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Biomedical subjects

E B McGoodwin

Publications and source records attributed to E B McGoodwin.

11 recordsLinked to original sources
PubMed1992

Chemical peritonitis following the intraperitoneal administration of vancomycin.

The Food and Drug Administration has received 51 reports of cases in the United States in which chemical peritonitis was associated with the intraperitoneal administration of sterile vancomycin hydrochloride, USP intravenous. The clinical presentation of the cases ranged from mild (cloudy dialysate alone) to more severe (severe abdominal pain and fever). The temporal circumstances suggest that intraperitoneal vancomycin may be associated with chemical peritonitis. A positive rechallenge was reported in 9 cases. The underlying mechanism responsible for this adverse reaction has not yet been identified.

Adverse Drug Reaction Reporting Systems↗
PubMed1978

Localization of the binding site for cell attachment in the alpha1(I) chain of collagen.

Certain cells such as CHO (Chinese hamster ovary) and fibroblasts attach to a substrate of type I collagen via proteins that link the cell surface to collagen. Serum contains a glycoprotein, c-CAP (collagen cell attachment protein), that can mediate this adhesion. Previously, we established that alpha1(I)-CB7 (cyanogen bromide peptide 7), which lies within residues 552 to 822 of collagen, contains a major binding site for c-CAP(alpha1(I)-CB7 has been renumbered to account for an additional triplet recently identified at residue 613 (P. P. Fietzek and R. W. Glanville, manuscript in preparation). Now we have examined the ability of various peptides derived by proteolytic digestion of alpha1(I)-CB7 to bind to c-CAP based upon their ability to inhibit cell attachment to collagen. The binding site lies within residues 757 to 791. It is likely that this is the sole binding site in the alpha1(I) chain since cleavage of the bond between residues 775 and 776 in the alpha1(I) chain destroys cell attachment activity.

Amino Acid Sequence↗
PubMed1978

Connective tissue structure: cell binding to collagen.

Established lines of fibroblasts have been shown to adhere to collagen substrates via a serum-derived glycoprotein. The attachment of various other cells to collagen types I-IV is examined here. Cells such as human skin fibroblasts, periosteum, hepatocytes, connective tissue cells, and monocytes required the serum glycoprotein and adhered equally well to all collagens, but attachment of chondrocytes, epidermal cells, and neutrophils was inhibited by the serum glycoprotein. Attachment of 2 tumorigenic cells, an osteosarcoma and a fibrosarcoma, was found to be unaffected by the serum glycoprotein. In addition, the fibrosarcoma and epidermal cells attached preferentially to type IV (basement membrane) collagen.

Animals↗
PubMed1977

Decreased lysyl oxidase activity in the aneurysm-prone, mottled mouse.

Inbred mice bearing certain alleles at the Mottled locus have defects in connective tissue which result in weakness of skin and of blood vessels. Previous studies have established that cross-links in collagen and elastin are decreased in these animals due to impaired formation of lysine-derived aldehydes. Lysyl oxidase activity in extracts of skin is markedly lower in those prepared from affected animals than control mice. An inhibitor of lysyl oxidase is present in equal amounts in affected and control skins and does not account for diminished activity found in affected animals.

Amino Acid Oxidoreductases↗
PubMed1977

A murine tumor producing a matrix of basement membrane.

We have studied a murine tumor previously classified as a poorly differentiated chondrosarcoma. Although the cells in this tumor are surrounded by large quantities of extracellular matrix material, the matrix fails to react with stains specific for the sulfated glycosaminoglycans present in normal cartilage. Here we show at the ultrastructural level that the tumor matrix is a homogeneous, nonfibrillar material, resembling basement membrane. Neither the proteoglycan matrix granules nor collagen fibrils characteristic of cartilage are present in the tumor matrix. Amino acid analyses of whole tumor tissue, enzyme-solubilized tumor components, and the protein extracted from lathyritic tumors confirmed that the tumor matrix is a basement membrane collagen. The collagenous protein extracted from the tumor by nonenzymatic means contains three unique polypeptides larger than the alpha-chain components of the other types of collagen. These studies indicate that the tumor is not a type of chondrosarcoma but a basement membrane producing tumor.

Amino Acids↗
PubMed1974

A sex-linked defect in the cross-linking of collagen and elastin associated with the mottled locus in mice.

A genetic abnormality in collagen and elastin cross-linking resembling experimental lathyrism has been identified in mice. The defect is an X-linked trait, attributed to the mottled locus which also influences coat color. The affected mice have aneurysms of the aorta and its branches, weak skin, and bone deformities in a spectrum of severity varying with the alleles at the mottled locus. A defect in the cross-linking of collagen was demonstrated in the skin of the affected animals by a marked increase in collagen extractability and a reduced proportion of cross-linked components in the extracted collagen. A decrease in lysine-derived aldehyde levels was found in both skin collagen and aortic elastin similar to that found in lathyritic tissue. Furthermore the in vitro formation of lysine-derived aldehyde was reduced. Thus the cause of the connective tissue abnormalities in these mice appears to be a defect in cross-link formation due to an impairment in aldehyde formation.

Animals↗
PubMed1971

The nature of the collagen synthesized by cultured human fibroblasts.

The hydroxyproline-containing proteins (hyproproteins) synthesized by cultured human fibroblasts have been partially characterized. The hyproprotein extracted from the cell layer was found to be similar to the collagen extracted from skin in the ratio of hydroxyproline to proline, chain composition, solubility, and resistance to proteolytic digestion.The hyproproteins isolated from the medium were different. About 20% of the peptide-bound hydroxyproline was found in randomly coiled chains. The alpha2 chains were present in considerable excess over the alpha1 chains, suggesting that the alpha2 chain may be synthesized in quantities greater than required to form a collagen molecule with a chain composition (alpha1)(2)alpha2. The remaining medium hyproprotein appeared to be an unusual form of native collagen which, unlike typical native collagen, was soluble under physiological conditions. This hyproprotein did not yield alpha chains when denatured and contained material that had a molecular weight greater than alpha chains. A similar size distribution was observed in the protein synthesized in the presence of beta-aminopropionitrile, a specific inhibitor of collagen cross-linking. After treatment with pepsin, typical alpha1 and alpha2 chains were obtained from the protein in a 2:1 ratio. Since the medium protein is soluble and has properties different from the typical collagen molecule, it may represent a modified form that functions in the transport of collagen from the cell to the fiber.

Aminopropionitrile↗