PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Collagen Type III”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1975

Isolation and characterization of pepsin-treated type III collagen from calf skin.

Calf skin collagen was solubilized by incubating acid-extracted calf skin with pepsin at pH 2.0 and 25 degrees C, conditions that did not cause degradation of the triple helical region of collagen. Type III collagen was separated from type I collagen by differential salt precipitation at pH 7.5. The isolated type III collagen contained mainly gamma and higher molecular weight components cross-linked by reducible and/or non-reducible bonds. The isolated alpha1 (III) chains had an amino acid composition characteristic of type III collagen. Denatured but unreduced type III collagen, chromatographed on carboxymethyl-cellulose, eluted in the alpha 2 region, while after reduction and alkylation the alpha1 (III) chains eluted between the positions of alpha1 (I) and alpha2. The mid-point melting temperature temperature (tm) of type III collagen (35.1 degrees C) in a citrate buffer at pH 3.7 was somewhat lower than that of type I collagen (35.9 degrees C). Renaturation experiments at 25 degrees C showed that denatured type III collagen molecules with intact intramolecular disulfide bridges (gamma components) reform the triple helical structure of collagen much faster than reduced and carboxymethylated alpha1 (III) chains.

Amino Acids↗
PubMed1979

Do Schwann cells produce collagen type III?

The fact that collagen from both normal nerve endoneurium and Schwann cell tumours present characteristics of collagen type III, suggests that Schwann cells produce this type of collagen.

Animals↗
PubMed1976

Production and specificity of antibodies against the aminoterminal region in type III collagen.

A cross-linked fragment (peptide T1X) with a molecular weight of 13,000 could be isolated from a tryptic digest of insoluble type III collagen of calf skin. Peptide T1X was conjugated on to bovine serum albumin by glutaraldehyde and used for immunization of rabbits. The antisera reacted in passive haemagglutination and radioimmune assay with peptide T1X, type III collagen and its constituent alpha1(III) chain. Little or no reaction was observed with type I collagen and alpha1(I) chain. While rabbit antisera to neutral salt-soluble type III Collagen also showed a strong binding for 125I-labelled peptide T1X much less reaction was observed with antisera to type I collagen. The antigenicity of type III collagen was largely destroyed by pepsin treatment suggesting that it resided in non-helical segments. A fragment of peptide T1X produced by digestion with collagenase retained antigenic activity. The data indicated that the aminoterminal region of type III collagen contains strong antigenic determinants located in a non-helical sequence of about sixteen amino acids. Antibodies to these antigenic determinants were purified and rendered specific for type III collagen by immunoadsorption. The antibodies stained in indirect immunofluorescence tests particularly those regions in various connective tissues which are rich in reticulin fibres. Different staining patterns were observed with antibodies to type I collagen.

Antibodies↗
PubMed1979

Metabolism of rabbit skin collagen. Differences in the apparent turnover rates of type-I- and type-III-collagen precursors determined by constant intravenous infusion of labelled amino acids.

Growing rabbits were infused for up to 10 h with labelled proline, tyrosine and leucine to achieve plateau conditions within body free pools, for [3H]proline infusion, blood free-proline specific radioactivity remained constant after about 1 h. For individual animals, type-I- and type-III-collagen precursors were isolated by precipitation with (NH4)2SO4 and DEAE-cellulose chromatography. Experiments where 3H- and 14C-labelled proline and tyrosine were infused concurrently for different periods of time showed that type I procollagen reached plateau specific radioactivity within 3 h and 90% of the plateau value after 2 h infusion, corresponding to a calculated apparent t 1/2 of less than 26 min. Plateau values for type I procollagen were taken as precursor amino acid pool specific radioactivities. The type-III-collagen-precursor fractions consistently showed lower rates of label incorporation and, by assuming that both type I and type III collagens are synthesized from the same amino acid pools, kinetic analysis revealed an apparent t 1/2 for the isolated type-III-collagen precursors of 3.9 h. For proline, there were large variations between animals in the ratio between the precursor pool for collagen synthesis and the skin homogenate free pool (0.31 +/- 0.13, mean +/- S.D.), so that collagen-synthesis rates based solely on total tissue free-pool values for proline are subject to large and inconsistent errors.

Amino Acids↗
PubMed1977

Granulocyte collagenase: selective digestion of type I relative to type III collagen.

Collagenases produced by human polymorphonuclear leukocytes, human lung fibroblasts, and rabbit pulmonary alveolar macrophages were compared in their ability to digest soluble native type I and type III collagens. While the fibroblast and macrophage collagenases attacked the two substrates at approximately equal rates, the leukocyte collagenase attacked type I collagen preferentially (15:1) in comparison to type III collagen. This was true with human or rabbit collagen substrates. Thus, proteolysis of collagen, particularly in acute inflammation, may have a significant role in controlling the types of collagen present in connective tissue.

Animals↗
PubMed1975

Type III collagen: A major constituent of rheumatoid and normal human synovial membrane.

The findings establish that type III collagen is a major constituent of grossly proliferated rheumatoid and normal synovium. Unlike the collagen of normal synovium most of that in rheumatoid tissue could be solubilised by pepsin at 4 degrees C. Moore than half the pepsin-solubilised collage was identified as type III, the remainder being type I, by CM-cellulose chromatography; SDS-polyacrylamide electrophoresis with and without reduction of disulphide bonds; and amino acid analysis. Moreover, at least half the total collagen in several samples of normal as well as rheumatoid tissue was clearly type III when cyanogen bromide-derived peptides were run on SDS-polyacrylamide electrophoresis and compared with peptides prepared from purified types I and III collagens. This conclusion was supported by the isolation on phosphocellulose and quantitation by amino acid analysis of the collagen peptides alpha(1)CB2 and alpha(III)CB2 from a cyanogen bromide digest of rheumatoid synovium.

Amino Acids↗
PubMed1977

The characterization of type I and type III collagens from human peripheral nerve.

The normal chemical features of peripheral nerve collagens were determined on postmortem, histologically normal adult human femoral nerve. 1. Genetically distinct type I, [alpha1(I)2]alpha2, and type III, [alpha1(III)]3, were isolated by differential salt precipitation and the component subunit chains, alphal(I), alpha2 and alphal(III) were obtained by ion-exchange chromatography and gel filtration. 2. The molecular weight of alphal(I) and alpha2 of type I collagen was 95 000 and that for type III was 280 000. Reduction of type III with dithiothreitol yielded expected alpha1(III) chains of 95 000 molecular weight. 3. The amino acid composition of the three collagen chains, alpha1(I), alpha2, and alpha1(III), was the same as previously reported values for the corresponding chains from human skin except for slightly elevated hydroxylysine content. 4. Peripheral nerve collagen was found to contain 81% type I collagen and 19% type III. These results indicate that peripheral nerve collagen characteristics closely simulate that of human skin and differ from that of human aorta and other parenchymal organs. These data will permit a chemical analysis for possible abnormalities of peripheral nerve collagen in various neurogenic disorders.

Aged↗
PubMed1977

Ordering of cyanogen bromide peptides of type III collagen based on their homology to type I collagen: preservation of sites for crosslink formation during evolution.

The order of the cyanogen-bromide-derived peptides from alpha 1 (III) chains of pepsin-solubilized calf skin collagen was found to be 3A-3B-3C-7-6-1,8,2-4-5-9A-9B. The amino-acid sequences of the NH2-terminal region of all peptides were determined by Edman's automated degradation procedure. The alignment of the peptides along the peptide chain was established by searching for the best homology between the partial sequences of the cyanogen bromide peptides from the alpha 1 (III) chain and the completely known sequence of the alpha 1 (I) chain. Characterization of three cyanogen-bromide-derived double peptides provided confirmation of the deduced order. A sequence Gly-Met-Hyl-Gly-His-Arg-Gly-Phe- was established near the NH2-terminus and a sequence Gly-Ile-Hyl-Gly-His-Arg-Gly-Phe near the COOH-terminus of the alpha 1(III) chain. Identical sequences have been found in the corresponding regions of the alph 1(I) chain. They include hydroxylysine, a site for intermolecular crosslink formation. Because these sequences are conserved during evolution of the collagen molecule, they are probably important for collagen structure and function.

Amino Acid Sequence↗
PubMed1978

Cleavage of native type III collagen in the collagenase susceptible region by thermolysin.

Viscometric assays were used to demonstrate the activity of thermolysin (EC 3.4.24.4) on native type III collagen in solution. Analysis of the reaction products by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and electron microscopic visualisation of segment long spacing aggregates demonstrated localised cleavage of the collagen in the collagenase susceptible region.

Collagen↗
PubMed1977

Dermal architecture and collagen type distribution.

The human dermis consists of two morphologically different layers. A loose meshwork of thin collagenous fibres is characteristic for the adventitial dermis with includes the papillary and the periadnexal dermis. Thick, coarse collagen bundles are the main feature of the reticular dermis. Two different collagens, type I and type III occur in the dermis as shown previously by biochemical analyses. Antibodies specific for type I collagen or type III collagen and their corresponding precursors were used in indirect immunofluorescence tests to localize the various collagens in frozen sections of normal adult skin. Whereas type I collagen is found in all dermal layers, the main part of type III collagen can be found within the adventitial dermis. Antibodies against the precursor of type I collagen stain only a bandlike region immediately beneath the epidermis. Antibodies against the precursor of type III collagen stain the same regions as antibodies against the helical part of type III collagen.

Antibodies↗
PubMed1976

Light microscopic distinction between elastin, pseudo-elastica (type III collagen?) AND INTERSTITIAL COLLAGEN.

Distinction between elastin and collagen in arteriosclerotic lesions is difficult because the so-called elastica stains are bound also by collagen fibers which resemble collagen of premature infants. Investigations of effects of organic solvents on dye binding led to the development of methods for selective demonstration of pseudo-elastica, and for simultaneous visualization of elastin and pseudo-elastica in contrasting colors. Paraffin sections of human autopsy material were stained with solutions of resorcin-fuchsin, orcein or aldehyde fuchsin in absolute ethanol. In other series, sections pretreated with this resorcin-fuchsin solution were counter-stained with tannic acid-phosphomolybdic acid (TP)-dye technics. Solutions of these "elastica stains" in absolute ethanol colored only pseudo-elastica; elastin, e.g. elastic membranes of aorta, remained unstained. In sections counterstained with TP-dye technics elastin was colored red; pseudo-elastica retained the purplish blue coloration imparted by resorcin-fuchsin. Other collagens were stained yellow. A review of the literature showed that until the 1920's elastin was classified as a gelatinoid of the collagen group. Elastic fibers were identified by mechanical properties, not a particular chemical composition. Hence, the elastic fibers of classical histology cannot be equated with the elastin of modern chemistry. Correlation of histochemical observations with chemical data indicates that the collagenous pseudo-elastica corresponds to [alpha1(III)]3 collagen.

Adult↗