Zhang, Xiaoming and Fei, Kaiyin and Agbas, Abdulbaki and Yan, Li and Zhang, Jinsong and O'Reilly, Brooke and Deutzmann, Rainer and Sarras, Michael P. (2002) Structure and function of an early divergent form of laminin in hydra: a structurally conserved ECM component that is essential for epithelial morphogenesis. DEVELOPMENT GENES AND EVOLUTION, 212 (4). pp. 159-172. ISSN 0949-944X
Full text not available from this repository. (Request a copy)Abstract
As a major component of the extracellular matrix (ECM), laminin has been found in many vertebrate and invertebrate organisms. Its molecular structure is very similar across species lines and its biological function in the ECM has been extensively studied. In an effort to study ECM structure and function in hydra, we have cloned a partial hydra laminin a chain and the full-length hydra laminin beta chain using ECM-enriched cDNA libraries. Analysis of deduced amino acid sequences indicated that both polypeptides have high sequence similarity to a number of invertebrate and vertebrate laminin alpha and beta subunits. Rotary shadow analysis of isolated hydra laminin indicates it has a heterotrimeric organization that is characteristic of vertebrate laminins. A putative integrin-class protein was also identified using a cell-binding peptide sequence from the laminin beta chain as an affinity probe, indicating that integrins are possible cell surface receptors in hydra. In agreement with previous results for the hydra laminin beta chain, in situ hybridization experiments revealed that hydra laminin alpha chain mRNA is restricted to endodermal cells. As with a number of other hydra ECM components, higher levels of laminin alpha chain mRNA are localized to regions where cell migration and differentiation are actively undertaken such as the base of tentacles, the peduncle region, buds, regenerating tentacles, and at the head end during regeneration. The role of laminin in morphogenesis was studied using an antisense approach and the results indicated that translation of the laminin alpha chain is required for head regeneration.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | EXTRACELLULAR-MATRIX MESOGLEA; HEAD REGENERATION; IV COLLAGEN; VULGARIS; FIBRONECTIN; EXPRESSION; DROSOPHILA; PROTEINS; CHAIN; METALLOPROTEINASE; hydra; morphogenesis; extracellular matrix; laminin; integrin |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I > Prof. Dr. Rainer Deutzmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 27 Oct 2021 04:37 |
| Last Modified: | 27 Oct 2021 04:37 |
| URI: | https://pred.uni-regensburg.de/id/eprint/40296 |
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