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PubMed2005

Thermal broadening of the J-band in disordered linear molecular aggregates: a theoretical study.

We theoretically study the temperature dependence of the J-band width in disordered linear molecular aggregates, caused by dephasing of the exciton states due to scattering on vibrations of the host matrix. In particular, we consider inelastic one- and two-phonon scatterings between different exciton states (energy-relaxation-induced dephasing), as well as the elastic two-phonon scattering of the excitons (pure dephasing). The exciton states follow from numerical diagonalization of a Frenkel exciton Hamiltonian with diagonal disorder; the scattering rates between them are obtained using the Fermi golden rule. A Debye-type model for the one- and two-phonon spectral densities is used in the calculations. We find that, owing to the disorder, the dephasing rates of the individual exciton states are distributed over a wide range of values. We also demonstrate that the dominant channel of two-phonon scattering is not the elastic one, as is often tacitly assumed, but rather comes from a similar two-phonon inelastic scattering process. In order to study the temperature dependence of the J-band width, we simulate the absorption spectrum, accounting for the dephasing-induced broadening of the exciton states. We find a power-law (T(p)) temperature scaling of the effective homogeneous width, with an exponent p that depends on the shape of the spectral density of the host vibrations. In particular, for a Debye model of vibrations, we find p approximately 4, which is in good agreement with the experimental data on J aggregates of pseudoisocyanine [I. Renge and U. P. Wild, J. Phys. Chem. A, 101, 7977 (1997)].

Journal Article↗
PubMed1990

Probing the sulfhydryl groups of nuclear matrix proteins with 6-iodoacetamidofluorescein.

Rat liver nuclear matrices were reacted with the fluorescent dye 6-iodoacetamidofluorescein and the matrix proteins were then separated by one and two-dimensional polyacrylamide gel electrophoresis. Upon transillumination with U.V. light it was possible to see that several proteins had reacted with the dy, thus indicating the presence of free -SH groups. This labelling technique allowed the detection of a large number of proteins, being several folds more sensitive than conventional Coomassie Blue staining, as demonstrated by two-dimensional electrophoretical separation. If nuclear matrices were treated with reducing agents before being reacted with 6-iodoacetamidofluorescein, the fluorescence increased with about the same intensity in all the protein bands. It is proposed that 6-iodoacetamidofluorescein can be used as a specific and very sensitive probe to study the -SH groups of nuclear matrix proteins.

Animals↗
PubMed2002

Comparison, characterization, and identification of proteases and protease inhibitors in epididymal fluids of domestic mammals. Matrix metalloproteinases are major fluid gelatinases.

The testicular and epididymal fluids of ram, boar, and stallion were analyzed by means of one-dimensional and two-dimensional gelatin gel zymography. Five main gelatinolytic bands were revealed in the ram and at least seven were observed in the boar and stallion. These proteolytic bands showed regionalized distribution throughout the organs. The two main proteolytic activities at around 54-66 kDa retrieved in all three species were inhibited by EDTA and phenanthroline, indicating that they were metallo-dependent enzymes. The activity of some of the low-molecular-weight gelatinases was also decreased by EDTA, whereas others were inhibited by serine protease inhibitors. One of the main proteases at 60-62 kDa from the caput fluid of the stallion and the ram was N-terminal sequenced; in both cases, high sequence homology was found with the N-terminal of the matrix-metalloproteinase-2 pro-form (pro-MMP-2). Antibodies against MMP-2, MMP-3, and MMP-9 gelatinases confirmed the regional distribution in the fluids of pre -, pro-, active, or degraded forms of these metalloproteases in all three species. We also observed the presence of acrosin in epididymal fluids, which was probably released by dead spermatozoa, but this enzyme did not explain all the serine protease activity. Moreover, the majority of this enzyme is bound to the protease inhibitor alpha(2)-macroglobulin, which is present in the fluids of all three species. TIMP-2, a potent inhibitor of MMPs, was present in the fluid of the caput regions in the ram and boar, and in the caput and caudal fluids of the stallion. This study demonstrated that similar types of proteases and inhibitors are regionally distributed in the epididymal fluids of three domestic species, suggesting an identical role in the sperm maturation process, the plasticity of this organ, or both.

Acrosin↗
PubMed1995

Extracellular matrix induces hormone responsiveness and differentiation in RUCA-I rat endometrial adenocarcinoma cells.

We recently described the establishment and the characterization of two rat endometrial adenocarcinoma cell lines which we called RUCA-I and RUCA-II. Despite fairly high estrogen receptor levels neither cell line responded to estradiol in conventional cell culture conditions on plastic and in the presence of serum. A limited hormonal response to the antiestrogen tamoxifen was detectable in RUCA-I but not in RUCA-II cells. To advance our cell culture conditions we plated RUCA-I cells on a layer of reconstituted basement membrane (Harbor Matrix) in the presence of a serum-free defined medium. These cell culture conditions induced hormone responsiveness of RUCA-I cells and permitted a stimulation of proliferation by estradiol. Further, two estradiol-induced secretory proteins with an apparent molecular weight of 115 kD and 60 kD could be identified by SDS-gelelectrophoresis if analyzed under reducing conditions. These proteins migrated as a single band in a non-reducing electrophoresis gel and were identified as components of the complement C3 system. Additionally, our results suggest that the effects of extracellular matrix and hormones on the expression of these proteins are additive. We conclude that processes of functional differentiation are most likely to occur in this in vitro model, particularly since the expression of components of the complement C3 system was under estrogenic control. Complement C3 proteins represent major estradiol-inducible secretory protein of the immature rat uterus in vivo. Culturing RUCA-I cells on top of a layer of reconstituted basement membrane provides a novel tool to study the importance of the extracellular environment on the hormone-induced gene expression in endometrial carcinogenesis in vitro.

Adenocarcinoma↗
PubMed2002

Use of SAMPL for a study of DNA polymorphism, genetic diversity and possible gene tagging in bread wheat.

Selective Amplification of Microsatellite Polymorphic Loci (SAMPL) technology was used in bread wheat for the first time for a study of genetic diversity, genotype identification and gene tagging. The diversity studies involved 55 wheat genotypes and two SAMPL primer pairs (SAMPL-6 and SAMPL-7, each with a M-CAG primer), which together gave 43 polymorphic bands out of a total of 87 SAMPL bands. The average polymorphic information content (PIC) of SAMPL primers was 0.221 and that of SAMPL markers was 0.264. The marker index of SAMPL markers was 9.61. The genetic similarity (GS) coefficients for 1,485 pairs of genotypes ranged from 0.35 to 0.96 with an average of 0.65. A dendrogram was prepared on the basis of a similarity matrix using the UPGMA algorithm, which corresponded well with the results of principal component analysis (PCA). From a total of 55 genotypes, 54 could be distinguished using the SAMPL banding patterns of both primers. For gene tagging, 568 bands from a total of 1,185 SAMPL bands detected polymorphism between each of the three pairs of parents differing for grain protein content (GPC), pre-harvest sprouting tolerance (PHST) and grain weight (GW). An association of six bands with GPC, of seven bands with PHST and four bands with GW was observed using bulked segregant analysis (BSA).

Journal Article↗
PubMed1990

Nonlinear optical effects in oxygen-binding reactions of hemoglobin A0.

Optical spectra have been taken in the Soret band (440-400 nm) under different oxygen partial pressures for hemoglobin (Hb) A0 at pH 7.0, 15 degrees C, 2-3 mM heme, 30 mM inositol hexaphosphate, 0.1 Hepes and 0.1 M NaCl. Application of the matrix method of singular value decomposition (SVD) to the difference spectra for different oxygen pressures shows the presence of at least two distinct optical transitions. From this result one concludes that the optical response to oxygen binding is nonlinear in the Soret band. The degree of nonlinearity has been determined by fitting the data at different wavelengths to the four-step reaction Adair equation with the inclusion of optical parameters that describe the intermediate oxygenated species. It is found that the data are well-represented by two optical parameters at each wavelengths, one which represents the optical change for the addition of the first and second oxygen molecules and the other which corresponds to the change for the addition of the third and fourth oxygen molecules. The ratio of these optical parameters depends only moderately upon wavelength with an average value of 0.8 over the Soret band. Thus, there is an approx. 20% smaller optical response for the first two ligated species than that for the last two ligated species. The overall Adair equilibrium constants are evaluated as follows: beta 1 = 0.081 +/- 0.003 Torr-1, beta 2 = 2.53 x 10(-3) +/- 2.4 x 10(-4) Torr-2, beta 3 = 1.25 x 10(-5) +/- 1.0 x 10(-6) Torr-3, beta 4 = 1.77 x 10(-6) +/- 1.5 x 10(-7) Torr-4.

Heme↗
PubMed2000

Interaction of localized electronic states with the conduction band: band anticrossing in II-VI semiconductor ternaries

We report a strongly nonlinear pressure dependence of the band gaps and large downward shifts of the conduction band edges as functions of composition in ZnS xTe (1-x) and ZnSe (y)Te (1-y) alloys. The dependencies are explained by an interaction between localized A1 symmetry states of S or Se atoms and the extended states of the ZnTe matrix. These results, combined with previous studies of III-N-V materials define a new, broad class of semiconductor alloys in which the introduction of highly electronegative atoms leads to dramatic modifications of the conduction band structure. The modifications are well described by the recently introduced band anticrossing model.

Journal Article↗
PubMed2000

Matrix-isolated Al2OF6(2-) ion in molten and solid LiF/NaF/KF.

A Raman spectrum consistent with that expected from an Al2OF6(2-) ion was observed when Na2O was dissolved in a eutectic LiF/NaF/KF (FLINAK) melt at 500 degrees C, which contained a low concentration of either AlF3 or Na3AlF6. Furthermore, it was possible to trap the Al2OF6(2-) ion in the frozen solid and to measure its Raman and IR spectra at 25 degrees C. A number of bands have been detected; among those, the two most characteristic bands of the Al2OF6(2-) ion at 494 (polarized) and 265 cm-1 in the FLINAK melt at 500 degrees C, and those at 509 and 268 (Raman) and approximately 780 to approximately 900 (IR) cm-1 for the compound matrix isolated in solid FLINAK at 25 degrees C. In the absence of added oxide, the dissolved aluminum fluoride was in the form of the octahedral AlF6(3-) ion, which has characteristic Raman bands at 542 and 325 cm-1 in the FLINAK melt at 500 degrees C. Whereas alumina, Al2O3, was found to be essentially insoluble in FLINAK melts, it was possible to dissolve sufficient amounts of Na2O to convert most of the AlF6(3-) to the oxyfluoroaluminate, Al2OF6(2-). These solutions appeared to be metastable with respect to formation of insoluble alumina at higher temperatures. The present results can be compared to previous measurements on alumina dissolved in pure molten cryolite at much higher temperatures, where alumina solubility is low and broad bands due to oxide species are difficult to detect due to overlap with bands from AlF6(3-) and AlF4-.

Journal Article↗
PubMed1993

Fourier transform infrared spectroscopy and electrochemistry of the primary electron donor in Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers: vibrational modes of the pigments in situ and evidence for protein and water modes affected by P+ formation.

Protein electrochemistry in an ultra-thin-layer electrochemical cell suitable for UV/vis and IR spectroscopy has been used to characterize the vibrational modes of the primary electron donors of Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers in their neutral and cation radical states (P and P+, respectively). The P-->P+ redox transitions could be well separated from redox reactions of other cofactors according to their redox midpoint potential. The IR difference bands of the primary electron donor bacteriochlorophylls all titrate in unison and exhibit the correct midpoint potential. Comparison of the difference spectra with those of isolated bacteriochlorophylls a and b in organic solvents of different polarity and proton activity [Mäntele, W., Wollenweber, A. M., Nabedryk, E., & Breton, J. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 8468-8472] leads to similar conclusions on the binding and interaction of the pigments within the protein matrix as previously obtained from light-induced P+Q-/PQ difference spectra. Equilibration of the reaction centers in D2O leads to few but distinct shifts of bands and changes of band intensities at 1662, 1634, and 1526 cm-1 (Rhodobacter sphaeroides) and 1694, 1664, 1648, 1630, and 1532 cm-1 (Rhodopseudomonas viridis) as well as to smaller deviations at other wavenumbers. The H-->D-sensitive band at 1662 cm-1 is interpreted in terms of a histidine NH2+ bending mode. A second H/D-sensitive difference band around 1648 cm-1 in the Rhodopseudomonas viridis reaction center may be associated with the peptide C = O of one of the amino acids surrounding P [eventually of the histidine(s) ligating the Mg] which is affected by P+ formation.(ABSTRACT TRUNCATED AT 250 WORDS)

Cations↗
PubMed1982

The structure and function of dermal connective tissue in normal individuals and patients with inherited connective tissue disorders.

Normal, human dermis is a dense, interwoven collagen and elastic matrix organized into papillary and reticular regions. the papillary dermis is a narrow zone beneath the epidermis which includes an even narrower subepidermal connective tissue band beneath the basal lamina. The reticular dermis has superficial intermediate and deep reticular zones. Each region is distinguished by the organization of the fibrous connective tissue. In this review, the structure, composition and function of each region of the normal dermis is surveyed and alterations in the tissue that have been recognized ultrastructurally in skin from patients with inherited connective tissue diseases are discussed. A molecular defect in a connective tissue molecule can be expressed phenotypically at one or more levels of dermal organization and can modify the structure of other matrix components. In some cases, the entire interwoven pattern of the dermis is altered; in others, the dermis retains the interwoven pattern and alterations are expressed as defects in the association of fibrils into fibers and fiber bundles. Abnormalities in the size, packing and relationships of fiber bundles also can occur. These changes involve the collagen matrix primarily. Depletion or exaggeration of elastin, or of the amorphous ground substance can also influence the organization of collagen and of the overall dermal architecture. The alterations described are illustrated with scanning electron micrographs of skin from patients with inherited connective disorders and are discussed in terms of the mechanical abnormalities of the tissue.

Collagen↗
PubMed2002

Snake venom hyaluronidase: an evidence for isoforms and extracellular matrix degradation.

The present study attempts to establish the isoforms of hyaluronidase enzyme and their possible role in the spreading of toxins during envenomation. Screening of venoms of 15 snakes belonging to three different families revealed varied hyaluronidase activity in ELISA-like assay, but with relatively similar pH and temperature optima. The zymograms of individual venoms showed varied activity banding patterns and indicated the presence of at least two molecular forms of the enzyme. During envenomation, activity of hyaluronidase is considered crucial for the spreading of toxins and is presumed to distort the integrity of extracellular matrix through the degradation of hyaluronic acid in it. This property has been addressed through localization of hyaluronic acid in human skin and muscle tissue sections using the probe, biotinylated hyaluronic acid binding protein. Faint and discontinuous staining pattern of hyaluronidase treated tissue sections over intense staining of untreated tissue sections confirm the selective degradation of hyaluronic acid in extracellular matrix and thus provide an evidence for the spreading property of the enzyme.

Animals↗
PubMed1972

Chlamydomonas flagella. I. Isolation and electrophoretic analysis of microtubules, matrix, membranes, and mastigonemes.

Methods were developed for the isolation of Chlamydomonas flagella and for their fractionation into membrane, mastigoneme, "matrix," and axoneme components. Each component was studied by electron microscopy and acrylamide gel electrophoresis. Purified membranes retained their tripartite ultrastructure and were shown to contain one high molecular weight protein band on electrophoresis in sodium dodecyl sulfate (SDS)-urea gels. Isolated mastigonemes (hairlike structures which extend laterally from the flagellar membrane in situ) were of uniform size and were constructed of ellipsoidal subunits joined end to end. Electrophoretic analysis of mastigonemes indicated that they contained a single glycoprotein of approximately 170,000 daltons The matrix fraction contained a number of proteins (particularly those of the amorphous material surrounding the microtubules), which became solubilized during membrane removal. Isolated axonemes retained the intact "9 + 2" microtubular structure and could be subfractionated by treatment with heat or detergent. Increasing concentrations of detergent solubilized axonemal microtubules in the following order: one of the two central tubules; the remaining central tubule and the outer wall of the B tubule; the remaining portions of the B tubule; the outer wall of the A tubule; the remainder of the A tubule with the exception of a ribbon of three protofilaments. These three protofilaments appeared to be the "partition" between the lumen of the A and B tubule. Electrophoretic analysis of isolated outer doublets of 9 + 2 flagella of wild-type cells and of "9 + 0" flagella of paralyzed mutants indicated that the outer doublets and central tubules were composed of two microtubule proteins (tubulins 1 and 2) Tubulins 1 and 2 were shown to have apparent molecular weights of 56,000 and 53,000 respectively

Acrylamides↗
PubMed1990

Three-dimensional organization of extracellular matrix in elastic cartilage as viewed by quick freeze, deep etch electron microscopy.

Freeze-etch electron microscopy was used to reexamine the ultrastructure of extracellular matrix in elastic cartilage. This revealed that extremely delicate, approximately 4 nm diameter fibrils join end-to-end and sometimes side-to-side to form a tightly woven mesh that extends continuously from the cell membrane throughout the intercellular space. Within this meshwork were found large, irregularly contoured and densely packed elastin fibers as well as long, thin (20 nm) fibers with the appearance of type II collagen. By comparison, type I collagen fibers found in the skin surrounding the cartilage appeared much thicker (30 nm) and displayed the usual periodic banding pattern. Freeze-etching the latter fibers displayed a helicoidal arrangement of subfibrils within. In both cartilage and type I collagen-rich extracellular matrix, some of the approximately 4 nm filaments in the matrix could be seen to contact collagen fibers orthogonally, apparently connecting adjacent fibers at regular intervals. The organization of these fine filaments and others composing the matrix has several features that suggest a different organization for cartilage than currently thought. Specifically, the distance between branch or contact points of fibrils in the matrix is seldom more than 35 nm, substantially less than the length of one extended proteoglycan monomer. This suggests that other proteoglycans, or other unidentified components of the matrix, bind along the proteoglycan core protein at intermediate binding sites in order to form a finely partitioned structure.

Animals↗
PubMed2005

Dendrimers made of porphyrin cores and carbazole chromophores as peripheral units. Absorption spectra, luminescence properties, and oxidation behavior.

Luminescent and redox-active porphyrin-based dendrimers of first and second generation have been synthesized, and their absorption spectra, photophysical properties, and oxidation behavior have been investigated, together with those of the corresponding aldehyde carbazole precursors. All the dendrimers contain a porphyrin core and carbazole-based chromophores as branches. The structural formulas of the new species are represented in Figures 1 and 2, with the corresponding schematizations. The absorption spectra of the aldehyde carbazole precursors A1-A6 in dichloromethane exhibit intense transitions in the UV region, centered on the carbazole and benzaldehyde subunits. The lowest-energy absorption bands receive contribution from charge-transfer transitions. Compounds A1-A6 are luminescent at room temperature in fluid solution; such a luminescence is attributed to twisted intramolecular charge-transfer excited states. The luminescence at 77 K in a rigid matrix is blue-shifted with respect to room-temperature emission and is assigned to locally excited states. Absorption spectra of the porphyrin-cored dendrimers P1-P6 appear additive as they are constituted by visible bands due to porphyrin absorption and bands in the UV region due to transitions centered on the carbazole-based branches. Emission spectra of P1-P6 both at 77 K and at room temperature are typical of porphyrin species and independent of excitation wavelength, indicating that the light collected by the peripheral chromophores is quantitatively transferred to the core. All the compounds exhibit a rich oxidation behavior in 1,2-dichloroethane solution, with reversible processes centered on the different carbazole subunits. Interaction between the different carbazole centers depends on the size of the spacer interposed.

Carbazoles↗
PubMed1994

Electronic absorption spectroscopy of matrix-isolated polycyclic aromatic hydrocarbon cations. II. The phenanthrene cation (C14H10+) and its 1-methyl derivative.

The ultraviolet, visible, and near infrared absorption spectra of phenanthrene (C14H10), 1-methylphenanthrene [(CH3)C14H9], and their radical ions [C14H10+; (CH3)C14H9+], formed by vacuum-ultraviolet irradiation, were measured in neon matrices at 4.2 K. The associated vibronic band systems and their spectroscopic assignments are discussed. The oscillator strengths were calculated for the phenanthrene ion and found lower than the theoretical predictions. This study presents the first spectroscopic data for phenanthrene and its methyl derivative trapped in a neon matrix where the perturbation of the isolated species by its environment is minimum; a condition crucial to astrophysical applications.

Argon↗
PubMed1991

Assignment of the gene for human tenascin to the region q32-q34 of chromosome 9.

Tenascin (TN) is a hexameric extracellular matrix glycoprotein that is highly expressed in solid tumors but has a restricted distribution in normal adult tissues. Each TN subunit is composed of segments with high homology to the sequences of epidermal growth factor, fibronectin and fibrinogen. Furthermore, it has been suggested that TN could modulate epithelial-mesenchymal and neuronal-glial interactions. Here, using a cDNA probe to human TN, we have carried out Southern blot analysis of the genomic DNAs from a panel of human-hamster somatic cell hybrids carrying different complements of human chromosomes. The results demonstrate that the human TN gene is located on chromosome 9. Furthermore, in situ hybridization studies demonstrate that human TN is located at 9q32-q34.

Animals↗
PubMed1998

Phosphorylation and biosynthesis of high molecular weight proteins of tumor nuclear matrix.

Our previous studies showed a predominance of high molecular weight protein group in tumor nuclear matrices. Contrary to normal cells, proteins of this group are preferentially phosphorylated. Phosphoproteins of hepatoma nuclear matrix are selectively subjected to rapid proteolysis. By alkali treatment and a monoclonal antibody against phosphotyrosyl residue the presence of two high molecular weight bands of phosphotyrosyl-containing proteins was detected in nuclear matrices of tumor but not of normal liver cells. High molecular weight protein group of tumor nuclear matrices revealed also a rapid turnover and preferential incorporation of labeled amino acids selectively inhibited by chloramphenicol.

Animals↗
PubMed2001

Effects of the extracellular matrix on lumican expression in rat aortic smooth muscle cells in vitro.

Lumican is a small leucine-rich proteoglycan (SLRP), which contributes to cell migration, proliferation, tissue hydration, and collagen fibrillogenesis. Whether lumican is localized in rat aortic smooth muscle cells (SMCs) and what its relationships might be to other extracellular matrix components have not yet been elucidated. In this study, using reverse transcription-polymerase chain reaction (RT-PCR), competitive RT-PCR, and western blot, lumican messenger ribonucleic acid (mRNA) was expressed in cultured rat aortic SMCs. SMCs cultured in serum-free medium showed four bands at 68, 62, 50, and 37 kD. The 68 and 62 kD bands corresponded to proteoglycan, the 50 kD band to glycoprotein, and the 37 kD band to the core protein form of lumican. The relationships of lumican to fibronectin and laminin were also investigated. The lumican mRNA level in SMCs cultured on fibronectin was highest at day 1, but it increased at day 3 in SMCs cultured on laminin. On the fibronectin or laminin-coated plates, SMCs expressed only the 68 and 62 kD bands, corresponding to proteoglycan. Pretreatment with anti-beta1 integrin receptor antibody revealed a decrease in the proteoglycan forms of lumican protein and an additional two bands at 50 and 37 kD, indicating glycoprotein and the core protein of lumican. These results show that lumican was synthesized in cultured rat aortic SMCs as proteoglycan, glycoprotein, and core protein. The extracellular matrix (ECM) affected lumican protein production and restricted the lumican protein form to proteoglycan via the beta1 integrin receptor in SMCs.

Animals↗