scholarly journals An echistatin C-terminal peptide activates GPIIbIIIa binding to fibrinogen, fibronectin, vitronectin and collagen type I and type IV

1993 ◽  
Vol 293 (1) ◽  
pp. 263-267 ◽  
Author(s):  
P S Wright ◽  
V Saudek ◽  
T J Owen ◽  
S L Harbeson ◽  
A J Bitonti
Keyword(s):  
Protein Interactions ◽  
Collagen Type ◽  
Collagen Type I ◽  
Human Platelets ◽  
Type I ◽  
Venom Protein ◽  
Type Iv ◽  
Fibrinogen Binding ◽  
Additional Protein ◽  
Integrin Ligand

Integrin binding to proteins often involves recognition of domains containing the arginine-glycine-aspartate (RGD) motif. Different binding affinities and specificities of the integrin-ligand protein interactions involve additional protein domains. The n.m.r. structure of the snake-venom protein echistatin suggested that the C-terminal portion of the molecule might be important, in addition to the RGD domain, in binding to the integrin glycoprotein IIbIIIa (GPIIbIIIa) [Saudek, Atkinson and Pelton (1991) Biochem. 30, 7369-7372]. The synthetic C-terminal peptide, echistatin-(40-49), PRNPHKGPAT, (1) inhibited binding of GPIIbIIIa to immobilized echistatin (IC50 3-6 mM), but did not inhibit binding of GPIIbIIIa to immobilized fibrinogen (up to 5 mM peptide), (2) activated GPIIbIIIa binding to fibronectin and vitronectin, usual ligands for the activated integrin, (3) activated binding of GPIIbIIIa to collagen type I and type IV, proteins not usually regarded as ligands for the integrin, and (4) stimulated 125I-fibrinogen binding by human platelets. These findings argue for an interaction of this non-RGD domain in echistatin with GPIIbIIIa, leading to activation of the integrin and extension of the ligand specificity to include immobilized collagen.

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.

Immunohistochemical Localization of Collagen Types I, III, and IV, Laminin, Fibronectin, and Keratin in the Endolymphatic Sac

2000 ◽  
Vol 109 (2) ◽  
pp. 180-186 ◽  
Author(s):  
Teruhiko Harada ◽  
Youngki Kim ◽  
Steven K. Juhn ◽  
Yasuo Sakakura
Keyword(s):  
Collagen Type ◽  
Collagen Type I ◽  
Immunohistochemical Localization ◽  
Basement Membranes ◽  
Endolymphatic Sac ◽  
Type I ◽  
Collagen Types ◽  
Type Iv ◽  
Baseline Information ◽  
Subepithelial Layer

We have employed immunohistochemistry to obtain baseline information on the molecular constituents of the extracellular matrix (ECM) of the endolymphatic duct (ED) and endolymphatic sac (ES) of the chinchilla. The results demonstrated that collagen types I and III were distributed in the subepithelial layer in the ED and ES, type IV collagen and laminin in the basement membranes, and fibronectin in the subepithelial layer and partly in the conglomerated cells in the ES. Collagen type III was diffusely distributed in the whole subepithelial layer of the ES, whereas collagen type I was concentrated densely in the deep layer of the interstitium, although gradually, the cuboidal epithelium in the ES was transformed into a flatter type in the ED. The epithelial cells of the ED and ES were clearly positive for keratin. This study deals, in particular, with the normal distribution of ECM components of the ED and ES of the chinchilla.

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.

Platelet Collagen Activation by Basement Membrane Collagens

1979 ◽  
Author(s):  
L. Balleisen ◽  
J. Rauterberg
Keyword(s):  
Basement Membrane ◽  
Collagen Type ◽  
Normal Subjects ◽  
Collagen Type I ◽  
Short Chain ◽  
Collagen Type Iv ◽  
Type I ◽  
Type Iv ◽  
Aggregation Activity ◽  
Type V

The collagen component of the vessel intima consists of collagen type I, III and basement membrane collagens. For type III a particularly potent platelet aggregation activity was found earlier.Three different basement membrane collagens were isolated from call placenta. Occurence of type IV and V(A/B collagen) in the intimal and medial layer of vessel walls has been shown by chemical and immunhistological means(1). The third basement membrane collagen is probably isentical with the 55000 molecular weight component described by CHUNG et al. (2).Platelets from normal subjects were tested for aggregation and spreading on Zaponlack with type IV, V, the separated A and B chains of type V and the short chain collagen. Complete aggregation was obtained only with native type V collagen. Spreading of platelets was induced only by collagen type IV, the A chain of type V and the short chain collagen.The data indicate that all basement membrane collagens activate platelets but in different respects.1. Rauterberg J. et al.: Coll. Int. Cent. Nat. Rech. Sc. 287:220(1978)2. Chung E. et al.: Bioehem. Biophys. Res. Comm. 71: 1167(1976)

Type I collagen gene regulation and the molecular pathogenesis of cirrhosis

1993 ◽  
Vol 264 (4) ◽  
pp. G589-G595 ◽  
Author(s):  
D. A. Brenner ◽  
J. Westwick ◽  
M. Breindl
Keyword(s):  
Protein Interactions ◽  
Type I Collagen ◽  
Collagen Type ◽  
Collagen Type I ◽  
Molecular Pathogenesis ◽  
Matrix Proteins ◽  
Type I ◽  
And Function ◽  
Collagen Genes ◽  
Insight Into

Cirrhosis is characterized by an increased deposition of extracellular matrix proteins, including type I collagen. Type I collagen is a product of two genes, alpha 1(I) and alpha 2(I), which are generally coordinately regulated. Since expression of type I collagen genes is increased during cirrhosis, understanding the structure and function of the regulatory components of the type I collagen genes should provide insight into the molecular pathogenesis of cirrhosis. This review will analyze the collagen alpha 1(I) gene with respect to chromatin structure, DNA methylation, regulation by agonists, and DNA-protein interactions.

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 Metabolites of type I, II, III, and IV collagen may serve as markers of disease activity in axial spondyloarthritis

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Markéta Hušáková ◽  
Anne-C. Bay-Jensen ◽  
Šárka Forejtová ◽  
Kateřina Zegzulková ◽  
Michal Tomčík ◽  
...  
Keyword(s):  
Disease Activity ◽  
Disease Duration ◽  
Collagen Type ◽  
Axial Spondyloarthritis ◽  
Serum Levels ◽  
Collagen Type I ◽  
Enzyme Linked Immunosorbent Assay ◽  
Type I ◽  
Type Iv ◽  
Affected Tissue

Abstract Local inflammation in axial spondyloarthritis (axSpA) leads to the release of collagen metabolites from the disease-affected tissue. We investigated whether collagen metabolites were associated with disease activity and could distinguish non-radiographic(nr)-axSpA from ankylosing spondylitis (AS). A total of 193 axSpA patients (nr-axSpA, n = 121 and AS, n = 72) and asymptomatic controls (n = 100) were included. Serum levels of metalloproteinase (MMP)-degraded collagen type I (C1M), type II (C2M), type III (C3M) and type IV (C4M2) were quantified by enzyme-linked immunosorbent assay (ELISA). All metabolites were higher in axSpA than in controls (all p < 0.001). Serum levels of C1M, C3M, and C4M2 were increased in AS compared to nr-axSpA (43.4 ng/mL vs. 34.6; p < 0.001, 15.4 vs. 12.8; p = 0.001, and 27.8 vs. 22.4; p < 0.001). The best metabolite to differentiate between axSpA and controls was C3M (AUC 0.95; specificity 92.0, sensitivity 83.4). C1M correlated with ASDAS-CRP in nr-axSpA (ρ = 0.37; p < 0.001) and AS (ρ = 0.57; p < 0.001). C1M, C3M, and C4M2 were associated with ASDAS-CRP in AS and nr-axSpA after adjustment for age, gender, and disease duration. Serum levels of collagen metabolites were significantly higher in AS and nr-axSpA than in controls. Moreover, the present study indicates that collagen metabolites reflect disease activity and are useful biomarkers of axSpA.

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 Schwann cells use a novel collagen-dependent mechanism for fibronectin fibril assembly

1998 ◽  
Vol 111 (18) ◽  
pp. 2763-2777 ◽  
Author(s):  
M.A. Chernousov ◽  
R.C. Stahl ◽  
D.J. Carey
Keyword(s):  
Extracellular Matrix ◽  
Schwann Cells ◽  
Collagen Type ◽  
Collagen Type I ◽  
Collagen Type Iv ◽  
Type I ◽  
Type Iv ◽  
The Matrix ◽  
Fibronectin Fibrils ◽  
Dependent Mechanism

Cultured rat Schwann cells were stimulated to deposit fibrillar extracellular matrix by treatment with ascorbic acid in the absence of nerve cells. Immunofluoresence staining of the matrix showed that it contains collagens types I and IV, fibronectin and perlecan but not laminin. Collagen type IV, fibronectin and perlecan co-distributed completely in the matrix fibrils, whereas collagen type I was present in only a subset of these fibrils. Time course studies indicated that collagen type I fibrils appear at late stages of matrix formation. Digestion of Schwann cell extracellular matrix with collagenase effectively disrupted most of the matrix including fibronectin fibrils. This was in contrast with fibroblasts, where collagenase treatment removed collagen with no visible effect on fibronectin fibrils. alpha5 integrin was expressed on the cell surface of Schwann cells and partially codistributed with fibronectin-containing fibrils. This suggests that the inability of Schwann cells to deposit fibronectin-containing matrix through a conventional, collagen-independent mechanism was not due to the lack of fibronectin-binding integrins on their cell surface. Polyclonal anti-fibronectin antibodies inhibited the deposition of fibronectin into the matrix fibrils, whereas collagen type IV fibrils were generally unaffected. Growth of Schwann cells on collagen type IV-coated substrate in the absence of ascorbate induced deposition of fine fibronectin fibrils. These results suggest that Schwann cells use an apparently novel, collagen type IV-dependent mechanism for the deposition of fibronectin into their extracellular matrix.

Sign in / Sign up

Export Citation Format

Share Document