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A Kress

Publications and source records attributed to A Kress.

35 records · Page 2Linked to original sources
PubMed1988

Antibody-independent activation of the complement system by mitochondria is mediated by cardiolipin.

Non-immune activation of the first component of complement (C1) by the heart mitochondrial inner membrane has been investigated. Cardiolipin, the only strong activator of C1 among phospholipids, is present in large amounts in the heart mitochondrial inner membrane. We therefore studied its contribution to C1 activation by mitochondria. The proteins of the mitochondrial inner membrane were found to activate C1 only weakly, in contrast with the phospholipid fraction which induces strong C1 activation. Furthermore, the digestion of mitochondrial inner membranes with proteolytic enzymes did not affect C1 activation. Additional support in favour of cardiolipin being the responsible activator came from competition experiments with mitochondrial creatine kinase (mt-CPK) and adriamycin, known to bind to cardiolipin. Both mt-CPK and adriamycin displaced C1q from the mitochondrial inner membrane. In addition, C1q displaced mt-CPK bound to mitoplasts.

Animals↗
PubMed1987

Antibody-independent activation of C1. I. Differences in the mechanism of C1 activation by nonimmune activators and by immune complexes: C1r-independent activation of C1s by cardiolipin vesicles.

C1 activation is controlled by the regulatory protein C1-inhibitor (C1-INH). In contrast to immune-complex-induced activation, which is insensitive to C1-INH, antibody-independent activation of C1 is modulated by C1-INH. The mechanisms regulating nonimmune activation were studied with two phospholipids varying in their capacity to activate C1 in the presence of C1-INH: cardiolipin (CL) and phosphatidylglycerol (PG). Whereas C1-INH consistently suppressed activation by PG vesicles, a dose-dependent increase in C1 activation was measured with CL vesicles above 40 mole %. A similar dose-response binding of C1s requiring C1q, but not C1r, was detected only on CL vesicles, but neither on PG vesicles nor on immune complexes. This binding was Ca2+-dependent, suggesting that dimeric C1s is involved and was inhibited by spermine. The C1q-bound C1s was specifically cleaved at 37 degrees C into its active 58 kDa and 28 kDa chains, in the absence of C1r. On the addition of anti-CL antibodies, the C1q-mediated cleavage of C1s by CL vesicles was specifically inhibited. The cleavage of C1r on CL vesicles was also determined. When macromolecular C1 was offered in the presence of C1-INH, C1r cleavage was detected; however, the presence of C1s was a critical factor for C1r activation, because it was required on CL vesicles, but not on immune complexes. These results show that nonimmune activation of C1 presents specific features which distinguish it from immune complex-induced activation. These characteristics varied with the capacity of antibody-independent activators to activate C1 in the presence of C1-INH.

Antigen-Antibody Complex↗
PubMed1985

The male copulatory apparatus in an opisthobranch mollusc, Runcina.

The copulatory apparatus of a primitive opisthobranch, Runcina, is described. The apparatus is comprised of the following organs: the spermatic bulb, the prostrate, the penis and the penial sac. The spermatic bulb wall consists of cuboidal epithelium with forked microvilli and densely arranged cilia. Prior to copulation the interior is tightly packed with sperm. The prostate is lined with alternating glandular and supporting cells, the latter being compressed but with a mushroom-shaped apex bearing a few forked microvilli and many cilia. The glandular cells produce differing secretions, each cell producing a single type. Large paracrystalline structures enclosed in cells close to the penial area are particularly striking. Considerable amounts of the secretory products are accumulated in the protruding cell apices. One type of inclusion is found at a later stage, packed around the sperm mass within the spermatophore; its function, and the fate of the other secretions is not yet clear. The epithelium of the penis is of more columnar structure, covered with forked microvilli and extremely long cilia which are anchored by long rootlets in the cells. Some of the cells contain large electron-dense secretory granules, others hold accumulations of small secretory vesicles in their apices. It seems likely that these contribute towards the outer layer of spermatophore. The wall of the penial sac is lined by one to two rows of flat-cuboidal cells bearing sparse forked microvilli and cilia.

Animals↗
PubMed1985

Antibody-independent activation of C1, the first component of complement, by cardiolipin.

Lipid vesicles containing phospholipids known to be present in substantial amounts in mitochondrial membranes were tested for their capacity to activate C1. Among them, only cardiolipin (CL) was highly efficient in C1 activation; no such effect was observed with phosphatidylcholine, phosphatidylethanolamine, or phosphatidylinositol. CL was shown to bind specifically C1q, because only unlabeled C1q competed with 125I-C1q for binding to CL. The requirement for C1q was confirmed by the finding that only fully reconstituted macromolecular C1, containing C1q, was activated by CL. The specificity of CL-induced activation of C1 was also demonstrated by introducing adriamycin, an agent known to interact with CL. Whereas adriamycin did not decrease C1 activation induced by immune complexes, it abrogated C1 activation by CL. The latter was shown to be a strong nonimmune activator of C1, because C1-INH did not inhibit CL-induced activation. When the concentration of CL in vesicles was decreased in the presence of phosphatidylcholine, C1 activation was detected only above a critical level of 35 mol% CL, compatible with a minimal density or clustering of CL molecules in the plane of the membrane. Moreover, C1 activation by CL was modulated by the addition of cholesterol. The threshold of CL required for C1 activation was lowered by the incorporation of more than 35 mol% cholesterol into the vesicles. These results show that CL incorporated into liposomes can be a potent nonimmune activator of C1. The negatively charged phosphate groups in CL are likely candidates for Clq-binding.

Cardiolipins↗
PubMed1984

Ultrastructural studies on oogenesis in the shrew (Crocidura russula): I. The preantral follicle.

Ultrastructural analysis of the ovarian follicle prior to antrum formation in the shrew, Crocidura russula, shows gradual differentiation of mitochondria, endoplasmic reticulum, Golgi complexes, vesicles, and multivescular bodies correlated with the growth of the oocyte from primordial to tertiary follicle and the development of the follicular wall. The growth rate of the follicle in relation to that of the oocyte was found to be biphasic.

Animals↗
PubMed1984

Ultrastructural study on oogenesis in shrews (Neomys fodiens, Sorex araneus).

The ultrastructure of early follicular oocytes is described. Among the differentiating organelles marked development of endoplasmic reticulum, often in close contact with mitochondria, is especially conspicuous. In addition, the dilatation of mitochondria, the accumulation of dense granular material and the formation of multivesicular bodies are discussed.

Animals↗
PubMed1982

Ultrastructural indications for autosynthetic proteinaceous yolk formation in amphibian oocytes.

The formation of proteinaceous yolk is a main feature during amphibian oogenesis. The main bulk is built up by a process called heterosynthesis. The precursor complex vitellogenin is synthesized in the liver, transported by the bloodstream to the ovary, where the oocytes sequester the material by means of endocytosis. This pathway has been described in detail by many authors. The ultrastructural study of amphibian oocytes indicates on the other hand a small but distinct contribution of the oocyte itself towards yolk formation. This process has been called autosynthesis and starts before the onset of heterosynthetic activities. The cell organelles possibly involved in yolk-recursor and yolk-platelet formation are the nuclear envelope, annulate lamellae, endoplasmic reticulum, Golgi complex, GERL and mitochondria. The aim of this paper is to discuss the data, mainly of ultrastructural nature, so far accumulated during the study of autosynthesis. It is hoped to stimulate more biochemically orientated research in this field.

Amphibians↗
PubMedDate not supplied

Neutrophil priming by cytokines and vitamin D binding protein (Gc-globulin): impact on C5a-mediated chemotaxis, degranulation and respiratory burst.

At the site of acute inflammation, leukocytes are confronted with multiple mediators which are expected to modulate each other with respect to cell responses to the individual ligand. Previous contact of neutrophils with pro-inflammatory cytokines, such as TNF-alpha or GM-CSF, or with the vitamin D binding protein (Gc-globulin) leads to the alteration of either multiple or rather distinct C5a-mediated neutrophil functions. Gc-globulin, the transport protein for 25-(OH)-D3, serves selectively as a cochemotactic factor for C5a/Ca(des)Arg. In contrast, TNF-alpha and GM-CSF, previously shown to modulate FMLP-induced neutrophil responses, are able to reduce C5a-mediated neutrophil chemotaxis, but augment their degranulation and respiratory burst activity. Cytokine priming was shown to be accompanied by a down-regulation of C5a receptors (CD88) whereas vitamin D binding protein had no impact on the level of neutrophil C5a receptors. C5a itself diminishes chemotaxis as well as degranulation and oxidative burst in response to a second dose of the same ligand (homologous desensitization). A similar effect, termed heterologous desensitization, occurs, if cell responses to a given mediator (e.g. to C5a) are reduced or even abolished upon the activation of another receptor of the same G-protein coupled chemoattractant receptor subfamily (e.g. receptors for FMLP or IL-8). In concert with C5a, certain molecules may either augment chemotaxis or shift neutrophil effector functions from migration to exocytosis, an essential step within the sequence of events in a coordinated inflammatory response.

Cell Degranulation↗