scholarly journals Multiple antigenic determinants on type III collagen

1991 ◽  
Vol 274 (3) ◽  
pp. 895-898 ◽  
Author(s):  
J A Werkmeister ◽  
J A M Ramshaw
Keyword(s):  
Monoclonal Antibodies ◽  
Connective Tissue ◽  
Tryptic Digestion ◽  
Antigenic Determinants ◽  
Type Iii Collagen ◽  
Collagen Types ◽  
Type Iii ◽  
Wide Range

Eight monoclonal antibodies have been produced against human pepsin-soluble type III collagen. All antibodies were shown to be highly specific for type III collagen and did not cross-react with a range of other collagen types or connective-tissue proteins. Examination of type III collagen from other species showed that these antibodies had a wide range of species specificities, indicating that several distinct epitopes were being recognized. The location of the epitopes was investigated by using reactivity of the antibodies to CNBr fragments and to sequential fragments formed by tryptic digestion of renaturing type III collagen. These data also indicated that several distinct epitopes were recognized and that they were located over the length of the type III collagen.

scholarly journals Specific features of the adhesion process of the abdominal cavity in children with different degrees of connective tissue dysplasia

2020 ◽  
Vol 10 (4) ◽  
pp. 381-389
Author(s):  
Sergey V. Minaev ◽  
Sergey I. Timofeev ◽  
Alina N. Grigorova ◽  
Oksana V. Vladimirova ◽  
Elena I. Pashneva ◽  
...  
Keyword(s):  
Growth Factor ◽  
Connective Tissue ◽  
Clinical Course ◽  
Abdominal Cavity ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Connective Tissue Dysplasia ◽  
Group 2 ◽  
Group 1

Aim. To assess adhesions of the abdominal cavity in children with varying degrees of connective tissue dysplasia (CTD) severity. Methods. A total of 91 children with average age of 10.6 1.4 years were observed from 2005 to 2019. Composed of 53 boys (58.2%) and 38 girls (41.8%). Patients were divided into two groups: group 1 (69 children without CTD) and group 2 (22 children with CTD). Clinical data and screening cards were used to diagnose DST. All patients underwent an assessment for the clinical course, a macroscopic visual assessment adhesive process severity in the abdominal cavity according to three different scales (Nair, F. Coccolini, N.I. Ayushinova). Immunohistochemistry was performed against collagen I, III, IV type, Laminin 1, angiogenesis factors, transforming growth factor beta (TGF-), and Fibroblast Growth Factor Receptor 1 (FGFR1). A semi-quantitative counting method was used to record the relative number of immunopositive structures. Statistical analysis was carried out by methods of variation statistics using the Chi-square test and MannWhitney U-tests, as well as the Spearman rank correlation method for the reliability of differences between groups. Results. In the adhesive process visualization, the N.I. Ayushinov scale was revealed to be the most informative, showing the average score of 7 0.8 points in group 2 and 14 1.2 in group 1 (rs 0.35; p 0.05). In group 2, the adhesive material showed no (56%) or chaotic fragments (44%) of type I collagen, and the ratio of type I to type III collagen is 2.7: 5.1. In group 1, the ratio of type I to type III collagen is 5.9:1.8. The ratio of collagen IV to type I is 6.5: 2.9. Both groups have a moderate (++) amount of TGF-. TGF- is positive with macrophages. FGFR1 was found in the control group (++++). A positive response was seen in fibroblasts and macrophages (U = 79.00; p = 0.006). Statistically significant analyzes of vascular endothelial growth factor in compared groups (rs = 0.632, p 0.001) had a positive correlation.. Conclusion. Thus, the study showed features of clinical course and morphological changes during the development of adhesions in the abdominal cavity in children with varying degrees of severity of CTD. Data obtained dictate the need for an individual approach in predicting adhesive disease, as well as targeted preventive care.

Repeated helical epitopes of defined amino acid sequence in human type III collagen identified by monoclonal antibodies

1992 ◽  
Vol 29 (6) ◽  
pp. 759-770 ◽  
Author(s):  
Hori Hisae ◽  
Douglas R. Keene ◽  
Lynn Y. Sakai ◽  
Mary K. Wirtz ◽  
Hans Peter Bächinger ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Human Type

Re-visiting Luck’s classification: a histological analysis of Dupuytren’s disease

2010 ◽  
Vol 35 (4) ◽  
pp. 312-317 ◽  
Author(s):  
W. L. Lam ◽  
J. M. Rawlins ◽  
R. O. S. Karoo ◽  
I. Naylor ◽  
D. T. Sharpe
Keyword(s):  
Disease Progression ◽  
Staging System ◽  
Dupuytren’S Disease ◽  
Type Iii Collagen ◽  
Type I ◽  
Collagen Types ◽  
Dupuytren's Disease ◽  
Type Iii ◽  
Three Stages ◽  
Stage 1

Luck (1959) described a histological staging system for Dupuytren’s disease, classifying the disease into three stages. Previous biochemical and immunochemical studies have detailed the decrease in type III/I collagen ratio with disease progression. Herovici (1963) described a histological stain that produced a differential red/purple and blue colour for type I and III collagen respectively. We stained 15 specimens of Dupuytren’s disease and quantified the different collagen types in each using computer analysis. We found a corresponding decrease in the amount of type III collagen as a percentage of the total collagen with disease progression: stage I range 35–49% (mean 38%); stage 2 range 21–33% (mean 27%) and stage 3 range 11–19% (mean 14%). We propose a new staging system based on the relative amount of type III collagen, where stage 1: >35%, stage 2: >20% and <35%, and stage 3: <20%.

scholarly journals Biochemical characterization of individual normal, floppy and rheumatic human mitral valves

1987 ◽  
Vol 244 (3) ◽  
pp. 597-603 ◽  
Author(s):  
Y Lis ◽  
M C Burleigh ◽  
D J Parker ◽  
A H Child ◽  
J Hogg ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Mean Value ◽  
Type Iii Collagen ◽  
Collagen Types ◽  
Mitral Valves ◽  
Type Iii ◽  
Normal Human ◽  
Proteoglycan Content ◽  
Chronic Rheumatic Disease

Human mitral valves (32 floppy and 17 rheumatic) obtained at surgery were analysed and compared with 35 normal (autopsy) valves. Total amounts of collagen, proteoglycan and elastin were increased approx. 3-fold in floppy and rheumatic valves. The water content of rheumatic cusps was lower than normal. The most significant changes in floppy valves were the 59% increase in mean value of the proteoglycan content, a large increase in the ease of extractability of proteoglycans from 26.7 to 57.2% of the total and a 62% increase in mean value of the elastin content in the anterior cusps. Normal human mitral valve cusps contained a mean proportion of 29.3 (and chordae 26.6) type III collagen (as % of total types III + I collagen), the values increasing significantly to 33.2 and 36.3% respectively in chronic rheumatic disease. The ratio observed in floppy valves depended on the extent of secondary surface fibrosis, which could be demonstrated histologically; in valve cusps with considerable secondary fibrosis, the percentage of type III increased significantly (to 34.4%), whereas it decreased significantly (to 25.2%) when fibrosis was negligible. It is concluded that the ratio of collagen types in floppy valves reflects the extent of secondary fibrosis rather than the pathogenesis of the disrupted collagen in the central core of the valve.

Collagen types in fibrosarcoma: Absence of type III collagen in reticulin

1985 ◽  
Vol 16 (5) ◽  
pp. 439-446 ◽  
Author(s):  
Jackson Hall ◽  
Scheffer C.G. Tseng ◽  
Rubert Timpl ◽  
Mary J.C. Hendrix ◽  
Robert Stern
Keyword(s):  
Type Iii Collagen ◽  
Collagen Types ◽  
Type Iii

scholarly journals The use of monoclonal antibodies in virology

1982 ◽  
Vol 88 (3) ◽  
pp. 361-368 ◽  
Author(s):  
J. Oxford
Keyword(s):  
Monoclonal Antibodies ◽  
Antigenic Determinant ◽  
Laboratory Diagnosis ◽  
Antigenic Determinants ◽  
Subsequent Generation ◽  
Virus Structure ◽  
Wide Range

Antibodies have been used for the last five decades in the laboratory diagnosis of a wide range of diseases caused by viruses and in detailed investigations of virus structure. However, immunological and serological assays have always had problems of interpretation, reproducibility and standardization, resulting partly from the unavoidable heterogeneity of the antibodies in the test. When a mouse, for example, is immunized with a virus, the animal may easily recognise 10–20 different antigenic determinants. As many as five distinct antibodies can be produced by the mouse against each determinant and these will often differ from antibodies made by another mouse against the same antigenic determinant. The method of lymphocyte fusion and the subsequent generation of monoclonal antibodies (Kohler & Milstein, 1975; Kohler, 1980) overcomes these limitations.

scholarly journals Collagen heterogeneity and quantification in developing bovine nuchal ligament

1984 ◽  
Vol 220 (2) ◽  
pp. 385-394 ◽  
Author(s):  
C A Chambers ◽  
C A Shuttleworth ◽  
S Ayad ◽  
M E Grant
Keyword(s):  
Type I Collagen ◽  
Type Iii Collagen ◽  
Type I ◽  
Collagen Types ◽  
Constant Amount ◽  
Foetal Development ◽  
Type Iii ◽  
Major Species ◽  
Cnbr Cleavage ◽  
Nuchal Ligament

The collagenous components were investigated in peptic digests of developing bovine nuchal ligament. Types I and III collagen were the major species isolated, but the presence of types IV, V and VI was also shown. Changes in the pepsin-susceptibility of nuchal ligament during foetal development were observed. CNBr-cleavage peptide analysis indicated that type I collagen became cross-linked rapidly, as evidenced by the lack of alpha 1(I)CB6. At present it is not clear if this decrease in pepsin-susceptibility is due to cross-linking of collagen, to increased deposition of elastin, or to both. Quantification of collagen types I and III was shown to depend on the method used. When pepsin-solubilized material was examined an apparent increase in type III collagen with respect to foetal age was observed, whereas when CNBr digests of intact ligament were examined a relatively constant amount of type III collagen (approx. 24%) was found. The constant amount of type III collagen observed during foetal development changed at birth and increased in mature nuchal ligament to represent approx. 45% of the total collagen.

scholarly journals Protection of mice from experimental infection with type III group B Streptococcus using monoclonal antibodies.

1983 ◽  
Vol 158 (3) ◽  
pp. 1006-1011 ◽  
Author(s):  
M L Egan ◽  
D G Pritchard ◽  
H C Dillon ◽  
B M Gray
Keyword(s):  
Monoclonal Antibodies ◽  
Experimental Infection ◽  
Group B Streptococcus ◽  
Antigenic Determinants ◽  
Group B Streptococci ◽  
Lethal Challenge ◽  
Type Iii ◽  
Group B

Mouse hybridoma antibodies of several major classes against group B streptococcus type III have been produced. Mice were immunized with either whole heat-killed or acid-treated organisms to obtain antibodies against both the complete (sialated) or incomplete (nonsialated) forms of the type III polysaccharide. Resulting monoclonal antibodies showed exclusive specificity for either the complete or incomplete antigen. The ability of these antibodies to protect mice from a lethal challenge of live type III organisms was tested with a mucin model that permitted use of very small inocula given intraperitoneally with antibody and mucin. Antibodies specific for the nonsialated antigen were not protective, whether of IgM, IgG2a, or IgG3 isotypes. Antibodies specific for the complete antigen were, however, highly protective, including monoclonals of IgM, IgG2a, and IgA isotypes. These mouse monoclonal antibodies against group B streptococci that are directed against either complete or incomplete antigenic determinants, and include isotypes other than IgM, should be particularly useful for studying the mechanism of protection against experimental infection.

scholarly journals Specific immunohistochemical localization of osteonectin and collagen types I and III in fetal and adult porcine dental tissues.

1985 ◽  
Vol 33 (6) ◽  
pp. 531-540 ◽  
Author(s):  
P S Tung ◽  
C Domenicucci ◽  
S Wasi ◽  
J Sodek
Keyword(s):  
Periodontal Ligament ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Type Iii Collagen ◽  
Similar Distribution ◽  
Type I ◽  
Collagen Types ◽  
Type Iii ◽  
Dental Tissues ◽  
Strong Staining

Affinity-purified antibodies have been used in combination with the peroxidase-antiperoxidase technique to study the distribution of osteonectin and collagen types I and III in porcine dental tissues. Tissue sections (2 mm thick), including unerupted (fetal) or erupted (adult) teeth, were fixed in periodate-lysine-paraformaldehyde, demineralized in 12% w/v ethylenediaminetetraacetic acid, and after embedding, 6 micron sections were prepared for immunolocalization. Strong staining for osteonectin was observed in dentine of unerupted teeth and in the associated alveolar bone. Light to moderate staining was observed in the dental pulp, stratum intermedium, stellate reticulum, and the reticular elements in the endosteal spaces. In erupted teeth, osteonectin staining in dentine was concentrated around dentinal tubules and the associated alveolar bone stained with variable intensity. Cementum was poorly stained. However, the periodontal ligament and reticular material in the endosteal spaces showed moderate to strong staining. Weaker staining was apparent in the pulp and lamina propria of the gingiva. In comparison, type I collagen showed a similar distribution to osteonectin in both fetal and adult tissues, whereas type III collagen was generally restricted to the periodontal ligament, reticular elements of the endosteal spaces, and Sharpey's fibers in bone and cementum. Both odontoblast and ameloblast layers in fetal tissues stained for osteonectin and type III collagen.

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