Herbert Zimmermann

Goethe University Frankfurt

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Walter Volknandt

Goethe University Frankfurt

Luı́sa V. Lopes

University of Lisbon

Matthias Schläfer

Goethe University Frankfurt

Christine Herrmann

Universität Ulm

Trevor W. Stone

University of Oxford

Eckart D. Gundelfinger

Leibniz Institute for Neurobiology

Lixia Zhang

Chinese Academy of Medical Sciences & Peking Union Medical College

Shuichi Kobayashi

Canon (Japan)

Marloes Schaddelee

Astellas Pharma (Netherlands)

David E. Millhorn

University of Cincinnati

Cooperative Institutions

Goethe University Frankfurt

University of California, Los Angeles

Universität Ulm

Technical University of Munich

University of Cincinnati

University of Cincinnati Medical Center

University of Lisbon

Instituto Politécnico da Guarda

Instituto de Medicina Molecular João Lobo Antunes

Weatherford College

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Chronic Hypoxia Enhances Adenosine Release in Rat PC12 Cells by Altering Adenosine Metabolism and Membrane Transport

Journal of Neurochemistry (2000)

Shuichi Kobayashi Herbert Zimmermann David E. Millhorn

Abstract: Acute exposure to hypoxia causes a release of adenosine (ADO) that is inversely related to the O 2 levels in oxygen‐sensitive pheochromocytoma (PC12) cells. In the current study, chronic exposure (48 h) of PC12 cells to moderate hypoxia (5% O 2 ) significantly enhanced the release of ADO during severe, acute hypoxia (1% O 2 ). Investigation into the intra‐ and extracellular mechanisms underpinning the secretion of ADO in PC12 cells chronically exposed to hypoxia revealed changes in gene expression and activities of several key enzymes associated with ADO production and metabolism, as well as the down‐regulation of a nucleoside transporter. Decreases in the enzymatic activities of ADO kinase and ADO deaminase accompanied by an increase in those of cytoplasmic and ecto‐5′‐nucleotidases bring about an increased capacity to produce intra‐ and extracellular ADO. This increased potential to generate ADO and decreased capacity to metabolize ADO indicate that PC12 cells shift toward an ADO producer phenotype during hypoxia. The reduced function of the rat equilibrative nucleoside transporter rENT 1 also plays a role in controlling extracellular ADO levels. The hypoxia‐induced alterations in the ADO metabolic enzymes and the rENT 1 transporter seem to increase the extracellular concentration of ADO. The biological significance of this regulation is unclear but is likely to be associated with modulating cellular activity during hypoxia.

Hypoxia

Nucleoside transporter

Adenosine kinase

10.1046/j.1471-4159.2000.740621.x

Cite

Citations (127)

Analysis of a cDNA encoding the major vault protein from the electric ray Discopyge ommata

Gene (1997)

Christine Herrmann Herbert Zimmermann Walter Volknandt

Vault (architecture)

Northern blot

Southern blot

10.1016/s0378-1119(96)00781-0

Cite

Citations (23)

Extracellular metabolism of ATP and other nucleotides

Naunyn-Schmiedeberg s Archives of Pharmacology (2000)

Herbert Zimmermann

Adenosine triphosphate

10.1007/s002100000309

Cite

Citations (974)

Putative Synaptic Vesicle Nucleotide Transporter Identified as Glyceraldehyde‐3‐Phosphate Dehydrogenase

Journal of Neurochemistry (1994)

Matthias Schläfer Walter Volknandt Herbert Zimmermann

Abstract: Synaptic vesicles isolated from electric ray electric organ have been shown previously to contain a 34‐kDa protein that binds azido‐ATP, azido‐AMP, and N ‐ethylmaleimide. The protein was found to share similarities with the mitochondrial ADP/ATP carrier and assumed to represent the synaptic vesicle nucleotide transporter. Synaptic vesicles were purified by sucrose density gradient centrifugation and subsequent chromatography on Sephacryl S‐1000 from both Torpedo electric organ and bovine brain cerebral cortex. They contained ATP‐binding proteins of 35 kDa and 34 kDa, respectively. ATP binding was inhibited by AMP. Both proteins were highly enriched after column chromatography of vesicle proteins of AMP‐Sepharose. Antibodies were obtained against both proteins. Antibodies against the bovine brain synaptic vesicle protein of 34 kDa bound specifically to the 35‐kDa protein of Torpedo vesicles. An N‐terminal sequence obtained against the 34‐kDa protein of bovine brain synaptic vesicles identified it as glyceraldehyde‐3‐phosphate dehydrogenase. The previously observed molecular characteristics of the putative vesicular nucleotide transporter in Torpedo fit those of glyceraldehyde‐3‐phosphate dehydrogenase. We, therefore, suggest that the protein previously identified as putative nucleotide transporter is, in fact, glyceraldehyde‐3‐phosphate dehydrogenase.

Glyceraldehyde 3-phosphate dehydrogenase

Vesicular Transport Proteins

10.1046/j.1471-4159.1994.63051924.x

Cite

Citations (26)

Purines in Portugal

Trends in Neurosciences (2001)

Trevor W. Stone Herbert Zimmermann Luı́sa V. Lopes Marloes Schaddelee

Allosteric modulator

Adenosine A1 receptor

10.1016/s0166-2236(00)01992-5

Cite