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Biomedical subjects

E J Miller

Publications and source records attributed to E J Miller.

At least 163 records · Page 9Linked to original sources
PubMed1975

Comparative electron-microscope studies on type-III and type-I collagens.

Long-spacing-segment crystallites prepared from type III collagen with the chain composition [alpha1(III)]3 and type I collagen with the chain composition [alpha(I)]i12alpha2 have been compared in the electron microscope after positive. staining with phosphotungstic acid and uranyl acetate. The comparison revealed several differences in intensities of the cross-striation bands as well as significant differences in band positions. The latter occur most prominently in three distinct regions of the crystallites. Further, crystallites prepared from type III collagen contain an additional intensely staining band in an area corresponding to the carboxy-terminal end of the molecule. The latter band is still observed following limited pepsin digestion and presumably represents a slight elongation of the helical portion of the type III molecule when compared to the type I molecule. In spite of the somewhat altered distribution of charged groups as indicated in studies on the long-spacing-segment crystallites, type III molecules are capable of forming fibrils of the native type with a cross-striation pattern and periodicity virtually identical to that observed when type I molecules are precipitated as native fibers.

Amino Acid Sequence↗
PubMed1975

Analysis of changes in collagen biosynthesis that occur when chick chondrocytes are grown in 5-bromo-2'-deoxyuridine.

Chick embryo chondrocytes, in primary culture, initially synthesize only Type ii collagen (chain composition, [alpha1(II)13), as judged by two criteria: (i) carbosymethyl-cellulose chromatography of the denatured collagen, and (ii) carbosymethyl-cellulose chromatography of the cyanogen bromide peptides derived from the isolated chains. After a period of growth in 5-bromo-2'-deoxyuridine, however, synthesis of two different types of collagen could be detected after differential salt precipitation of the newly synthesized native collagens from neutral salt solutions at 2.2 M NaCl and subsequently at 0.01 M Na2hPO4. By criteria indicated above, the collagen precipitating at 2.2 M NaCl was identified as Type I collagen (chain composition, [alpha(I)]2alpha2), whereas the collagen subsequently precipitated at 0.01 M Na2HPO4 was found to be comprised entirely of alpha1(I) chains, indicating a chain composition, [alpha](I)]3. We propose to designate the latter type of molecule as the Type I trimer.

Animals↗
PubMed1975

Presence of antibodies specific to cartilage-type collagen in rheumatoid synovial tissue.

Synovial membranes of rheumatoid arthritis patients were examined by fluorescence microscopy for the presence of cells producing different classes of immunoglobulins and for the incidence of antibodies to human collagens. IgG and IgM immunoglobulins were detected while IgA, IgD and IgE were absent. When consecutive tissue sections were incubated with tetramethylrhodamine isothiocyanate-labelled collagen preparations, prominent cellular and extra-cellular staining was observed only with cartilage-derived Type II collagen.

Antibody Specificity↗
PubMed1975

Demonstration of a unique antigenic specificity for the collagen alpha1 (II) chain from cartilaginous tissue.

The rabbit antibody response to native collagen (chain composition [alpha1(II)3) from cartilaginous tissue, has been examined by agglutination assays, gel diffusion, haemagglutination-inhibition studies, and immunoadsorption. The results show that the rabbit antibody response to the cartilage-type collagen is characterized by considerable reactivity to both helical [alpha1(II)]3 as well as alpha1(II) chains. This is in contrast to the rat antibody response to the same antigens where titres are generated to largely helical antigenic determinants. Similarly to the rat response, rabbit antibodies to [alpha(II)]3 exhibit no strong cross-reaction with the genetically distinct [alpha(I)]2ALPHA2 collagen or its component chains. Strong cross-reactions were, however, observed between bovine and chick alpha1(II) chains. One of the major antigenic sites on [alpha1(II)]3 collagen appears to reside in the sequence represented by CB-11, a peptide derived from the helical portion of the [alpha1(II)]3 molecule after cyanogen bromide cleavage. The data, however, are compatible with the presence of other antigenic determinants which are probably located in the amino- and carbocy-terminal portions of the molecule.

Agglutination Tests↗
PubMed1974

Lathyrism: a review.

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Abnormalities, Drug-Induced↗
PubMed1974

Collagen polymorphism: characterization of molecules with the chain composition (alpha 1 (3)03 in human tissues.

Collagen moleculess with the chain comizposition [alpha1(III)](3), have been isolated from pepsin-solubilized collagen of dermis, aorta, and leiomlyoma of the uterus by differential salt precipitation. On denaturation, approximately 90 percent of this collagen is recovered as a gamma component (300,000 daltons). Reduction and alkylation of the high-molecular-weight component yields alpha1(III) chains (95,000 daltons). In addition to containing cysteine, alpha1(III) chains exhibit several other compositional differences when compared to alpha1(I), alpha1(II), or alpha2 chains from human tissues.

Amino Acid Sequence↗