scholarly journals Inhibition of Collagen-Induced Platelet Aggregation by Antibodies to Distinct Types of Collagen

1977 ◽  
Author(s):  
L. Balleisen ◽  
R. Timpl ◽  
S. Gay
Keyword(s):  
Platelet Aggregation ◽  
Serum Albumin ◽  
Type I Collagen ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Fibrillar Collagen ◽  
Type Ii ◽  
Molecular Parameters ◽  
Inhibition Reaction

The reaction of platelets with fibrillar collagen was measured by recording aggregation according to Borns method and by retraction of Ancrod-fibrin clots. These reactions could be completely inhibited by coating the fibrils with stoichiometric amounts of purified antibodies to type I, II or III collagens. The inhibition was specific, i. e. antibodies to type I collagen prevented aggregation by type I collagen but not by type II or III collagen. Comparable amounts ofantibodies to fibrinogen or to serum albumin had no effect on the reaction. The data indicate that platelet aggregation by type I or II collagen fibrils is not due to contamination with type III collagen. The inhibition reaction may be useful for further studies on molecular parameters of the interaction between platelets and collagen fibers.

scholarly journals Methylated Type I Collagen as a New Tool for Platelet Function Tests

1977 ◽  
Author(s):  
L. Balleisen ◽  
K. Kühn ◽  
R. Marx
Keyword(s):  
Platelet Aggregation ◽  
Platelet Adhesion ◽  
Type I Collagen ◽  
Type I ◽  
Fibrillar Collagen ◽  
Platelet Function Tests ◽  
Carboxylic Groups ◽  
Pre Treatment ◽  
Aggregation Activity ◽  
One Year

Methylated type I collagen with blocked carboxylic groups was used for testing platelet aggregation and adhesion on collagen, andas thrombogenic substance in experimental animals. This modified collagen is soluble in buffers at neutral pH, but when added to plasma immediately precipitates. Its platelet aggregation activity as tested by the inhibitory action of ASS and by the depression or absence of collagen induced platelet aggregation in uremia and thrombasthenia was comparable to fibrillar collagen. Preincubation of platelets with Antimycin A and 2-Deoxyglucose also inhibited platelet aggregation by meth. collagen. In a new test for measuring platelet adhesion on collagen, platelets and meth. collagen were rotated in a silastic tube; the decrease of platelets was determined. Furthermore, meth. collagen can be used as a thrombogenic substance in rabbits: The recorded decrease of platelets after injection of meth. collagen can be inhibited by pre-treatment with ASS. Summarizing, meth. collagen, which can be stored over one year in lyophilised or frozen form without a decrease of activity, is a substance with the biochemical characteristics of collagen, which allows handling as a dissolved collagen but behaves like a fibrillar collagen.

Platelet Uptake On Bioprosthetic Heart Valves

1981 ◽  
Author(s):  
C Oyama ◽  
S Klein ◽  
D J Magilligan
Keyword(s):  
Heart Valves ◽  
Type I Collagen ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Primary Role ◽  
Standard Size ◽  
Consistent Finding ◽  
Bioprosthetic Heart Valves ◽  
Platelet Adherence

Single and aggregated platelets have been a consistent finding on the surface of 28 degenerated porcine bioprosthetic heart valves. Both the degenerated valves as well as unimplanted commercially available valves exhibit loss of endocardium with bare collagen fibers on scanning electron microscopy. The role of platelet adherence to the collagen fibers of these glutaraldehyde treated bioprostheses in causing degeneration is an unanswered question. Platelet adherence to porcine (P) valve (Type III collagen) and bovine (B) pericardium (Type I collagen) was measured in the glutaraldehyde treated bioprosthesis and in the fresh state with saline (F, S) and with plasma (F, P). Single cusps or similar samples of pericardium were rotated at 200 RPM for 10 min in a concentration of human platelets tagged with 51Cr. The tissue was trimmed to standard size, counted in a gamma counter and adherence calculated as platelets (pits)/mm2.Our experimental observations did not show a difference in platelet adherence between porcine or bovine tissue either G-treated or F. The G-treated valves showed significantly less (p=<.01) adherence than the F tissue. Although G- treated bioprostheses have collagen fibers exposed to circulating blood, platelet collagen reaction probably does not play a primary role in degeneration of the bioprosthetic heart valve.

scholarly journals Analysis of collagen types synthesized by rabbit ear cartilage chondrocytes in vivo and in vitro

1984 ◽  
Vol 221 (1) ◽  
pp. 189-196 ◽  
Author(s):  
K Madsen ◽  
K von der Mark ◽  
M van Menxel ◽  
U Friberg
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Type Ii Collagen ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Ii ◽  
Collagen Types ◽  
Rabbit Ear ◽  
Ear Cartilage

This study compares the collagen types present in rabbit ear cartilage with those synthesized by dissociated chondrocytes in cell culture. The cartilage was first extracted with 4M-guanidinium chloride to remove proteoglycans. This step also extracted type I collagen. After pepsin solubilization of the residue, three additional, genetically distinct collagen types could be separated by fractional salt precipitation. On SDS (sodium dodecyl sulphate)/polyacrylamide-gel electrophoresis they were identified as type II collagen, (1 alpha, 2 alpha, 3 alpha) collagen and M-collagen fragments, a collagen pattern identical with that found in hyaline cartilage. Types I, II, (1 alpha, 2 alpha, 3 alpha) and M-collagen fragments represent 20, 75, 3.5, and 1% respectively of the total collagen. In frozen sections of ear cartilage, type II collagen was located by immunofluorescence staining in the extracellular matrix, whereas type I collagen was closely associated with the chondrocytes. Within 24h after release from elastic cartilage by enzymic digestion, auricular chondrocytes began to synthesize type III collagen, in addition to the above-mentioned collagens. This was shown after labelling of freshly dissociated chondrocytes with [3H]proline 1 day after plating, fractionation of the pepsin-treated collagens from medium and cell layer by NaCl precipitation, and analysis of the fractions by CM(carboxymethyl)-cellulose chromatography and SDS/polyacrylamide-gel electrophoresis. The 0.8 M-NaCl precipitate of cell-layer extracts consisted predominantly of type II collagen. The 0.8 M-NaCl precipitate obtained from the medium contained type I, II, and III collagen. In the supernatant of the 0.8 M-NaCl precipitation remained, both in the cell extract and medium, predominantly 1 alpha-, 2 alpha-, and 3 alpha-chains and M-collagen fragments. These results indicate that auricular chondrocytes are similar to chondrocytes from hyaline cartilage in that they produce, with the exception of type I collagen, the same collagen types in vivo, but change their cellular phenotype more rapidly after transfer to monolayer culture, as indicated by the prompt onset of type III collagen synthesis.

scholarly journals Collagen immunotyping in human liver: light and electron microscope study.

1980 ◽  
Vol 28 (11) ◽  
pp. 1145-1156 ◽  
Author(s):  
J A Grimaud ◽  
M Druguet ◽  
S Peyrol ◽  
O Chevalier ◽  
D Herbage ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Fibers ◽  
Immunofluorescent Staining ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Type Iv ◽  
Matrix Organization ◽  
Human Livers ◽  
Type Ab

Types I, III, IV, and AB collagens have been extracted from human cirrhotic livers and specific antibodies have been raised in rabbits and purified. Histological immunofluorescent staining of collagen types in normal and fibrotic human livers reveals the respective distribution of the various collagens among the hepatic connective matrix and the modification of the normal pattern in fibrosis: types I and III appear to be the main components of the fibrotic connective matrix in enlarged portal spaces and of the Dissian reticulin framework; type IV collagen deposits are thickened around portal vessels and ducts and outline lobular capillarized sinusoids; type AB collagen appears as thin punctual deposits in portal and Dissian fibrotic connective matrix. Ultrastructural immunoperoxidase labeling of type I and III collagen makes it possible to identify the typical collagen fibers, using 65 nm periodicity, as type I collagen and the fibrillar associated network as type III collagen. Fibers of type I collagen are preferentially organized in large dense bundles in Dense Connective Matrix Organization (DCMO), since fibrillar type III collagen network is predominant in Loose Connective Matrix Organization (LCMO) surrounding vascular and biliary tracts.

scholarly journals The effects of posterior cruciate ligament rupture on the biomechanical and histological characteristics of the medial collateral ligament: an animal study

2021 ◽  
Vol 16 (1) ◽  
Author(s):  
Wen-qing Xie ◽  
Miao He ◽  
Yu-qiong He ◽  
Deng-jie Yu ◽  
Hong-fu Jin ◽  
...  
Keyword(s):  
Posterior Cruciate Ligament ◽  
Medial Collateral Ligament ◽  
Type I Collagen ◽  
Cruciate Ligament ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Collateral Ligament ◽  
Intact Group ◽  
Significant Difference

Abstract Background To investigate the effect of complete rupture of the posterior cruciate ligament (PCL) on the biomechanics and histology of the medial collateral ligament (MCL). Materials and methods Seventy-two male rabbits were randomly divided into two groups: the ruptured group was treated with complete PCL amputation, while the intact group was only subjected to PCL exposure without amputation. Eighteen rabbits were randomly sacrificed at 8, 16, 24, and 40 weeks after the operation, and their specimens were processed for mechanical tensile testing, nano-indentation experiments, hematoxylin-eosin (HE) staining, and picrosirius-polarization staining. Results There was no significant difference in the length and maximum displacement of the MCL between the ruptured group and the intact group at each time point. The maximum load of the ruptured group was significantly smaller than that of the intact group at 40 W. The elastic modulus and micro-hardness of the ruptured group increased significantly at 24 W and decreased significantly at 40 W. At 16 W and 24 W after PCL rupture, the number of type I collagen fibers and type III collagen fibers in the MCL of the ruptured group was significantly increased compared with that of the intact group. While the type I collagen fibers of the ruptured group were significantly decreased compared with the intact group at 40 W, there was no significant difference in type III collagen fibers between the ruptured group and the intact group. Conclusion PCL rupture has no significant effect on the mechanical and histological properties of MCL in a short period of time under physiological loading, but the histological and mechanical properties of MCL decrease with time.

Binding of Collagen to Platelets

1975 ◽  
Author(s):  
R. M. Jaffe ◽  
D. Deykin
Keyword(s):  
Platelet Aggregation ◽  
Type Ii Collagen ◽  
Type I ◽  
Fibrillar Collagen ◽  
Type Ii ◽  
Binding Studies ◽  
Lysine Residues ◽  
Lag Period ◽  
Tritiated Amino Acids ◽  
Observation Period

Type I (chick calvaria) and Type II (chick cartilage) collagen were synthesized in organ culture on tritiated amino acids. The final, purified collagen has sp. act. > 106 DPM/mg. protein. 3H-Tropocollagen, from 5000–40,000 molecules per platelet, does not bind during a 15 minute observation period. Multimeric collagen, at the same dose, binds to platelets after a lag period of 90–120 sec. Fibrillar collagen will bind within 10 sec. Gelatin, prepared from this radiolabeled collagen, does not bind during the observation period. Similar results obtain for both Type I and Type II collagen.Aggregation and binding studies were carried out simultaneously. Tropocollagen does not initiate aggregation; multimeric collagen initiates aggregation after a lag of about 180 seconds; fibrillar collagen initiates aggregation with a lag of about 60 seconds. Gelatin does not initiate aggregation. Thus binding precedes aggregation by about 60 seconds. These observations are consistent with a quaternary requirement for platelet aggregation induced by collagen.Chemical modification of ॉ-amino groups of lysine residues in collagen was performed. Certain modifications inhibit fibrillogenesis and/or denature the protein. These modifications inhibit collagen-induced platelet aggregation. Permethylation of lysines in collagen does not impair fibrillogenesis, does not denature the protein and does not inhibit collagen-induced platelet aggregation.

Methionine-Specific Staining of Collagen

1982 ◽  
Vol 40 ◽  
pp. 294-295
Author(s):  
E.M. Kuhn ◽  
K.D. Marenus ◽  
M. Beer
Keyword(s):  
Amino Acids ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Electron Microscopic ◽  
Good Correspondence ◽  
Specific Staining ◽  
Type Iii ◽  
Different Types ◽  
Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

scholarly journals Intracellular and Extracellular Markers of Lethality in Osteogenesis Imperfecta: A Quantitative Proteomic Approach

2021 ◽  
Vol 22 (1) ◽  
pp. 429
Author(s):  
Luca Bini ◽  
Domitille Schvartz ◽  
Chiara Carnemolla ◽  
Roberta Besio ◽  
Nadia Garibaldi ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Type I ◽  
Tandem Mass ◽  
Type Ii ◽  
Type Iii ◽  
Bioinformatic Tools ◽  
Proteomic Approach ◽  
Fibrillin 1 ◽  
Heritable Disorder

Osteogenesis imperfecta (OI) is a heritable disorder that mainly affects the skeleton. The inheritance is mostly autosomal dominant and associated to mutations in one of the two genes, COL1A1 and COL1A2, encoding for the type I collagen α chains. According to more than 1500 described mutation sites and to outcome spanning from very mild cases to perinatal-lethality, OI is characterized by a wide genotype/phenotype heterogeneity. In order to identify common affected molecular-pathways and disease biomarkers in OI probands with different mutations and lethal or surviving phenotypes, primary fibroblasts from dominant OI patients, carrying COL1A1 or COL1A2 defects, were investigated by applying a Tandem Mass Tag labeling-Liquid Chromatography-Tandem Mass Spectrometry (TMT LC-MS/MS) proteomics approach and bioinformatic tools for comparative protein-abundance profiling. While no difference in α1 or α2 abundance was detected among lethal (type II) and not-lethal (type III) OI patients, 17 proteins, with key effects on matrix structure and organization, cell signaling, and cell and tissue development and differentiation, were significantly different between type II and type III OI patients. Among them, some non–collagenous extracellular matrix (ECM) proteins (e.g., decorin and fibrillin-1) and proteins modulating cytoskeleton (e.g., nestin and palladin) directly correlate to the severity of the disease. Their defective presence may define proband-failure in balancing aberrances related to mutant collagen.

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