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.

scholarly journals Characterization of Human Type III Collagen Expressed in a Baculovirus System

1996 ◽  
Vol 271 (20) ◽  
pp. 11988-11995 ◽  
Author(s):  
Arja Lamberg ◽  
Tarja Helaakoski ◽  
Johanna Myllyharju ◽  
Sirkku Peltonen ◽  
Holger Notbohm ◽  
...  
Keyword(s):  
Type Iii Collagen ◽  
Type Iii ◽  
Human Type ◽  
Baculovirus System

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 Erratum: Molecular and biochemical characterization of Tunisian patients with glycogen storage disease type III

2012 ◽  
Vol 57 (3) ◽  
pp. 221-221
Author(s):  
Amira Mili ◽  
Ilhem Ben Charfeddine ◽  
Ons Mama ◽  
Sonia Abdelhak ◽  
Labiba Adala ◽  
...  
Keyword(s):  
Glycogen Storage Disease ◽  
Storage Disease ◽  
Biochemical Characterization ◽  
Glycogen Storage Disease Type ◽  
Glycogen Storage ◽  
Disease Type ◽  
Type Iii ◽  
Tunisian Patients

scholarly journals Structural and Biochemical Characterization of SrcA, a Multi-Cargo Type III Secretion Chaperone in Salmonella Required for Pathogenic Association with a Host

2010 ◽  
Vol 6 (2) ◽  
pp. e1000751 ◽  
Author(s):  
Colin A. Cooper ◽  
Kun Zhang ◽  
Sara N. Andres ◽  
Yuan Fang ◽  
Natalia A. Kaniuk ◽  
...  
Keyword(s):  
Type Iii Secretion ◽  
Biochemical Characterization ◽  
Type Iii ◽  
Secretion Chaperone

scholarly journals Purification and partial biochemical characterization of normal human interleukin 1.

1984 ◽  
Vol 160 (3) ◽  
pp. 772-787 ◽  
Author(s):  
J A Schmidt
Keyword(s):  
High Performance ◽  
Biochemical Characterization ◽  
Interleukin 1 ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Size Exclusion ◽  
Thymocyte Proliferation ◽  
Exclusion Chromatography ◽  
Normal Human

A protocol for the rapid, efficient purification of the major charged species of human interleukin 1 (IL-1) has been developed using high performance anion exchange and size exclusion chromatography. The isolated material is pure as determined by sodium dodecyl sulfate (SDS) gradient polyacrylamide gel electrophoresis (PAGE) and analytical isoelectric focusing (IEF). The molecular weight of the purified material is 15,000 and the isoelectric point (pI) is 6.8, values that are in good agreement with those previously reported for human IL-1. 10(-10) M concentrations of the purified material give half-maximal stimulation in the thymocyte proliferation assay. Amounts of IL-1 sufficient for receptor studies and detailed biochemical analysis can now be produced on a regular basis.

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%.

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