohistochemical evaluation of fibrillar components of the extracellular matrix of transversalis fascia and anterior abdominal rectus sheath in men with inguinal hernia

2014 ◽  
Vol 41 (1) ◽  
pp. 23-29 ◽  
Author(s):  
Rogério De Oliveira Gonçalves ◽  
Evandro De Moraes e Silva ◽  
Gaspar De Jesus Lopes Filho
Keyword(s):  
Extracellular Matrix ◽  
Inguinal Hernia ◽  
Rectus Sheath ◽  
Staining Technique ◽  
Collagen I ◽  
Elastic Fibers ◽  
Collagen Iii ◽  
Extracellular Matrix Components ◽  
Matrix Components ◽  
Age Range

OBJECTIVE: to evaluate the role of fibrillar extracellular matrix components in the pathogenesis of inguinal hernias. METHODS: samples of the transverse fascia and of the anterior sheath of the rectus abdominis muscle were collected from 40 men aged between 20 and 60 years with type II and IIIA Nyhus inguinal hernia and from 10 fresh male cadavers (controls) without hernia in the same age range. The staining technique was immunohistochemistry for collagen I, collagen III and elastic fibers; quantification of fibrillar components was performed with an image analysis processing software. RESULTS: no statistically significant differences were found in the amount of elastic fibers, collagen I and collagen III, and the ratio of collagen I / III among patients with inguinal hernia when compared with subjects without hernia. CONCLUSION: the amount of fibrillar extracellular matrix components did not change in patients with and without inguinal hernia.

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.

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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