Production and characterization of monoclonal antibodies recognizing head activator in precursor form and immunocytochemical localization of head activator precursor and head activator peptide in the neural cell line NH15-CA2 and in hydra

Schawaller, Manfred; Schenck, Klaus; Hoffmeister, S. A. H.; Schaller, Heinz

doi:10.1111/j.1432-0436.1988.tb00209.x

Cited by 8 publications

(5 citation statements)

References 17 publications

(20 reference statements)

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“…The hydra LBP cDNA was obtained repeatedly by immunoscreening with monoclonal antibodies which recognize two main proteins in hydra: a 33-kDa protein which is associated with filamentous actin and occurs mainly in the muscular processes of epithelial cells (Keppel and Schaller 1991), and a 43-kDa protein mainly located in interstitial cells and in regions of high growth potential such as outgrowing buds (Schawaller et al 1988). The hydra LBP cDNA codes for a protein with a calculated molecular mass of 33 kDa.…”

Section: Discussionmentioning

confidence: 99%

“…The monoclonal IgM antibodies E21, B74, and V were originally produced against head activator-containing conjugates (Schawaller et al 1988). …”

Section: Other Antibodiesmentioning

confidence: 99%

“…Incubation with antibodies and visualization followed the same procedure as described by Schawaller et al (1988) and Keppel and Schaller (1991).…”

Section: Immunocytochemistrymentioning

confidence: 99%

“…In hydra, filamentous actin and the associated V immunoreactivity are most strongly expressed in muscular processes of ecto-and endodermal epithelial cells, including nondividing, terminally differentiated epithelial cells of the tentacles and the foot (Keppel and Schaller 1991;Schawaller et al 1988). …”

Section: Introductionmentioning

confidence: 99%

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Expression and characterization of the ”laminin binding protein" in hydra

Keppel

Fenger

Schaller

1997

Cell and Tissue Research

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Recently, a cDNA was isolated from hydra with extensive homology to a mammalian and invertebrate gene which codes for a protein called laminin binding protein (LBP). In this paper we describe the protein expression of the hydra LBP in Escherichia coli. On SDS gels the recombinant hydra LBP displayed an apparent molecular mass of 43 kDa, although the calculated mass, including six additional histidines, is 33.7 kDa. Polyclonal antibodies were produced against the hydra recombinant LBP. The antiserum reacted with a 42-kDa and a 43-kDa protein from Hydra vulgaris and from a multiheaded mutant of Chlorohydra viridissima, respectively. In hydra, LBP RNA and protein were highly expressed in cells with short cell cycles, such as all cells of the interstitial cell lineage, less in slowly cycling epithelial cells, and at very reduced levels or not at all in differentiated cells. Higher expression in the multiheaded mutant of C. viridissima than in H. vulgaris, the cells of which differ in doubling time, hint at a function in cell proliferation. This is supported by the finding that in vitro hydra LBP is a substrate for the cell-cycle-specific kinase CDC2.

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Section: Discussionmentioning

confidence: 99%

“…The monoclonal IgM antibodies E21, B74, and V were originally produced against head activator-containing conjugates (Schawaller et al 1988). …”

Section: Other Antibodiesmentioning

confidence: 99%

“…Incubation with antibodies and visualization followed the same procedure as described by Schawaller et al (1988) and Keppel and Schaller (1991).…”

Section: Immunocytochemistrymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Expression and characterization of the ”laminin binding protein" in hydra

Keppel

Fenger

Schaller

1997

Cell and Tissue Research

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“…The monoclonal antibody B74 was produced against a mixture of HA conjugates, but was very similar in its properties to E2 1. The characterization of these antibodies is described in Schaller et al (1984) and in Schawaller et al (1988). The HA anti-idiotypic antiserum 64 was produced against the monoclonal IgM HA antibody B74.…”

Section: Ha Antiseramentioning

confidence: 99%

Head activator acts as an autocrine growth factor for NH15-CA2 cells in the G2/mitosis transition.

Schaller¹,

Druffel-Augustin²,

Dübel³

1989

The EMBO Journal

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Developmental Signaling in Hydra: What Does It Take to Build a “Simple” Animal?

Steele

2002

Developmental Biology

128

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Developmental processes in multicellular animals depend on an array of signal transduction pathways. Studies of model organisms have identified a number of such pathways and dissected them in detail. However, these model organisms are all bilaterians. Investigations of the roles of signal transduction pathways in the early-diverging metazoan Hydra have revealed that a number of the well-known developmental signaling pathways were already in place in the last common ancestor of Hydra and bilaterians. In addition to these shared pathways, it appears that developmental processes in Hydra make use of pathways involving a variety of peptides. Such pathways have not yet been identified as developmental regulators in more recently diverged animals. In this review I will summarize work to date on developmental signaling pathways in Hydra and discuss the future directions in which such work will need to proceed to realize the potential that lies in this simple animal.

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Production and characterization of monoclonal antibodies recognizing head activator in precursor form and immunocytochemical localization of head activator precursor and head activator peptide in the neural cell line NH15-CA2 and in hydra

Cited by 8 publications

References 17 publications

Expression and characterization of the ”laminin binding protein" in hydra

Expression and characterization of the ”laminin binding protein" in hydra

Head activator acts as an autocrine growth factor for NH15-CA2 cells in the G2/mitosis transition.

Developmental Signaling in Hydra: What Does It Take to Build a “Simple” Animal?

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