scholarly journals Interaction of astrochondrin with extracellular matrix components and its involvement in astrocyte process formation and cerebellar granule cell migration.

1993 ◽  
Vol 120 (3) ◽  
pp. 799-814 ◽  
Author(s):  
A Streit ◽  
C Nolte ◽  
T Rásony ◽  
M Schachner
Keyword(s):  
Granule Cell ◽  
Granular Layer ◽  
Collagen Type ◽  
Granule Cells ◽  
Collagen Type Iv ◽  
Collagen Types ◽  
Type Iv ◽  
Process Formation ◽  
Extracellular Matrix Components ◽  
Matrix Components

We have recently characterized a chondroitin sulfate proteoglycan from the murine central nervous system which is expressed by astrocytes in vitro and carries the L2/HNK-1 and L5 carbohydrate structures. In the present study, we provide evidence that its three core proteins of different size are similar in their proteolytic peptide maps and thus designate this group of structurally related molecules astrochondrin. During development, astrochondrin and the L5 carbohydrate were hardly detectable in the brain of 14-d-old mouse embryos by Western blot analysis. Expression of astrochondrin and the L5 epitope was highest at postnatal day 8, the peak of cerebellar granule cell migration and Bergmann glial process formation, and decreased to weakly detectable levels in the adult. Immunocytochemical localization of astrochondrin in the cerebellar cortex of 6-d-old mice showed association of immunoreactivity with the cell surface of astrocytes, including Bergmann glial processes and astrocytes in the internal granular layer or prospective white matter. Endfeet of astrocytes contacting the basal lamina of endothelial and meningeal cells and contact sites between Bergmann glial processes and granule cells also showed detectable levels of astrochondrin. Furthermore, granule cell axons in the molecular layer were astrochondrin immunoreactive. In the adult, astrochondrin immunoreactivity was weakly present in the internal granular layer and white matter. Both Fab fragments of polyclonal antibodies to astrochondrin and monovalent fragments of the L5 monoclonal antibody reduced the formation of processes of mature GFAP-positive astrocytes on laminin and collagen type IV, but not on fibronectin as substrata. Interestingly, the initial attachment of astrocytic cell bodies was not disturbed by these antibodies. Antibodies to astrochondrin also reduced the migration of granule cells in the early postnatal mouse cerebellar cortex. In a solid phase radioligand binding assay, astrochondrin was shown to bind to the extracellular matrix components laminin and collagen type IV, being enhanced in the presence of Ca2+, but not to fibronectin, J1/tenascin or other neural recognition molecules. Furthermore, astrochondrin interacted with collagen types III and V, less strongly with collagen types I, II, and IX, but not with collagen type VI. The interaction of astrochondrin with collagen types III and V was saturable and susceptible to increasing ionic strength, and could be competed by chondroitin sulfate, heparin, and dextran sulfate, but not by hyaluronic acid, glucose-6-phosphate, or neuraminic acid.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals Recombinant human bone morphogenetic protein 2B stimulates PC12 cell differentiation: potentiation and binding to type IV collagen.

1992 ◽  
Vol 119 (6) ◽  
pp. 1721-1728 ◽  
Author(s):  
V M Paralkar ◽  
B S Weeks ◽  
Y M Yu ◽  
H K Kleinman ◽  
A H Reddi
Keyword(s):  
Extracellular Matrix ◽  
Cell Differentiation ◽  
Bone Morphogenetic Protein ◽  
Collagen Type ◽  
Activin A ◽  
Collagen Type Iv ◽  
Type Iv ◽  
Morphogenetic Protein ◽  
Extracellular Matrix Components ◽  
Matrix Components

Bone morphogenetic protein 2B (BMP 2B, also known as BMP 4) induces cartilage and bone morphogenesis in ectopic extraskeletal sites. BMP 2B is one of several bone morphogenetic proteins which along with activins and inhibins are members of the transforming growth factor-beta (TGF-beta) family. Both BMP 2B and activin A, but not TGF-beta 1, induce rat pheochromocytoma PC12 neuronal cell differentiation and expression of VGF, a nervous system-specific mRNA. PC12 cells exhibited approximately 2,500 receptors per cell for BMP 2B with an apparent dissociation constant of 19 pM. Extracellular matrix components, including fibronectin, laminin, and collagen type IV potentiated the activity of BMP and activin A, with the latter being the most active. Direct experiments demonstrated that radioiodinated BMP 2B bound to collagen type IV better than to either laminin or fibronectin. These data demonstrate a common neurotrophic activity of both BMP 2B and activin A, and suggest that these regulatory molecules alone and in conjunction with extracellular matrix components may play a role in both the development and repair of nervous tissue.

scholarly journals Migration through the Extracellular Matrix by the Parasitic Protozoan Leishmania Is Enhanced by Surface Metalloprotease gp63

2003 ◽  
Vol 71 (2) ◽  
pp. 1008-1010 ◽  
Author(s):  
Bradford S. McGwire ◽  
Kwang-Poo Chang ◽  
David M. Engman
Keyword(s):  
Extracellular Matrix ◽  
Collagen Type ◽  
Collagen Type Iv ◽  
Parasitic Protozoan ◽  
Type Iv ◽  
Extracellular Matrix Components ◽  
Matrix Components

ABSTRACT Leishmania species engineered to express high levels of the surface metalloprotease gp63 have enhanced capacity of migration through extracellular matrix in vitro. This correlates with gp63 degradation of extracellular matrix components, such as collagen type IV and fibronectin, and suggests an important role for gp63 in the pathogenesis of leishmaniasis.

scholarly journals Platelet adhesion to collagen in healthy volunteers is influenced by variation of both α2β1 density and von Willebrand factor

Blood ◽  
2000 ◽  
Vol 96 (4) ◽  
pp. 1433-1437 ◽  
Author(s):  
Mark Roest ◽  
Jan J. Sixma ◽  
Ya-Ping Wu ◽  
Martin J. W. Ijsseldijk ◽  
Mariëlle Tempelman ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
Collagen Type ◽  
Normal Subjects ◽  
Collagen Type Iv ◽  
Collagen Types ◽  
Platelet Surface ◽  
Type Iv ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Platelet thrombus formation on collagen is initiated by platelet GPIb interaction with von Willebrand factor (vWF) bound to collagen, followed by firm attachment of the platelet to collagen by the integrin α2β1. Platelet and plasma vWF levels and α2β1 density on the platelet surface are highly variable among normal subjects; however, little is known about the consequences of this variability on platelet adhesion to collagen. A population of 32 normal subjects was studied to evaluate the relation between genetic and phenotypic variations of α2β1 density on the platelet surface, plasma vWF levels, platelet vWF levels, and adenosine diphosphate and adenosine triphosphate concentrations on the one hand and platelet adhesion to collagen under flow on the other hand. Platelet adhesion to collagen types I and III under flow was correlated with plasma levels of vWF (r2 = 0.45 and 0.42, respectively) and α2β1 density on the platelet surface (r2 = 0.35 and 0.17, not significant). Platelet adhesion to collagen type IV under flow was significantly correlated with platelet vWF levels (r2 = 0.34) and α2β1 density on the platelet surface (r2 = 0.42). Platelet adhesion to collagen types I and III depends on both plasma levels of vWF and α2β1 density on the platelet surface, whereas platelet adhesion to collagen type IV is mediated by both platelet vWF levels and α2β1 density on the platelet surface.

Extracellular matrix components in the heart of the white bass, Morone chrysops (Rafinesque)

1994 ◽  
Vol 72 (3) ◽  
pp. 449-454
Author(s):  
Dominic S. Raso ◽  
Louis Terracio ◽  
Thomas K. Borg
Keyword(s):  
Type Iv Collagen ◽  
Collagen Type ◽  
Periodic Acid ◽  
Longitudinal Axis ◽  
Collagen Type Iv ◽  
Histological Techniques ◽  
White Bass ◽  
Morone Chrysops ◽  
Type Iv ◽  
Extracellular Matrix Components

The distribution of laminin, collagen type IV, collagen bundles, proteoglycans, elastin, and periodic acid–Schiff's moieties (glycoproteins) within the heart of the adult white bass, Morone chrysops (Rafinesque), was investigated by means of immunohistochemical and histological techniques. Laminin and collagen type IV were heavily expressed within the epimysium and the basal lamina of the lining epicardial epithelium and valvular endothelium, moderately expressed within the myocardium, and slightly expressed within the subendocardium. This co-localized distribution of laminin and collagen type IV corresponds to the biochemically unidentified basal and external lamina observed in the hearts of other fish by previous ultrastructural investigations and is similar to the distribution observed in the hearts of birds and mammals. Also demonstrated was an interesting division of connective tissue components along the longitudinal axis of the atrioventricular valve, which is most likely intimately involved with the effective functioning and durability of the valve.

scholarly journals Morphometric analysis of the human endoneurial extracellular matrix components during aging

2021 ◽  
Vol 73 (1) ◽  
pp. 103-110
Author(s):  
Braca Kundalic ◽  
Sladjana Ugrenovic ◽  
Ivan Jovanovic ◽  
Vladimir Petrovic ◽  
Aleksandar Petrovic ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Collagen Type ◽  
Linear Regression Analysis ◽  
Collagen Type I ◽  
Nerve Fibers ◽  
Collagen Type Iv ◽  
Type I ◽  
Type Iv ◽  
Ecm Proteins ◽  
Extracellular Matrix Components

The aim of this study was to analyze the expression of extracellular matrix (ECM) proteins in human endoneurium during aging. We harvested 15 cadaveric sural nerves, distributed in 3 age groups (I: 25-44, II: 45-64, III: 65-86 years old). Histological sections were stained immunohistochemically for the presence of collagen type I, type IV and laminin, and the ImageJ processing program was used in morphometrical analysis to determine the percentages of these endoneurial proteins. In two younger groups, the endoneurial matrix of the sural nerve was composed from about equal proportions of these proteins, which may be considered a favorable microenvironment for the regeneration of nerve fibers. Linear regression analysis showed a significant increase in endoneurial collagen type IV with age, while collagen type I and laminin significantly decreased during the aging process. In cases older than 65 years, remodeling of the endoneurial matrix was observed to be significantly higher for the presence of collagen type IV, and lower for the expression of collagen type I and laminin. This age-related imbalance of ECM proteins could represent a disadvantageous microenvironment for nerve fiber regeneration in older adults. Our findings contribute to the development of therapeutic approaches for peripheral nerve regeneration.

scholarly journals Platelet adhesion to collagen in healthy volunteers is influenced by variation of both α2β1 density and von Willebrand factor

Blood ◽  
2000 ◽  
Vol 96 (4) ◽  
pp. 1433-1437 ◽  
Author(s):  
Mark Roest ◽  
Jan J. Sixma ◽  
Ya-Ping Wu ◽  
Martin J. W. Ijsseldijk ◽  
Mariëlle Tempelman ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
Collagen Type ◽  
Normal Subjects ◽  
Collagen Type Iv ◽  
Collagen Types ◽  
Platelet Surface ◽  
Type Iv ◽  
Von Willebrand ◽  
Willebrand Factor

Platelet thrombus formation on collagen is initiated by platelet GPIb interaction with von Willebrand factor (vWF) bound to collagen, followed by firm attachment of the platelet to collagen by the integrin α2β1. Platelet and plasma vWF levels and α2β1 density on the platelet surface are highly variable among normal subjects; however, little is known about the consequences of this variability on platelet adhesion to collagen. A population of 32 normal subjects was studied to evaluate the relation between genetic and phenotypic variations of α2β1 density on the platelet surface, plasma vWF levels, platelet vWF levels, and adenosine diphosphate and adenosine triphosphate concentrations on the one hand and platelet adhesion to collagen under flow on the other hand. Platelet adhesion to collagen types I and III under flow was correlated with plasma levels of vWF (r2 = 0.45 and 0.42, respectively) and α2β1 density on the platelet surface (r2 = 0.35 and 0.17, not significant). Platelet adhesion to collagen type IV under flow was significantly correlated with platelet vWF levels (r2 = 0.34) and α2β1 density on the platelet surface (r2 = 0.42). Platelet adhesion to collagen types I and III depends on both plasma levels of vWF and α2β1 density on the platelet surface, whereas platelet adhesion to collagen type IV is mediated by both platelet vWF levels and α2β1 density on the platelet surface.

scholarly journals Enterococcus faecalis Adhesin, Ace, Mediates Attachment to Extracellular Matrix Proteins Collagen Type IV and Laminin as well as Collagen Type I

2000 ◽  
Vol 68 (9) ◽  
pp. 5218-5224 ◽  
Author(s):  
Sreedhar R. Nallapareddy ◽  
Xiang Qin ◽  
George M. Weinstock ◽  
Magnus Höök ◽  
Barbara E. Murray
Keyword(s):  
Extracellular Matrix ◽  
Enterococcus Faecalis ◽  
Collagen Type ◽  
Collagen Type I ◽  
Immune Serum ◽  
Collagen Type Iv ◽  
Type I ◽  
Collagen Types ◽  
Type Iv ◽  
Ecm Proteins

ABSTRACT Adhesin-mediated binding to extracellular matrix (ECM) proteins is thought to be a crucial step in the pathogenic process of many bacterial infections. We have previously reported conditional adherence of most Enterococcus faecalis isolates, after growth at 46°C, to ECM proteins collagen types I and IV and laminin; identified an E. faecalis-specific gene, ace, whose encoded protein has characteristics of a bacterial adhesin; and implicated Ace in binding to collagen type I. In this study, we constructed an ace disruption mutant from E. faecalis strain OG1RF that showed marked reduction in adherence to collagen types I and IV and laminin when compared to the parental OG1RF strain after growth at 46°C. Polyclonal immune serum raised against the OG1RF-derived recombinant Ace A domain reacted with a single ∼105-kDa band of mutanolysin extracts from OG1RF grown at 46°C, while no band was detected in extracts from OG1RF grown at 37°C, nor from the OG1RF ace mutant grown at 37 or 46°C. IgGs purified from the anti-Ace A immune serum inhibited adherence of 46°C-grown E. faecalis OG1RF to immobilized collagen type IV and laminin as well as collagen type I, at a concentration as low as 1 μg/ml, and also inhibited the 46°C-evoked adherence of two clinical isolates tested. We also showed in vitro interaction of collagen type IV with Ace from OG1RF mutanolysin extracts on a far-Western blot. Binding of recombinant Ace A to immobilized collagen types I and IV and laminin was demonstrated in an enzyme-linked immunosorbent assay and was shown to be concentration dependent. These results indicate that Ace A mediates the conditional binding of E. faecalis OG1RF to collagen type IV and laminin in addition to collagen type I.

scholarly journals Evidence for the location of a binding sequence for the α2β1 integrin of endothelial cells, in the β1 subunit of laminin

1995 ◽  
Vol 309 (3) ◽  
pp. 765-771 ◽  
Author(s):  
P A Underwood ◽  
F A Bennett ◽  
A Kirkpatrick ◽  
P A Bean ◽  
B A Moss
Keyword(s):  
Endothelial Cells ◽  
Cell Adhesion ◽  
Type Iv Collagen ◽  
Collagen Type ◽  
Collagen Type Iv ◽  
Collagen Types ◽  
Type Iv ◽  
Integrin Binding Site ◽  
Beta 1 Integrin ◽  
Laminin 1

To date no specific location on laminin 1 for the binding of alpha 2 beta 1 integrin has been described, although recent evidence supports a location in the E1XNd fragment of the cross region. We have identified a peptide sequence from this region, in the beta 1 chain of laminin 1, YGYYGDALR, which inhibits the adhesion of endothelial cells to laminin 1 and type-IV collagen. A structurally related sequence from the CNBr-cleaved fragment CB3 of the alpha 1 chain of collagen type IV, FYFDLR, inhibits endothelial cell adhesion to both collagen types I and IV and laminin 1. The CB3 fragment containing the FYFDLR sequence has been shown to contain binding sites for both alpha 1 beta 1 and alpha 2 beta 1 integrins. Present experiments with anti-integrin antibodies indicate that the alpha 2 beta 1 integrin on endothelial cells can account for all the cell binding to collagen types I and IV, and that this integrin makes a major contribution towards the adhesion of these cells to laminin 1. We therefore propose that the peptide FYFDLR participates in alpha 2 beta 1 binding to collagen type IV and that the putatively structurally similar peptide, YGYYGDALR, participates in alpha 2 beta 1 binding to laminin 1. This is the first account of structurally related peptide sequences from laminin 1 and type-IV collagen which show reciprocal inhibition of cell adhesion to either ligand and which might form part of a common integrin-binding site, as well as the first suggestion of a precise location contributing to the alpha 2 beta 1 integrin binding site on laminin 1.

scholarly journals Human Basement Membrane Collagens do not Elicit Platelet Aggregation

1977 ◽  
Author(s):  
R. L. Trelstad ◽  
A. C. Carvalho
Keyword(s):  
Platelet Aggregation ◽  
Basement Membrane ◽  
Collagen Type ◽  
Serotonin Release ◽  
Basement Membranes ◽  
Collagen Type Iv ◽  
Collagen Types ◽  
Type Iv ◽  
Skin Collagen ◽  
Human Collagen

The immediate subendothelial connective tissue matrix consists of the basement membrane, a collagenous felt-like cell surface coat. The collagen from basement membranes has been isolated from human lung, skin, and kidney using a new fractionation method which separates native forms of collagen Types I, II, III, and IV. The Type IV collagens from the basement membranes have been characterized in respect to amino acid and carbohydrate composition, molecular size, charge and native structure. Antibodies prepared against the Type IV collagen reacted with both epithelial and vascular basement membranes as judged by immunofluorescence. Platelet-rich plasma (250,000/μl) from 5 normal subjects were tested for aggregation and 14C-serotonin release with human collagen Types I, II, III, and IV. Complete aggregation (100%) and 14C-serotonin release (80–100%) was obtained when Types I, II, and III were used. Human kidney, lung, and skin collagen Type IV (10–100μg/ml) did not aggregate platelets nor cause release of their contents. Pre-incubation of platelets and human collagen Type IV for periods of 30 minutes did not result in inhibition of platelet aggregation by Types I, II, or III.These data indicate that the collagenous component of the basement membrane, the first extra-vascular collagen to which a platelet is exposed, does not elicit aggregation as do the fibrillar collagens in the perivascular matrix.

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