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Esterification reactions in the biosynthesis of tropane alkaloids in transformed root cultures (1994)

Robins, Richard J ; Bachmann, Peter ; Peerless, Abigael C J ; [et al.]

Springer

Plant cell, tissue and organ culture 38 (1994), S. 241-247

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ISSN: 1573-5044

Keywords: Acryl-coenzyme A transferase ; biosynthesis ; coenzyme A thioester ; Datura ; pseudotropine ; transformed root cultures ; tropane alkaloids ; tropine

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Transformed root cultures of Datura stramonium and of related species contain both aliphatic and aromatic tropane esters. It has been shown that these esters are produced by the action of several acyl transferases that transfer the acidic moiety to tropan-3α-ol (tropine) or tropan-3β-ol (pseudotropine) from various acyl-coenzyme A thioesters. The presence of these enzymes has been examined in a range of tropane-alkaloid-producing and non-tropane-alkaloid-producing species. Activities that esterify tropine appear to be confined to species that accumulate tropane alkaloids, whereas a number of species that do not accumulate tropane alkaloids possess some ability to esterify pseudotropine. The present state of knowledge of these enzymes is reviewed. One of these activities, tigloyl-Coenzyme A:pseudotropine acyl transferase, has been purified to near homogeneity and the properties of this enzyme are summarized.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00033883

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Laminin inhibits human keratinocyte migration (1988)

Woodley, David T. ; Bachmann, Peter M. ; O'Keefe, Edward J.

New York, NY [u.a.] : Wiley-Blackwell

Journal of Cellular Physiology 136 (1988), S. 140-146

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ISSN: 0021-9541

Keywords: Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: A quantitative migration assay for human keratinocytes was developed to assess the influence of extracellular matrix molecules on cell motility independently from their effect on cell proliferation. Fibronectin and collagen types I and IV markedly promoted keratinocyte migration, but albumin, type V collagen, and heparan sulfate proteoglycan had little effect. In contrast, laminin inhibited keratinocyte motility and dramatically reduced type IV collagen-induced migration in a concentration-dependent manner. Laminin was not toxic, since it had no apparent effect on morphology, growth, or ability of cells to be passaged. Laminin, a major component of the lamina lucida, may inhibit motility of keratinocytes in vivo. Absence of contact with laminin, which accompanies wounding, may facilitate motility and healing in the epidermis.

Additional Material: 7 Ill.