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 Expression of collagen type IV in human kidney during prenatal development

2020 ◽  
pp. 111-111
Author(s):  
Vladimir Petrovic ◽  
Ivan Nikolic ◽  
Marko Jovic ◽  
Vladimir Zivkovic ◽  
Miodrag Jocic ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Collagen Type ◽  
Kidney Tissue ◽  
Volume Density ◽  
Collagen Iv ◽  
Basement Membranes ◽  
Collagen Type Iv ◽  
Type Iv ◽  
Metanephric Kidney ◽  
Collecting System

Background / Aim. Type IV collagen belongs to the group of non-fibrillar collagens and is an important component of the basement membranes where it accounts for approximately 50% of its structural elements. The aim of the paper was to describe the expression and distribution of collagen type IV in embryonic and fetal metanephric kidney, and to determine the volume density of collagen type IV in kidney tissue in each trimester of development. Methods. The material consisted of 19 human embryos/fetuses, in the gestational age from 8th to 37th week. Kidney tissue specimens were routinely processed to paraffin molds and stained with hematoxylin and eosin and immunohistochemically using polyclonal anti-collagen IV antibody. Stained slides were examined using light microscope and images of the selected areas, under different lens magnification were captured with digital camera. Volume density of collagen type IV was determined by using ImageJ 1.48v and a plugin of the software which inserted a grid system with 336 points. For the data comparison One-Way Analysis of Variance was used. Results. Strong collagen IV immunopositivity was seen in all specimens, with a distribution in the basement membranes of urinary bud, parietal leaf of Bowman?s capsule, glomerular basement membrane, basement membrane of interstitial blood vessels, and basement membranes of nephron tubules and collecting ducts. No statistically significant difference in the volume density of type IV collagen was found between the different trimesters of development. Conclusion. The synthesis and secretion of collagen type IV simultaneously follows the development of nephron structures, collecting system and blood vessels. The volume density of collagen type IV remains constant throughout all the trimesters of metanephric kidney development, indicating that it plays a crucial role in normal development of nephron and collecting system structures, as well as in maintaining the normal kidney function.

Selective increase in the binding of the alpha 1 beta 1 integrin for collagen type IV during neurite outgrowth of human neuroblastoma TR 14 cells

1994 ◽  
Vol 107 (12) ◽  
pp. 3379-3392
Author(s):  
G. Carmeliet ◽  
B. Himpens ◽  
J.J. Cassiman
Keyword(s):  
Neurite Outgrowth ◽  
Collagen Type ◽  
Collagen Type I ◽  
Collagen Type Iv ◽  
Type I ◽  
Human Neuroblastoma ◽  
Specific Antibodies ◽  
Type Iv ◽  
Beta 1 Integrin ◽  
In Cells

Regulation of beta 1 integrins in neurite outgrowth following N6,2′-O-dibutyryladenosine 3′:5′-cyclic monophosphate (dBcAMP) treatment was investigated using the human neuroblastoma cell line TR 14. Three beta 1 integrins were identified: the alpha 1 beta 1 receptor bound collagen type I, collagen type IV and probably laminin; the alpha 2 beta 1 integrin bound collagen type I; and the alpha v beta i receptor bound fibronectin. Neurite extension was detectable as early as 30 minutes following dBcAMP treatment, was maximal after 24 hours and remained constant during treatment for 4 days. Adhesion-perturbing beta 1 subunit-specific antibodies, added together with dBcAMP, prevented the outgrowth of new neurites. During the first 24 hours of neurite outgrowth, no change was observed in the amount of beta 1 integrins nor in their topographic distribution. However, dBcAMP treatment increased the binding of alpha 1 beta 1 receptors to collagen type IV-Sepharose by a factor 2.3 +/- 0.6 (P < 0.02), while no alteration in the binding to collagen type I was detected. Moreover, neurites and growth cones were immunoreactive for collagen type IV but not for collagen type I. Consistently dBcAMP-induced neurite outgrowth was inhibited by adhesion-perturbing alpha 1 subunit-specific antibodies. Following maximal neurite outgrowth, the amount of beta 1 integrins determined by immunoprecipitation and by confocal microscopy decreased to 58.3 +/- 11.2% (P < 0.001) and to 55.4 +/- 17.5% (P < 0.001) of untreated levels, respectively, without any change in the level of beta 1 mRNA or de novo synthesized beta 1 precursor. However, pulse-chase experiments showed an increased turnover of the beta 1 subunit: the amount of beta 1 precursor that was degraded after 1 hour chase was 50.5 +/- 8.4% in cells treated for 4 days and 34.2 +/- 3.9% in untreated cells (P < 0.02); the amount of mature beta 1 after 24 hours chase was smaller in cells treated for 4 days compared to untreated cells. In conclusion, during neurite outgrowth, alpha 1 beta 1 integrins are required and acquire an enhanced binding activity for collagen type IV; but following maximal neurite outgrowth, expression of beta 1 integrins is reduced.

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.

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)

Malotilate Prevents Accumulation of Type III pN-Collagen, Type IV Collagen, and Laminin in Carbon Tetrachloride-induced Pulmonary Fibrosis in Rats

1989 ◽  
Vol 139 (5) ◽  
pp. 1105-1111 ◽  
Author(s):  
Paavo Pääkkö ◽  
Raija Sormunen ◽  
Leila Risteli ◽  
Juha Risteli ◽  
Leena Ala-Kokko ◽  
...  
Keyword(s):  
Carbon Tetrachloride ◽  
Pulmonary Fibrosis ◽  
Type Iv Collagen ◽  
Collagen Type ◽  
Collagen Type Iv ◽  
Type Iii ◽  
Type Iv

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 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.

Distribution of laminin, collagen type IV, collagen type I, and fibronectin in chicken cardiac jelly/basement membrane

1989 ◽  
Vol 224 (3) ◽  
pp. 417-425 ◽  
Author(s):  
Charles D. Little ◽  
Dominique M. Piquet ◽  
Lynn A. Davis ◽  
Luanne Walters ◽  
Christopher J. Drake
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Collagen Type ◽  
Collagen Type I ◽  
Collagen Type Iv ◽  
Type I ◽  
Type Iv

scholarly journals Intracellular signaling of transcription and secretion of type IV collagen after angiotensin II-induced cellular hypertrophy in cultured proximal tubular cells.

1991 ◽  
Vol 2 (3) ◽  
pp. 219-227 ◽  
Author(s):  
G Wolf ◽  
P D Killen ◽  
E G Neilson
Keyword(s):  
Angiotensin Ii ◽  
Type Iv Collagen ◽  
Collagen Type ◽  
Regulatory Elements ◽  
Collagen Type Iv ◽  
Intracellular Camp ◽  
Tubular Epithelium ◽  
Cellular Hypertrophy ◽  
Type Iv ◽  
Proximal Tubular

Physiologic concentrations of angiotensin II (AII) can induce cellular hypertrophy in murine proximal tubular epithelium (MCT cells). This response is characterized by an increase in cell size, new protein synthesis, and by the secretion of new basement membrane type IV collagen in the absence of cellular proliferation. The present study was undertaken to evaluate the second messengers of these AII-induced cellular events with special reference to the increase in type IV collagen secretion. In initial experiments we observed that pretreatment of MCT cells with agents that increase concentrations of intracellular cAMP, like forskolin, dibutyryl cAMP, and isobutyl-methyl-xanthine abolish AII-induced amino acid incorporation, but have no effect on control cells or on their proliferation. In addition, 10(-8) M AII significantly decreased the concentration of intracellular cAMP. Phorbolesters were without significant effect on the hypertrophy or proliferation of AII-stimulated MCT cells or their rested controls. The transfection of MCT cells with reporter genes containing regulatory elements for type IV collagen revealed that the stimulatory effects of AII on collagen type IV depend, at least to some extent, on an increase in gene transcription. Agents increasing intracellular cAMP concentrations inhibited the AII-induced increase in transcription and secretion of collagen type IV, but had no effect on MCT cells grown in media without AII. Our findings provide evidence that AII-induced changes in tubular epithelium leading to the secretion of type IV collagen are mediated by a decrease in intracellular cAMP.

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