scholarly journals Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP)

1991 ◽  
Vol 277 (1) ◽  
pp. 277-279 ◽  
Author(s):  
G Murphy ◽  
M I Cockett ◽  
R V Ward ◽  
A J P Docherty
Keyword(s):  
Matrix Metalloproteinases ◽  
Connective Tissue ◽  
Matrix Metalloproteinase ◽  
Quantitative Data ◽  
Type Iv Collagen ◽  
Quantitative Comparison ◽  
Degrading Enzymes ◽  
Type Iv ◽  
The Matrix

The abilities of the matrix metalloproteinases 95 kDa and 72 kDa gelatinases (type IV collagenases), stromelysins-1 and -2 and punctuated metalloproteinase (PUMP) to degrade insoluble elastin, type IV collagen films and proteoglycan have been compared. The gelatinases and PUMP were markedly more active in the degradation of elastin than were the stromelysins. PUMP and the stromelysins were more potent proteoglycan-degrading enzymes. All of the enzymes studied degraded soluble native type IV collagen, but the gelatinases were more effective at higher temperatures. These quantitative data allow an analysis of the potential relative roles of these metalloproteinases in the breakdown of the key components of connective tissue matrices.

scholarly journals Hereditary Connective Tissue Diseases in Young Adult Stroke: A Comprehensive Synthesis

2011 ◽  
Vol 2011 ◽  
pp. 1-18 ◽  
Author(s):  
Olivier M. Vanakker ◽  
Dimitri Hemelsoet ◽  
Anne De Paepe
Keyword(s):  
Connective Tissue ◽  
Metabolic Disorders ◽  
Type Iv Collagen ◽  
Connective Tissue Diseases ◽  
Haemorrhagic Stroke ◽  
Monogenic Disease ◽  
Connective Tissue Disorders ◽  
Ehlers Danlos Syndrome ◽  
Type Iv ◽  
Danlos Syndrome

Though the genetic background of ischaemic and haemorrhagic stroke is often polygenetic or multifactorial, it can in some cases result from a monogenic disease, particularly in young adults. Besides arteriopathies and metabolic disorders, several connective tissue diseases can present with stroke. While some of these diseases have been recognized for decades as causes of stroke, such as the vascular Ehlers-Danlos syndrome, others only recently came to attention as being involved in stroke pathogenesis, such as those related to Type IV collagen. This paper discusses each of these connective tissue disorders and their relation with stroke briefly, emphasizing the main clinical features which can lead to their diagnosis.

Comparative analysis of basal lamina type IV collagen α chains, matrix metalloproteinases-2 and -9 expressions in oral dysplasia and invasive carcinoma

2013 ◽  
Vol 115 (2) ◽  
pp. 113-119 ◽  
Author(s):  
Ryo Tamamura ◽  
Hitoshi Nagatsuka ◽  
Chong Huat Siar ◽  
Naoki Katase ◽  
Ichiro Naito ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Matrix Metalloproteinases ◽  
Basal Lamina ◽  
Type Iv Collagen ◽  
Invasive Carcinoma ◽  
Oral Dysplasia ◽  
Type Iv

scholarly journals Nonenzymatic glycation of type IV collagen and matrix metalloproteinase susceptibility

1997 ◽  
Vol 52 (5) ◽  
pp. 1302-1312 ◽  
Author(s):  
Joni D. Mott ◽  
Raja G. Khalifah ◽  
Hideaki Nagase ◽  
Charles F. Shield ◽  
Julie K. Hudson ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Type Iv Collagen ◽  
Nonenzymatic Glycation ◽  
Type Iv

Expression of matrix metalloproteinases, type IV collagen, and interleukin-10 in rabbits treated with morphine after lamellar keratectomy

2011 ◽  
Vol 15 (3) ◽  
pp. 153-163 ◽  
Author(s):  
Alexandre P. Ribeiro ◽  
Miguel L. Silva ◽  
Rodrigo L. Araújo ◽  
Danilo L. Ferrucci ◽  
Tiago Mineo ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Type Iv Collagen ◽  
Interleukin 10 ◽  
Type Iv

scholarly journals Regulation of proteinases during mouse peri-implantation development: urokinase-type plasminogen activator expression and cross talk with matrix metalloproteinase 9

Reproduction ◽  
2011 ◽  
Vol 141 (2) ◽  
pp. 227-239 ◽  
Author(s):  
M G Martínez-Hernández ◽  
L A Baiza-Gutman ◽  
A Castillo-Trápala ◽  
D Randall Armant
Keyword(s):  
Matrix Metalloproteinase ◽  
Mrna Expression ◽  
Plasminogen Activator ◽  
Type Iv Collagen ◽  
Matrix Metalloproteinase 9 ◽  
Trophoblast Cells ◽  
Type Iv ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Metalloproteinase 9

Trophoblast cells express urokinase-type plasminogen activator (PLAU) and may depend on its activity for endometrial invasion and tissue remodeling during peri-implantation development. However, the developmental regulation, tissue distribution, and function of PLAU are not completely understood. In this study, the expression of PLAU and its regulation by extracellular matrix proteins was examined by RT-PCR, immunocytochemistry, and plasminogen–casein zymography in cultured mouse embryos. There was a progressive increase inPlaumRNA expression in blastocysts cultured on gestation days 4–8. Tissue-type plasminogen activator (55 kDa) and PLAU (a triplet of 40, 37, and 31 kDa) were present in conditioned medium and embryo lysates, and were adsorbed to the culture plate surface. The temporal expression pattern of PLAU, according to semi-quantitative gel zymography, was similar in non-adhering embryos and embryos cultured on fibronectin, laminin, or type IV collagen, although type IV collagen and laminin upregulatedPlaumRNA expression. Immunofluorescence revealed PLAU on the surface of the mural trophectoderm and in non-spreading giant trophoblast cells. Exogenous human plasminogen was transformed to plasmin by cultured embryos and activated endogenous matrix metalloproteinase 9 (MMP9). Indeed, the developmental expression profile of MMP9 was similar to that of PLAU. Our data suggest that the intrinsic developmental program predominantly regulates PLAU expression during implantation, and that PLAU could be responsible for activation of MMP9, leading to localized matrix proteolysis as trophoblast invasion commences.

scholarly journals Characterization of muscle epimysium, perimysium and endomysium collagens

1984 ◽  
Vol 219 (3) ◽  
pp. 1017-1026 ◽  
Author(s):  
N Light ◽  
A E Champion
Keyword(s):  
Connective Tissue ◽  
Sodium Dodecyl Sulphate ◽  
Type Iv Collagen ◽  
Sodium Dodecyl ◽  
Basement Membranes ◽  
Type Iii Collagen ◽  
Type I ◽  
Type V Collagen ◽  
Type Iv ◽  
Type V

In the past it has been proven difficult to separate and characterize collagen from muscle because of its relative paucity in this tissue. The present report presents a comprehensive methodology, combining methods previously described by McCollester [(1962) Biochim. Biophys. Acta 57, 427-437] and Laurent, Cockerill, McAnulty & Hastings [(1981) Anal. Biochem. 113, 301-312], in which the three major tracts of muscle connective tissue, the epimysium, perimysium and endomysium, may be prepared and separated from the bulk of muscle protein. Connective tissue thus prepared may be washed with salt and treated with pepsin to liberate soluble native collagen, or can be washed with sodium dodecyl sulphate to produce a very clean insoluble collagenous product. This latter type of preparation may be used for quantification of the ratio of the major genetic forms of collagen or for measurement of reducible cross-link content to give reproducible results. It was shown that both the epimysium and perimysium contain type I collagen as the major component and type III collagen as a minor component; perimysium also contained traces of type V collagen. The endomysium, the sheaths of individual muscle fibres, was shown to contain both type I and type III collagen as major components. Type V collagen was also present in small amounts, and type IV collagen, the collagenous component of basement membranes, was purified from endomysial preparations. This is the first biochemical demonstration of the presence of type IV collagen in muscle endomysium. The preparation was shown to be very similar to other type IV collagens from other basement membranes on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and was indistinguishable from EHS sarcoma collagen and placenta type IV collagen in the electron microscope after rotary shadowing.

scholarly journals Role of type IV collagen and matrix metalloproteinase-9 in remodeling of the left ventricular in coronary artery disease

2019 ◽  
pp. 83-87
Author(s):  
M. A. Popov ◽  
D. V. Shumakov ◽  
D. I. Zybin ◽  
L. E. Gurevich ◽  
V. E. Ashevskaya ◽  
...  
Keyword(s):  
Coronary Artery Disease ◽  
Coronary Artery ◽  
Matrix Metalloproteinase ◽  
Type Iv Collagen ◽  
Basal Membrane ◽  
Left Ventricular ◽  
Type Iv ◽  
Artery Disease ◽  
Metalloproteinase 9

Currently, the analysis of the fibrosis severity during the restructuring of the surrounding extracellular matrix (ECM) is studied in most of the research works devoted to “cardiac remodeling”. At the same time, the role of the basal membrane of cardiomyocytes in heart diseases was not studied. The basal membrane of cardiomyocytes is a highly organized layer of the ECM which is located on the outer side of the sarcolemma. Degradation of ECM components is carried out by different types of matrix metalloproteinases (MMP), which have proteolytic activity and are actively involved in the process of ECM remodeling, destroying its components such as collagen, elastin, fibronectin, glycosaminoglycans and other structural components.Aim. To evaluate the ECM status in patients with coronary artery disease and its effect on left ventricular myocardial remodeling.Material and methods. Morphological and immunohistochemical (IHC) examination of left ventricular myocardial biopsies was performed in 16 patients undergoing left ventricular reconstruction in combination with coronary artery bypass grafting.Results. The IHC study revealed the accumulation of matrix metalloproteinase-9 in the cytoplasm of cardiomyocytes. This accumulation was combined with partial or complete destruction of the basal membranes (BM) of cardiomyocytes formed by type IV collagen.Conclusion. Type IV collagen destruction in basal membranes of left ventricular cardiomyocyteswasrevealed. It iscausedbytheactionofmatrixmetalloproteinase-9, which accumulates in the cell cytoplasm.

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