Notes onLaboulbenia stenolophi andLaboulbenia anoplogenii (Ascomycetes, Laboulbeniales)

Laboulbenia stenolophi is reported for the first time from Japan.Stenolophus iridicolor andS. propinquus are added as new hosts. The crowded antheridia and the protruding (bulging) cell IV are characteristic of this fungus, although thalli with an almost normal cell IV sometimes occur.Laboulbenia anoplogenii onAnoplogenius is easily distinguished from what has been calledL. anoplogenii onStenolophus, Astigis, Abacetus andChlaeminus by the following characters: 1) no crowded antheridia can be observed throughout thallus development, but many sterile long branches can be observed instead; 2) cell IV starts to undergo cell division early in thallus development; 3) cell V extends downward to the level of cell VII, rather than extending only as far as the perithecial basal cells; and 4) cell VI is usually longer and extends farther distally than cell III.Anoplogenius is the host genus ofL. anoplogenii and the records from other hosts represent misapplied names.     

Isolation of skeletal muscle collagen

A new method for the isolation of a high yield of collagen from human skeletal muscle is described. This technique employs rapid stirring of the homogenate of skeletal muscle with a magnetic stirrer. Fibrous material entangled during rapid stirring was recovered by passing the homogenate through a sieve and then sequentially extracted with Hasselbach-Schneider solution and 0.6 m KI-0.06 m Na₂S₂O₃. The insoluble residue obtained after these extractions was shown to be highly purified collagen by amino acid analysis, and the recovery of collagen by this method was found to be more than 90% of the total collagen in skeletal muscle. The isolated collagen from 5 years of age was mostly composed of Type I collagen, and small amounts of Type III collagen and an unidentified collagenous protein migrating in a position near Type V collagen (αB chain) were also found on a sodium dodecyl sulfate-polyacrylamide gel.     

Hepatic stellate cells (vitamin A-storing cells) change their cytoskeleton structure by extracellular matrix components through a signal transduction system

 When cultured on a polystyrene surface or aminoalkylsilane-coated cover glasses, rat and human hepatic stellate cells exhibit a flattened, fibroblast-like shape with well-developed stress fibers. However, culturing the cells on type I collagen gel results in the elongation of long, multipolar cellular processes, whereas cells cultured on Matrigel maintain their round shapes. Dual fluorescence staining of microtubules and fibrillar actin indicated that the processes extend together with collagen fibers and contained microtubules as the core, whereas the periphery contained fibrillar actin. Immunofluorescence staining of vinculin showed that the focal adhesions were distributed mainly in lamellipodia when cultured on aminoalkylsilane-coated cover glasses, whereas in the cells cultured on type I collagen gel they were localized to the tips of the processes and along their bottom surface contacting collagen fibers. Wortmannin, as well as staurosporin and herbimycin A, inhibited the elongation process and induced the retraction of elongated processes. The wortmannin treatment also resulted in an alteration in focal adhesion distribution from the processes to cell bodies. These results indicate that the cell surface integrin binding to interstitial collagen fibers induces the elongation of processes through signaling events and the subsequent cytoskeleton assembly in hepatic stellate cells. Accepted: 12 February 1998