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Ehlers-Danlos syndrome type VII: a single base change that causes exon skipping in the type I collagen alpha 2(I) chain.

We have examined the procollagens and collagens produced by skin fibroblasts from a patient with Ehlers-Danlos syndrome type VII. The patient was heterozygous for an abnormal alpha 2(I) chain migrating with the approximate size of pN alpha 2(I) chains after pepsin digestion. Peptide mapping suggested that the abnormality was located at the amino-terminus of the alpha 2(I) chain. Quantitative analysis of the alpha 2(I) mRNA indicated loss of the exon 6 sequences, and subsequent polymerase chain reaction amplification of cDNA demonstrated a deletion of the 54 bp of exon 6 from some of the alpha 2(I) mRNA. Analysis of genomic DNA from the patient revealed a single base change in one COL1A2 allele, substituting an A for a G as the first base of intron 6. This change mutates the obligate GT-dinulceotide splicing signal to AT and leads to exon skipping with splicing from exon 5 to exon 7. Loss of exon 6 sequences results in the loss of the procollagen-N-propeptidase cleavage site and a lysine residue that normally participates in covalent intermolecular crosslinking within collagen fibres.

Adult↗

Proteomic and immunochemical characterization of a role for stathmin in adult neurogenesis.

Stathmin is a developmentally regulated cytosolic protein expressed at high levels in the brain. Two-dimensional differential in-gel electrophoresis and mass spectroscopy of proteins expressed in immature and mature cultures from embryonic rat cerebral cortex identified stathmin among several differentially expressed proteins, consistent with a possible role in neurogenesis. Stathmin immunohistochemistry in adult rodent brain revealed prominent expression in neuroproliferative zones and neuronal migration pathways, a pattern that resembles the expression of doublecortin, which is implicated in neuronal migration. Stathmin immunoreactivity was also associated with neurons undergoing ectopic chain migration into the ischemic striatum and cerebral cortex following focal cerebral ischemia. Reducing the expression of stathmin or doublecortin with an antisense oligonucleotide inhibited the migration of new neurons from the subventricular zone to the olfactory bulb via the rostral migratory stream. These results suggest a role for stathmin in the migration of newborn neurons in the adult brain.

Aging↗

Glycoprotein III (clusterin, sulfated glycoprotein 2) in endocrine, nervous, and other tissues: immunochemical characterization, subcellular localization, and regulation of biosynthesis.

Specific antisera were raised against the A and B chains of glycoprotein III. Immunoblotting revealed that in adrenal medulla both chains migrate very closely together in two-dimensional electrophoresis. Both chains with slightly differing molecular sizes are found in several endocrine tissues and in brain, kidney, liver, and serum. The mRNA has an analogous widespread distribution. In primary cultures of chromaffin cells the level of message becomes significantly increased by treatment with histamine or 12-O-tetradecanoylphorbol 13-acetate/forskolin. However, the increase is small when compared with that of secretogranin II. The subcellular localization of glycoprotein III in endocrine organs and in the posterior pituitary was investigated by subcellular fractionation and immunoelectron microscopy. Glycoprotein III was found to be confined to the large dense-core vesicles of these organs. For a discussion of the function of glycoprotein III, its localization in these organelles has to be taken into account.

Animals↗

A behavioral model of international labor and nonlabor migration: the case of Turkish movements to West Germany, 1960-1986.

"In this paper behavioral models of international labor and nonlabor migration are presented. The models are based on the concept of chain migration, where the immigrant stock, differentiated by the duration of stay, induces and directs future migration flows. Three roles of the immigrant stock in inducing the inflow of potential migrants are identified: provider of assimilation aid; transmitter of information; and source of family reunification. Operationalized versions of the models are empirically tested for Turkish labor and nonlabor migration to West Germany, 1960-86. The results support the importance of information for labor migrants, and reunification ties for nonlabor migrants."

Acculturation↗

Out-migration and ethnic communities.

"Comparative analysis of out-migration [in the United States]...reveals substantial ethnic differentials. Part of the variation results from group compositional differences in social class and other characteristics normally related to migration, particularly age, education and local birth. Equally important, however, are indicators of social and economic bonds." The data concern 3,345 adults who were first interviewed between 1967 and 1969 in Rhode Island and were reinterviewed in 1970, 1971, and 1979. "The results suggest that ethnic groups characterized by a dense network of social and economic ties do not sponsor out-migration, which has been the emphasis of many past studies of chain migration and migrant assimilation. Rather, they deter out-migration by providing alternative opportunities within the ethnic community."

Age Factors↗

Calorimetric evidence for phase transitions in spin-label lipid bilayers.

Dispersions of pure, spin-label phosphatidylcholines in aqueous buffer have been investigated with the Privalov high-sensitivity differential scanning calorimeter. The lipids studied are mixed-chain ones in which C-2 of glycerol bears a spin-label derivative of stearic acid and the fatty acid group at C-1 is palmitate. A well-defined phase transition is observed at 30.3-30.7 degrees C for the phosphatidylcholine labeled near the polar end of the stearate chain (label at C-5). A sharp transition (32-34 degrees C) is also observed for the lipid spin-labeled near the terminal methyl of stearate (label at C-16), but the thermodynamic parameters for this lipid depend strongly on the history of the sample. Calorimetric evidence for hysteresis in the phase transition of the C-16-labeled lipid is presented. In contrast to the above spin-label lipids, the lipid labeled at C-12 does not show a sharp transition in the region 5-35 degrees C. In general, therefore, the thermal behavior of the spin-label phosphatidylcholines resembles that of phosphatidylcholines bearing double bonds or branched methyl groups at similar locations on acyl chains. During synthesis of mixed-chain lipids, migration of acyl chains occurs. Methyl esterification procedures which are compatible with the acid-labile spin-label group are described. Gas chromatographic analysis of methyl esters shows that chain migration during synthesis gives 15-20% of the spin-label fatty acid at the glycerol C-1 position.

Calorimetry, Differential Scanning↗

Plasma fibronectin is synthesized and secreted by hepatocytes.

Primary cultures of hepatocytes of rats and hamsters were established and examined for the synthesis and secretion of fibronectin. Hepatocytes of both species secreted fibronectin as a soluble dimeric protein which could be purified by its affinity for gelatin and using specific antisera. Plasma and cellular fibronectins could be clearly resolved on two-dimensional gels. In both species, the majority of the fibronectin secreted by hepatocytes was of the plasma type, as shown by analyses on one- and two-dimensional gels. The secretion of plasma fibronectin increased with time in culture, both in absolute terms and relative to the secretion of albumin. Even during the first day of culture, the secretion of fibronectin relative to that of albumin appeared to be sufficient to account for the relative levels of these two proteins in plasma. Hepatocytes of both species secreted preferentially the chain of plasma fibronectin with higher apparent molecular weight, although the faster migrating chain was also secreted. In addition, hamster hepatocytes cultured for 2 or more days appeared to secrete a cellular form of fibronectin. Possible origins for the different chain types of cellular and plasma fibronectins are discussed.

Animals↗

Non-white migration patterns in northern metropolitan areas, 1960-1970: the interaction between economic and affinitive factors.

"The principal objective of this article is to investigate the determinants of variation in the growth of non-white populations attributable to migration across northern [U.S.] metropolitan areas during the 1960s." The investigation is done by means of a single equation framework model, which is applied to U.S. Bureau of the Census data. The results indicate that "the migration-related growth of non-white populations in northern metropolitan areas during the 1960s was...importantly and directly associated both with the level of employment opportunities as measured by the proportion of the non-white population of labor force age officially employed in the mainstream economy of an SMSA and with the SMSA rate of net migration occurring over the preceding 10-year period, which indicates the role of chain migration."

Black or African American↗

Expression of glycolipid blood group antigens in single human kidneys: change in antigen expression of rejected ABO incompatible kidney grafts.

Total neutral glycolipid fractions were separated into molecular species on thin-layer chromatography plates and detected by immunostaining with monoclonal anti-blood group antibodies. Blood group A antigens based on type 1, 2, 3 and 4 carbohydrate core saccharides were present in kidneys of A1 and A1B individuals. Blood group A2 individuals expressed only small amounts of A antigen compared to A1 individuals especially of the type 3 and 4 compounds. Kidneys from non-secretor individuals contained less A antigen compared to secretor individuals, and in both groups a variation in the antigen expression between single individuals was noted. Blood group A type 2 and 3 (which is an extension of A type 2) antigens were present both as basic 6 and 9 sugar structures as well as extended saccharide chains migrating in the 8 to 11 sugar interval. In contrast, the type 1 chain based A and Lewis antigens were only present as their basic 5 to 7 sugar chains, and no elongated structures were found. Four cases of A2 kidneys initially transplanted into O recipients and removed after 5, 12, 21 days and 4 years, respectively, were also analyzed. Two of these kidneys, originating from the same donor, showed a difference in A antigen expression. The kidney functioning for four years (lost due to chronic rejection) completely lacked X antigen with five sugar residues (present in all other individuals) and contained a large amount of A antigens.(ABSTRACT TRUNCATED AT 250 WORDS)

ABO Blood-Group System↗

alpha-, beta- or gamma-chain-specific RNA interference of laminin assembly in Drosophila Kc167 cells.

Drosophila laminin alphabetagamma trimer assembly in Kc167 cells was perturbed by chain-specific RNA interference (RNAi). The intracellular pool of alpha and gamma chains remained unchanged under beta-chain RNAi by lipofection of double-stranded RNA encoding a beta-chain partial sequence. This was also the case for the intracellular pool of alpha and beta chains under gamma-chain-specific RNAi. Nonetheless, the intracellular pool of beta and gamma chains increased markedly under alpha-chain-specific RNAi. Non-reducing SDS/PAGE revealed that some of the increased beta and gamma chains migrated as disulphide-linked betagamma dimers but that the rest migrated as monomers. Since the monomeric beta and gamma bands detected under alpha-chain RNAi were denser than the beta band under gamma-chain RNAi and the gamma band under beta-chain RNAi, respectively, beta and gamma also appeared to accumulate by forming betagamma dimers without the disulphide linkage. We suggest that interconversion of these betagamma dimers is crucial for the replaceable and selective assembly of the alpha chain for alphabetagamma trimer formation.

Animals↗

Analysis of structural properties and cellular distribution of avian Ia antigen by using monoclonal antibody to monomorphic determinants.

In this report, we describe the analysis of Ia-like antigens in the chicken by using a monoclonal antibody (CIa-1) reactive with monomorphic determinants of the Ia-like (B-L) antigens. This antibody reacts with determinants on B cells in all avian species tested, but does not detect antigens on lymphocytes of representative mammals, reptiles, and amphibians. In addition to B cells, this antibody defines a subpopulation of the monocyte-macrophage series and reacts with mitogen-activated T cells. Immunochemical analysis indicates that the CIa-1 reactive antigen is a 65,000-dalton glycoprotein consisting of an alpha-chain of 32,000 daltons noncovalently bound to a beta-chain of 27,000 daltons. Under nonreducing conditions, the beta-chain migrates with slightly faster mobility. Two-dimensional gel analysis indicates that the beta-chain is the more heterogeneous of the two chains. Thus, the antigen detected by CIa-1 antibody is similar in cell distribution and structure to the murine Ia antigens and human DR antigens. During in ovo development, Ia+Ig- cells were not found in the yolk sac but were detected in the spleen, mesonephros, and bursa of 9-day embryos. Two populations of Ia+Ig- cells were identified in the bursa: 40 to 60% of the bursacytes, mostly larger cells, exhibited brighter immunofluorescence reactivity than the smaller bursacytes.

Animals↗

The "8-kD" cytoplasmic dynein light chain is required for nuclear migration and for dynein heavy chain localization in Aspergillus nidulans.

The heavy chain of cytoplasmic dynein is required for nuclear migration in Aspergillus nidulans and other fungi. Here we report on a new gene required for nuclear migration, nudG, which encodes a homologue of the "8-kD" cytoplasmic dynein light chain (CDLC). We demonstrate that the temperature sensitive nudG8 mutation inhibits nuclear migration and growth at restrictive temperature. This mutation also inhibits asexual and sexual sporulation, decreases the intracellular concentration of the nudG CDLC protein and causes the cytoplasmic dynein heavy chain to be absent from the mycelial tip, where it is normally located in wild-type mycelia. Coimmunoprecipitation experiments with antibodies against the cytoplasmic dynein heavy chain (CDHC) and the nudG CDLC demonstrated that some fraction of the cytoplasmic dynein light chain is in a protein complex with the CDHC. Sucrose gradient sedimentation analysis, however, showed that not all of the NUDG protein is complexed with the heavy chain. A double mutant carrying a cytoplasmic dynein heavy chain deletion plus a temperature-sensitive nudG mutation grew no more slowly at restrictive temperature than a strain with only the CDHC deletion. This result demonstrates that the effect of the nudG mutation on nuclear migration and growth is mediated through an interaction with the CDHC rather than with some other molecule (e.g., myosin-V) with which the 8-kD CDLC might theoretically interact.

Amino Acid Sequence↗

DNA electrophoresis in designed channels.

We present a simple description on the electrophoretic dynamics of polyelectrolytes going through designed channels with narrow constrictions of slit geometry. By analyzing rheological behaviours of the stuck chain, which is coupled to the effect of solvent flow, three critical electric fields (permeation field E((per)) approximately N(-1), deformation field E((def)) approximately N(-3/5) and injection field E((inj)) approximately N(0), with N polymerization index) are clarified. Between E((per)) and E((inj)), the chain migration is dictated by the driven activation process. In particular, at E > E((def)), the stuck chain at the slit entrance is strongly deformed, which enhances the rate of the permeation. From these observations, electrophoretic mobility at a given electric field is deduced, which shows non-monotonic dependence on N. For long enough chains, mobility increases with N, in good agreement with experiments. An abrupt change in the electrophoretic flow at a threshold electric field is formally regarded as a nonequilibrium phase transition.

Computer Simulation↗

Myosin in cultured human endothelial cells.

Myosin was isolated from cultured human endothelial cells by extraction with 0.6 M KCl and chromatography on Sepharose 4B. The extracted endothelial cell protein was identified as myosin by the characteristic ATPase profile, that is, the ATPase was activated by Ca2 + and EDTA and inhibited by Mg2 +. On sodium dodecyl sulphate polyacrylamide gel electrophoresis, the endothelial cell myosin heavy chain migrated with a molecular weight of 200 000 as did rabbit uterine and human platelet myosin heavy chains. A crude preparation of the endothelial cell myosin reacted immunologically with an antiserum to platelet myosin, a smooth muscle type of myosin. In indirect immunofluorescence studies, antiserum to the purified endothelial cell myosin stained cultured endothelial cells in a fibrillar pattern. The fibrillar pattern was more intense when the endothelial cells were stained with antiserum to platelet myosin. The presence of myosin in the endothelial cell provides a basis for the contractility of these cells. This contractile property may plan an important role in the physiologic function of these cells.

Adenosine Triphosphatases↗

Analysis of human serum proteins by molecular weight dependent acrylamide gel electrophoresis.

The technique of acrylamide gel electrophoresis of sodium dodecyl sulfate treated protein mixtures has been applied to the analysis of human serum proteins in the 70,000 to 250,000 molecular weight range. After staining, the bands are well defined, the molecular weight is defined and, hence, the identity of each can be estimated from the migration distance. In ambiguous cases, the identification of a band is confirmed by an independent method. The procedure is particularly valuable in the study of the gammopathies. The immunoglobulins migrate as expected, in contrast to the problems often encountered in the Ornstein-Davis gel method. Furthermore, light chains migrate more rapidly, are well separated from other serum proteins and, therefore, are readily detected. Paraproteins from three patients with documented gammopathies have been studied and characterized using this method.

Animals↗

'Stealth' corona-core nanoparticles surface modified by polyethylene glycol (PEG): influences of the corona (PEG chain length and surface density) and of the core composition on phagocytic uptake and plasma protein adsorption.

Nanoparticles possessing poly(ethylene glycol) (PEG) chains on their surface have been described as blood persistent drug delivery system with potential applications for intravenous drug administration. Considering the importance of protein interactions with injected colloidal dug carriers with regard to their in vivo fate, we analysed plasma protein adsorption onto biodegradable PEG-coated poly(lactic acid) (PLA), poly(lactic-co-glycolic acid) (PLGA) and poly(varepsilon-caprolactone) (PCL) nanoparticles employing two-dimensional gel electrophoresis (2-D PAGE). A series of corona/core nanoparticles of sizes 160-270 nm were prepared from diblock PEG-PLA, PEG-PLGA and PEG-PCL and from PEG-PLA:PLA blends. The PEG Mw was varied from 2000-20000 g/mole and the particles were prepared using different PEG contents. It was thus possible to study the influence of the PEG corona thickness and density, as well as the influence of the nature of the core (PLA, PLGA or PCL), on the competitive plasma protein adsorption, zeta potential and particle uptake by polymorphonuclear (PMN) cells. 2-D PAGE studies showed that plasma protein adsorption on PEG-coated PLA nanospheres strongly depends on the PEG molecular weight (Mw) (i.e. PEG chain length at the particle surface) as well as on the PEG content in the particles (i.e. PEG chain density at the surface of the particles). Whatever the thickness or the density of the corona, the qualitative composition of the plasma protein adsorption patterns was very similar, showing that adsorption was governed by interaction with a PLA surface protected more or less by PEG chains. The main spots on the gels were albumin, fibrinogen, IgG, Ig light chains, and the apolipoproteins apoA-I and apoE. For particles made of PEG-PLA45K with different PEG Mw, a maximal reduction in protein adsorption was found for a PEG Mw of 5000 g/mole. For nanospheres differing in their PEG content from 0.5 to 20 wt %, a PEG content between 2 and 5 wt % was determined as a threshold value for optimal protein resistance. When increasing the PEG content in the nanoparticles above 5 wt % no further reduction in protein adsorption was achieved. Phagocytosis by PMN studied using chemiluminescence and zeta potential data agreed well with these findings: the same PEG surface density threshold was found to ensure simultaneously efficient steric stabilization and to avoid the uptake by PMN cells. Supposing all the PEG chains migrate to the surface, this would correspond to a distance of about 1.5 nm between two terminally attached PEG chains in the covering 'brush'. Particles from PEG5K-PLA45K, PEG5K-PLGA45K and PEG5K-PCL45K copolymers enabled to study the influence of the core on plasma protein adsorption, all other parameters (corona thickness and density) being kept constant. Adsorption patterns were in good qualitative agreement with each other. Only a few protein species were exclusively present just on one type of nanoparticle. However, the extent of proteins adsorbed differed in a large extent from one particle to another. In vivo studies could help elucidating the role of the type and amount of proteins adsorbed on the fate of the nanoparticles after intraveinous administration, as a function of the nature of their core. These results could be useful in the design of long circulating intravenously injectable biodegradable drug carriers endowed with protein resistant properties and low phagocytic uptake.

Journal Article↗

Expression in Escherichia coli of the human fibrinogen B beta chain and its cleavage by thrombin.

The human fibrinogen B beta chain was expressed in Escherichia coli to study the functions of fibrinogen associated with this subunit. Recombinant B beta chains were expressed at 100 ng/mL in an IPTG-dependent manner. A first cistron sequence, inserted into the expression vector 5' to the B beta chain cDNA, was required to express the protein. Recombinant B beta chains were expressed within five minutes after induction with IPTG and were soluble in physiologic buffers. The recombinant B beta chains migrated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) at a rate identical to B beta chains from fibrinogen treated with N-glycanase. Recombinant B beta chains were cleaved by thrombin, as demonstrated by the loss of cross-reactivity with a monoclonal antibody (MoAb) specific for the undigested B beta 1-42 fragment. The levels of expression of the B beta chain were much lower than those reported previously for the gamma chain of fibrinogen expressed in a similar vector in E coli. However, these levels are sufficient to allow further characterization of this fibrinogen subunit.

Base Sequence↗

Lower rhombic lip-derived cells undergo transmedian tangential migration followed by radial migration in the chick embryo brainstem.

Migration behaviour and fate of cells originated from the lower rhombic lip (LRL) was examined in the chick embryo hindbrain. LRL-derived cells tangentially migrate along the pial surface of the brainstem and form a transient subpial migratory stream. In the initial stages of migration, LRL-derived cells appose each other or axon-like processes, which is indicative of mode of homophilic chain migration and/or axophilic migration. Some LRL-derived cells relocate rostroventrally towards the pontine region, although the majority of them migrate circumferentially to the ventral medulla oblongata. Depending on the stage of generation, LRL-derived cells undergo transmedian migration; late-generated LRL-derived cells preferentially colonize the contralateral brainstem compared with early generated cells. Thus, latecomer neuron precursors may migrate past their predecessors in the migratory stream. When LRL-derived cells leave the subpial migratory stream, they change their migratory direction to a radial one and relocate inwardly, with a profile that resembles a tangential-to-radial change seen in cerebellar granule cell precursors. After they enter the parenchymal region of the brainstem, they exhibited morphological differentiation, and some differentiate into excitatory neurons. The present results suggest that LRL-derived cells migrate across boundaries such as midline or rhombomere, which may facilitate to build up cellular and functional architectures of the hindbrain.

Animals↗