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R Heim

Publications and source records attributed to R Heim.

At least 37 records · Page 2Linked to original sources
PubMed1993

[Patricide and the dialectics of enlightenment. The "fatherless society" as a model of psychoanalytic archaeology of modern times].

Proceeding from Alexander Mitscherlich's socio-psychological diagnosis of the fatherless society (1963), the author goes back from there to Freud's "Totem and Taboo" (1912/13) and its treatment of the myth of the origins of culture. Heim reflects on the recurrent failure of culture, its constant relapse into murder and barbarism and sees this in connection with the dialectic nature of enlightenment, the patently intrinsic ambiguity of all progress achieved by homo sapiens. On the one hand, patricide and the advent of a fatherless society promise emancipation from mythic forces; on the other, latent feelings of guilt ensure that those forces remain operative and periodically explode into murderous activity. The fatherless society could only lose the terrors of ambivalence if it were possible to bring to an end the symbolism of the murdered father in the secularized equivalents of the totem, and to resolve the culturally seminal Oedipus complex of the primeval age in the conciliatory figures of post-Oedipal super-ego and ego-ideal.

Cultural Characteristics↗
PubMed1992

Expression, purification, and properties of the plasma membrane Ca2+ pump and of its N-terminally truncated 105-kDa fragment.

Isoform 4b of the human plasma membrane Ca2+ pump was expressed in COS cells and in the baculovirus system (Sf9 cells). A 105-kDa pump fragment lacking the first two transmembrane domains and the so-called transduction domain was also expressed. The expression level was 2-4 times the background in COS cells and at least 7 times in the baculovirus system. Tests on membranes from both systems showed that the expressed pump was active. The expressed pump and the 105-kDa fragment were isolated from Sf9 cell membranes by calmodulin affinity chromatography. The pump had Ca(2+)-dependent ATPase activity with a calmodulin stimulation factor of 3, formed a La(3+)-stabilized phosphoenzyme, and had a KM (Ca2+) in the presence of calmodulin of about 1 microM. The 105-kDa fragment, assayed by the phosphoenzyme test on COS or Sf9 cell membranes or by ATPase measurements after isolation from Sf9 cells, proved inactive. Laser confocal microscopy on Sf9 cells showed that both the pump and the 105-kDa fragment were apparently associated with the plasma membrane. The expressed pump in COS and Sf9 cells and the endogenous pump in a number of other cell lines had a slower gel mobility (i.e. a higher apparent molecular mass) than the erythrocyte pump.

Amino Acid Sequence↗
PubMed1992

Study of calmodulin binding to the alternatively spliced C-terminal domain of the plasma membrane Ca2+ pump.

The C-terminal regions of the four human plasma membrane Ca2+ pump isoforms 1a-d generated from alternatively spliced RNA have been expressed in Escherichia coli, and the recombinant proteins have been purified to a very high degree. The C-termini of isoforms 1a, 1c, and 1d contain an insert encoded by an alternatively spliced exon which is homologous to the calmodulin binding domain of isoform 1b. In isoforms 1c and 1d (29 and 38 amino acid insertions, respectively), subdomain A of the original calmodulin binding site of isoform 1b is followed by the spliced-in domain, which is then followed by subdomain B of the original calmodulin binding site. The positive charges of histidine residues at positions 27, 28, and 38 of the alternatively spliced sequence are likely to be responsible for the observed pH-dependent calmodulin binding to the novel "duplicated" binding site. The affinity of calmodulin for the C-terminal domains of isoforms 1a, 1c, and 1d, which contain the histidine-rich inserts, is much higher at pH 5.9 than at pH 7.2. A synthetic peptide (I31) containing 31 amino acids of the alternatively spliced sequence (from residue 9 to 40) also binds calmodulin with strong pH dependency. Alternative splicing in the C-terminal domain is proposed to confer pH dependence to the regulation of the activity of Ca2+ pump isoforms.

Amino Acid Sequence↗
PubMed1992

Overexpression of the erythrocyte plasma membrane Ca2+ pump in COS-1 cells.

A full-length cDNA corresponding to the hPMCA4 plasma membrane Ca2+ pump was assembled and expressed in COS-1 cells. The original sequence of hPMCA4 gave a very low expression. The mutation of the initiation translation site of this sequence to the consensus A/G-X-X-AUG-G increased the production of the protein. The Ca2+ pump activity in transfected cells was 1.5-3.5-fold higher than in controls. The Ca(2+)-dependence and the calmodulin stimulation of hPMCA4 expressed in COS-1 cells were comparable with those of the erythrocyte Ca2+ pump. Immunohistochemistry experiments showed that most of the expressed protein remained in intracellular membranes. Possible explanations for this targeting of the pump are discussed.

Animals↗
PubMed1992

Microdiversity of human-plasma-membrane calcium-pump isoform 2 generated by alternative RNA splicing in the N-terminal coding region.

cDNA species covering the entire coding sequence of the human homologue of the rat plasma membrane Ca(2+)-ATPase (PMCA) isoform 2 have been isolated and characterized. The deduced amino acid sequence shows 99% identity with that of the rat protein and can be aligned with the latter without gaps except for one 14-amino-acid-residue insert in the region immediately preceding the putative phospholipid-sensitive domain in the human pump. cDNA clones isolated by anchored polymerase-chain reaction revealed additional microheterogeneity in the same N-terminal PMCA2-coding region. Alternative RNA splicing involving a region of 135 nucleotides generates three types of cDNA. One does not contain any of the 135 bp, and the other two contain 42 bp or the entire 135 bp of the optional sequence. Analysis of genomic DNA indicates that this sequence is encoded by three separate exons of 33, 60 and 42 bp. Although each of these exons could be inserted into the mRNA without changing the reading frame, polymerase-chain amplifications using cDNA libraries from several human tissues show that the 33-bp and the 60-bp exons are never independently used during splicing. The unequal distribution of the splice variants suggests tissue-specific regulation of the alternative-splicing pathways and indicates a functional specialization of the encoded isoform subtypes.

Amino Acid Sequence↗
PubMed1992

[Hatred of foreigners and purity--current aspects of an illusion. Social psychological and psychoanalytic considerations].

This study draws upon both Carlo Ginzburg's procedures for establishing and preserving (historical) evidence and Claude Lévi-Strauss' structuralist approach with its analysis of "primitive" mythologies to demonstrate that binary coding of the social domain is an all-pervasive structural principle. Heim's intention in this is to show that (present-day) xenophobia and racism are the products of a phantasm centering around the division of the world into pure and impure. The author brings into alignment collective fantasies about the homogeneity of the "body politic" with a form of primary narcissism which, if it is to preserve the illusion of original purity, is forced to externalize instinctual urges experienced as heterogeneous and unpleasurable and project them onto "foreigners" and things foreign.

Culture↗
PubMed1991

Cloning an Escherichia coli gene encoding a protein remarkably similar to mammalian aldehyde dehydrogenases.

The nucleotide (nt) sequence of 2.9 kb of Escherichia coli genomic DNA that encompasses a gene encoding a putative aldehyde dehydrogenase (ALDH) has been determined. The presence of an open reading frame beginning 2 nt downstream from the ALDH-coding sequence indicates that this gene may be part of a larger operon. An extended upstream nt sequence displays striking similarity to sequences found upstream or in intergenic regions of a number of other bacterial genes. Crude cell extracts from E. coli grown under several different conditions show weak but measurable ALDH enzyme activity that prefers NADP+ over NAD+ as coenzyme; however, aldH gene expression appears to be very low, since no specific transcripts derived from the novel gene can be detected on Northern blots of RNA isolated from these cells. The deduced E. coli protein contains 495 amino acid (aa) residues with a calculated Mr of 53418. Its aa sequence showed marked similarity to NAD(+)-dependent ALDHs of eukaryotes. About 40% aa sequence identity, and over 60% similarity, are detected between the E. coli protein and both the cytosolic (class-1) and the mitochondrial (class-2) forms of mammalian ALDHs. In contrast to the mammalian enzymes, which contain eight to eleven Cys residues, only four Cys are present in the E. coli protein, and of these only Cys302, corresponding to the disulfiram-sensitive residue in the mammalian enzymes, is found at a conserved position in both the prokaryotic and the eukaryotic ALDHs. The availability of a bacterial ALDH with a high degree of similarity to mammalian ALDHs promises to facilitate future structural studies on these enzymes.

Aldehyde Dehydrogenase↗
PubMed1990

Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane.

The sequence of more than 1,000 amino acid residues, derived from two different isoforms, has been determined from peptides generated from purified human erythrocyte membrane Ca2(+)-ATPase (hPMCA). Several of these peptide sequences correspond to the previously reported, cDNA deduced sequence of the "teratoma" Ca2+ pump isoform hPMCA1 (Verma, A. K., Filoteo, A. G., Stanford, D. R., Wieben, E. D., Penniston, J. T., Strehler, E. E., Fischer, R., Heim, R., Vogel, G., Matthews, S., Strehler-Page, M.-A., James, P., Vorherr, T., Krebs, J., and Carafoli, E. (1988) J. Biol. Chem. 263, 14152-14159). The complete primary structure of a novel isoform (hPMCA3) has been determined by molecular cloning and nucleotide sequencing of its corresponding cDNA. This new member of the plasma membrane Ca2+ pump family consists of 1,205 amino acid residues with a calculated Mr of 133,930, and it shows 88% similarity (75% identity) with the previously sequenced pump isoform. Specific probes detect major mRNA species of 5.6 kilobases for hPMCA1, and of 7.5 kilobases for hPMCA3, on Northern blots of human K562 erythroleukemic cell RNA. A large number of peptide sequences match perfectly with only one or the other of these isoforms and all peptides (with 6 exceptions corresponding to a contaminant protein or to a third minor Ca2+ pump isoform) are found in either only one or in both of the isoforms. The two erythrocyte Ca2+ pumps display high sequence divergence in a few localized regions that may determine isoform-specific functional specializations; for example, the putative extracellular loop separating transmembrane domains 1 and 2, the highly negatively charged region previously suggested to be involved in Ca2+ binding, and the site of cAMP-dependent protein kinase phosphorylation.

Amino Acid Sequence↗
PubMed1988

Complete primary structure of a human plasma membrane Ca2+ pump.

cDNAs coding for a plasma membrane Ca2+ pump were isolated from a human teratoma library and sequenced. The translated sequence contained 1,220 amino acids with a calculated molecular weight of 134,683. All regions of functional importance known from other ion-transporting ATPases could be identified. The translated sequence also contained, near the carboxyl terminus, the calmodulin-binding domain and two domains which are very rich in glutamic acid and aspartic acid. These two domains resemble calmodulin somewhat and one of them may play a role in the binding of Ca2+. The enzyme also contains domains rich in serine and threonine, one of which has a sequence matching those of good cAMP-dependent protein kinase substrates. The carboxyl-terminal region is important for regulation by calmodulin, proteolysis, and phosphorylation. Near the amino terminus are two domains which are very rich in lysine and glutamic acid, as well as two domains resembling EF hands, one of which also has some resemblance to calmodulin. Comparison of the cloned sequence with peptide sequences from the erythrocyte Ca2+ pump showed that the two proteins have a very high proportion of identical residues but are not 100% identical, indicating that they represent different isozymes.

Amino Acid Sequence↗
PubMed1975

[Proceedings: Diagnostic value of myocardial perfusion scintigraphy in coronary sclerosis].

UNLABELLED: Perfusion scintigrams with Technetium-labeled microspheres were performed in 60 patients undergoing selective coronary angiography. The scintigrams were analyzed semiquantitatively with the aid of a computer. In addition, angiograms were quantitated with regard to proximal obstructions as well as regional wall changes of the left ventricle (VCF). RESULTS: 1. A reduction of scintigraphic activity was already seen in narrowings of lesser degrees (50%); 2. scintigraphic activity followed the degree of obstruction rather than the contraction abnormality. Perfusion scintigrams are helpful in selecting patients for revascularization.

Coronary Disease↗