V

Gerke, Wolfgang

doi:10.1007/978-3-322-82631-2_22

Cited by 12 publications

(26 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The expression pro¢ling and an immunocytochemical analysis of mouse embryos employing the antibody described here [23] reveals that the protein appears to be restricted to certain types of tissues, in particular spleen and liver. Such a speci¢c expression pattern contrasts with that of most other annexins (for review see [2]) and argues for a rather specialized function of annexin A9.…”

Section: Expression Of the Annexin A9 Protein In Cultured Cellsmentioning

confidence: 98%

“…They typically provide carboxyl oxygens of an acidic residue and carbonyl oxygens of a nearby site in the backbone for Ca 2þ coordination and have a Ca 2þ a⁄nity which is at least an order of magnitude lower than that of canonical type II sites [10,24,25]. Type III sites have thus been considered irrelevant for intracellular activities of annexins although they might participate in regulating extracellular functions reported for some members of the annexin family (for review see [2,27]). Interestingly and in contrast to other type II site annexin mutants engineered recombinantly [24,25], annexin A9 bound to liposomes at the elevated Ca 2þ levels could not be released by chelating Ca 2þ with EGTA.…”

Section: Biochemical Characteristics Of Recombinantly Expressedmentioning

confidence: 99%

“…In conclusion, our data con¢rm that annexin A9 is an atypical member of the annexin family, since it is not capable of binding acidic phospholipids in the presence of submillimolar Ca 2þ concentrations. This suggests that the protein ful¢lls a rather special function which due to its low abundance and biochemical properties does not involve the providing of a membrane sca¡old proposed for other annexins (for review see [2]). High resolution structural studies have to reveal whether annexin A9 shares a common structural fold with other annexins with the core constituting an entity designed to interact with negatively charged macromolecular surfaces.…”

Section: Biochemical Characteristics Of Recombinantly Expressedmentioning

confidence: 99%

“…Annexins are a family of evolutionarily conserved proteins characterized by their ability to interact with membrane phospholipids in a Ca 2þ -dependent manner. This property most likely underlies annexin functions in membrane organization and tra⁄c and has been proposed to depend on so-called type II Ca 2þ binding sites found in annexin proteins (for recent reviews on annexins see [1,2]). Type II sites are located in the protein core domains which are structurally conserved within the annexin family and are built of four or eight homologous segments known as annexin repeats.…”

Section: Introductionmentioning

confidence: 99%

“…While this classi¢cation is based on sequences of the annexin core region similar sequence features are also found in the N-terminal domains of annexins A2 and A9. Typically, the N-terminal domains of di¡erent annexins are highly divergent and are believed to confer speci¢city to individual members of the family (for review see [2]). Although showing limited sequence identity, the N-terminal regions of annexins A2 and A9 share the potential of forming an amphipathic K-helix.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca²⁺ and lipid binding proteins

et al. 2003

View full text Add to dashboard Cite

Annexin A9 is a novel member of the annexin family of Ca 2+ and phospholipid binding proteins which has so far only been identi¢ed in EST data bases and whose deduced protein sequence shows mutations in residues considered crucial for Ca 2+ coordination in other annexins. To elucidate whether the annexin A9 protein is expressed as such and to characterize its biochemical properties we probed cell extracts with speci¢c antiannexin A9 antibodies and developed a recombinant expression system. We show that the protein is found in HepG2 hepatoma cell lysates and that a green £uorescent protein-tagged form is abundantly expressed in the cytosol of HeLa cells. Recombinant expression in bacteria yields a soluble protein that can be enriched by conventional chromatographic procedures. The protein is capable of binding phosphatidylserine containing liposomes albeit only at Ca 2+ concentrations exceeding 2 mM. Moreover and in contrast to other annexins this binding appears to be irreversible as the liposome-bound annexin A9 cannot be released by Ca 2+ chelation. These results indicate that annexin A9 is a unique member of the annexin family whose intracellular activity is not subject to Ca2+ regulation.

show abstract

Section: Expression Of the Annexin A9 Protein In Cultured Cellsmentioning

confidence: 98%

Section: Biochemical Characteristics Of Recombinantly Expressedmentioning

confidence: 99%

Section: Biochemical Characteristics Of Recombinantly Expressedmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca²⁺ and lipid binding proteins

et al. 2003

View full text Add to dashboard Cite

show abstract

Proteomic analysis of mouse mammary terminal end buds identifies axonal growth cone proteins

Morris

Davies

Griffiths³

et al. 2004

Proteomics

View full text Add to dashboard Cite

Ductal morphogenesis in the mouse mammary gland occurs mainly postnatally and is driven by specialized structures at the ends of the developing ducts, the terminal end buds (TEBs), which later regress once ductal growth is complete. To identify proteins that are specifically associated with migration of TEBs we developed a novel method of isolating TEBs, which eliminated the mammary stroma. The protein expression profile of the TEBs was then compared with that of isolates taken from the 4th inguinal mammary gland of adult virgin mice using two-dimensional (2-D) gel electrophoresis and mass spectrometry (MS) analysis (matrix-assisted laser desorption/ionization and quadrupole time of flight). Following construction of an integrated protein expression database, 44 protein features which showed differential expression levels between the two sets were chosen for MS analysis. Of these, 24 gave protein annotations whereas the other 20 produced unidentified peptides. Fourteen unequivocal proteins were identified from these 24, whereas the remaining 10 matched more than one protein within a single 2-D gel feature. Several of the identified proteins were associated with the cytoskeleton and have previously been reported in axonal growth cones, suggesting that they may influence cell shape and motility within the advancing TEBs, in a similar fashion to migrating axons.

show abstract

Expanding the protein catalogue in the proteome reference map of human breast cancer cells

Pucci‐Minafra

Cancemi²,

Fontana³

et al. 2006

Proteomics

View full text Add to dashboard Cite

In this report we present a catalogue of 162 proteins (including isoforms and variants) identified in a prototype of proteomic map of breast cancer cells. This work represents the prosecution of previous studies describing the protein complement of breast cancer cells of the line 8701-BC, which has been well characterized for several parameters, providing to be a useful model for the study of breast cancer-associated candidate biomarkers. In particular, 110 spots were identified ex novo by PMF, or validated following previous gel matching identification method; 30 were identified by N-terminal microsequencing and the remaining by gel matching with maps available from our former work. As a consequence of the expanded number of proteins, we have updated our previous classification extending the number of protein groups from 4 to 13. In order to facilitate comparative proteome studies of different kinds of breast cancers, in this report we provide the whole complement of proteins so far identified and grouped into the new classification. A consistent number of them were not described before in other proteomic maps of breast cancer cells or tissues, and therefore they represent a valuable contribution for breast cancer protein databases and for future application in basic and clinical researches.

show abstract

V

Cited by 12 publications

References 0 publications

Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca²⁺ and lipid binding proteins

Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca²⁺ and lipid binding proteins

Proteomic analysis of mouse mammary terminal end buds identifies axonal growth cone proteins

Expanding the protein catalogue in the proteome reference map of human breast cancer cells

Contact Info

Product

Resources

About

V

Cited by 12 publications

References 0 publications

Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca2+ and lipid binding proteins

Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca2+ and lipid binding proteins

Proteomic analysis of mouse mammary terminal end buds identifies axonal growth cone proteins

Expanding the protein catalogue in the proteome reference map of human breast cancer cells

Contact Info

Product

Resources

About

Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca²⁺ and lipid binding proteins

Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca²⁺ and lipid binding proteins