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PubMed2003

Differential activity of the gelatinases (matrix metalloproteinases 2 and 9) in the fetal membranes and decidua, associated with labour.

Degradation of the extracellular matrix in fetal membranes has been implicated in the rupture of fetal membranes, the process of parturition and placental detachment from the decidua after parturition. In this study we assessed labour-associated changes in gelatinase activity in cultured human amnion, chorion and decidua, as well as in amniotic fluid. We found that in media conditioned by decidua, following the establishment of uterine contractions, matrix metalloproteinase-2 (MMP-2) activity is increased while the protein tissue inhibitors of matrix metalloproteinase-1 (TIMP-1) level is decreased. The formation of a 130 kDa gelatinase band was also significantly increased after contractions began. In media conditioned by chorion, the initiation of uterine contractions did not change MMP activity or TIMP-1 levels. However, an increase in MMP-9 activity and a decrease in TIMP-1 protein levels were observed following the establishment of uterine contractions in media conditioned by amnion. We suggest that this differential spatial regulation provides a form for modulatory hieratical activity of the MMPs in the onset of labour allowing rupture of the membranes while avoiding premature placental separation.

Decidua↗
PubMed1995

Cytokines regulate gelatinase A and B (matrix metalloproteinase 2 and 9) activity in cultured rat astrocytes.

Under a tightly regulated expression mechanism, matrix metalloproteinases degrade extracellular matrix proteins and are thought to play a role in injury repair and tumor metastasis in peripheral tissues. Little is known about the function of matrix metalloproteinases or agents that regulate their production in adult brain; however, it has been shown that the activity of a calcium-dependent metalloproteinase is elevated in Alzheimer's hippocampus. The goals of this study were to determine whether cultured rat astrocytes produce matrix metalloproteinases and to identify agents that regulate protease activity. Enriched astrocyte cultures were prepared from brains of 1-day-old rat pups, and experiments were performed 13 days later. Gelatinase activity in astrocyte conditioned medium was determined using zymography with gelatin copolymerized with acrylamide in the gel. Under basal conditions after a 24-h incubation, rat astrocytes produce gelatinases of 58 and 66 kDa. On stimulation of astrocytes with lipopolysaccharide, interleukin-1 alpha or -beta, or tumor necrosis factor-alpha for 24 h, a dose-dependent increase in the activity of the 58- and 66-kDa gelatinases and the induction of a 94-kDa gelatinase occurred. All three astrocyte-derived proteases showed maximal activity in the presence of millimolar levels of Ca2+, their activity was inhibited in the presence of 1,10-phenanthroline, and their proenzymes were cleaved and activated after incubation with p-aminophenylmercuric acetate. Using immunoblotting, immunopositive bands at the respective molecular sizes indicated that the 58-kDa gelatinase was gelatinase A (matrix metalloproteinase 2) and the 94-kDa activity was gelatinase B (matrix metalloproteinase 9).(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1996

Synthesis of membrane- and matrix-bound colony-stimulating factor-1 by cultured osteoblasts.

Colony-stimulating factor-1 (CSF-1) is synthesized as a secreted or membrane-bound molecule. We investigated whether osteoblastic cells produce these forms of CSF-1. Glutaraldehyde-fixed cell layers supported proliferation of the macrophage cell line BAC1.2F5, suggesting the presence of membrane- or/and matrix-associated CSF-1. Furthermore, CSF-1 activity could be either extracted from the matrix or released from the cell membrane. A neutralizing antiserum against CSF-1 inhibited these activities. After labeling the cellular proteins with [35S] met/cys or [35S] SO4(2-), CSF-1 was immunoprecipitated and analyzed by SDS-PAGE. Under nonreducing conditions, bands with MW more than 200, 200, 100, and 50 kd were detected. These bands shifted to lower MW under reducing conditions. Treatment with chondroitin lyase ABC decreased the MW of the 200 kd monomer, proving the proteoglycan structure. Much smaller quantities of CSF-1 were found in the matrix extract than in the conditioned medium. Transforming growth factor beta (TGF-beta) increased both the synthesis of CSF-1 and its accumulation in the matrix. CSF-1 released with trypsin from the membrane fraction yielded on SDS-PAGE a band with MW of 60 and 30 kd under nonreducing and reducing conditions, respectively. Transcripts encoding both the secreted and the membrane-associated forms of the cytokine were detected in osteoblasts by reverse transcription polymerase chain reaction. These data indicate that osteoblastic cells produce the secreted forms, either remaining in the culture supernatant, or being associated to the matrix, and the membrane associated form of CSF-1.

Animals↗
PubMed2003

Subepithelial myofibroblasts and tenascin expression in microscopic colitis.

AIMS: To assess differences in the pattern of subepithelial myofibroblasts and the expression of tenascin as a marker of extracellular matrix production in collagenous and lymphocytic colitis. METHODS AND RESULTS: Colorectal biopsies were studied from 122 patients with chronic diarrhoea and normal colonoscopy. The pathological diagnoses were collagenous colitis (n = 35), lymphocytic colitis (n = 37), mild non-specific chronic inflammation (n = 28) and normal mucosa (n = 18). Four cases showed features of collagenous colitis but with collagen bands <10 micro m thick. Normal mucosa from 14 patients without diarrhoea served as healthy control tissue. Immunohistochemical expression of alpha-smooth muscle actin (myofibroblast marker) and tenascin was evaluated in well-orientated sections. The expression of alpha-smooth muscle actin was significantly increased in collagenous colitis compared with all the other groups. Strong tenascin subepithelial expression was seen in all cases of collagenous colitis, including the four without full-blown features. The mean thickness of tenascin bands was greater than that obtained by conventional stains. CONCLUSIONS: There are clear differences, with respect to extracellular matrix remodelling, between collagenous and lymphocytic colitis. These results support the theory of matrix overproduction in the genesis of collagenous colitis.

Actins↗
PubMed1995

Oriented growth of octacalcium phosphate on and inside the collagenous matrix in vitro.

To investigate the factors which regulate the growth of apatite in a collagenous matrix, a calcification experiment was carried out in a model system, where Ca2+ and PO43- ions diffused into a slice of Achilles tendon from mutually opposite grew on the Ca-side of the collagenous matrix, while small plate-like OCP crystals (< 1 micron) grew inside the matrix. The major part of crystals grew with the c-axis parallel to the collagen fibers. Others grew with the c-axis parallel to the collagen bands or perpendicular to the fibrils. Crystals grew with orientation on collagen fibrils from the beginning. It was concluded that collagen fibrils and property of the collagenous matrix played a regulatory role in the deposition and growth of OCP in the collagenous matrix.

Achilles Tendon↗
PubMed2001

Infrared spectrum of the hyponitrite dianion, N(2)O(2)2-, isolated and insulated from stabilizing metal cations in solid argon.

Ultraviolet irradiation of a rigid 7 K argon matrix containing alkali or alkaline earth metal atoms and NO(2) isolated from each other by one or two layers of argon forms N(2)O(2)2-dianions insulated from two M(+) cations by argon atoms, and visible photolysis reverses this electron-transfer process likely involving the N(2)O(2)(-) anion intermediate. The isolated N(2)O(2)2- dianion is identified from isotopic substitution and isotopic mixtures, which show that the new 1028.5 cm(-1) metal independent absorption involves two equivalent NO subunits. DFT calculations predict a strong 1078.1 cm(-1) fundamental for the Li(NO)(2)Li molecule and isotopic frequency ratios in excellent agreement with the observed values, which provides a model for the matrix dianion system. The spectrum of solid Na(2)N(2)O(2) exhibits a 1030 cm(-1) infrared band, which strongly supports the present N(2)O(2)2- dianion assignment. The electrostatic stabilization of N(2)O(2)2-, which is probably unstable in the gas phase, is made possible by metal cations separated by one or two insulating layers of argon in the rigid 7 K matrix.

Journal Article↗
PubMed1986

The extracellular matrix in "sclerosing" follicular center cell lymphomas: an immunohistochemical and ultrastructural study.

"Sclerosis" is frequently seen in follicular center cell (FCC) lymphomas. The mechanism of its deposition, as well as its composition and significance, are unknown. Several clinical studies have suggested that the course of these lymphomas is more indolent than that of lymphomas of the same histologic type without sclerosis. Nine immunologically characterized cleaved FCC lymphomas with sclerosis and 14 reactive lymph nodes with follicular hyperplasia were investigated by special staining methods, electron microscopy, and immunohistochemical studies with antibodies to types I, III, IV, and V collagen, laminin, and fibronectin. The sclerotic tissue in FCC lymphomas stained uniformly with periodic acid-Schiff (PAS) and Masson's stain, with the patterns ranging from delicate filamentous strands to dense doubly refractile bands. Ultrastructurally, the bands of connective tissue were continuous with the adventitia of vessels and composed of varying amounts of banded collagen (types I and III) admixed with filamentous and flocculent material. In all cases the neoplastic lymphocytes were separated from the extra-cellular matrix by fibroblasts and myofibroblasts with long cell processes. Immunohistochemical studies demonstrated intense staining of sclerotic bands with antibodies to fibronectin and type I collagen and, usually, weaker marking with antibodies to types III and V collagen. No significant staining of sclerotic bands was found with antibodies to type IV collagen or with laminin. Weak pericellular staining for type V collagen was present in eight of nine lymphomas and half of the control lymph nodes. These studies suggest that the increased amounts of extracellular matrix in cleaved FCC lymphomas are produced primarily by fibroblasts and myofibroblasts and represent predominantly fibronectin and types I, III, and V collagen. The composition of the sclerotic areas of FCC lymphomas is similar immunohistochemically to that of the capsule and trabeculae of reactive lymph nodes, which are also intimately associated with fibroblasts and myofibroblasts.

Extracellular Matrix↗
PubMed2005

Effective chromophore potential, dissipative trajectories, and vibrational energy relaxation: Br2 in Ar matrix.

The intramolecular wave packet dynamics on the electronic B (3pi0) potential of Br2 in solid argon is induced and interrogated by femtosecond pump-probe spectroscopy. An effective potential of the chromophore in the solid is derived from the wave packet period for different excitation photon energies. Deep in the potential well, it is consistent with vibrational energies from wavelength-resolved spectra. It extends to higher energies, where the vibrational bands merge to a continuum, and even beyond the dissociation limit, thus quantifying the cage effect of the argon matrix. This advantage of pump-probe spectroscopy is related to a reduced contribution of homogeneous and inhomogeneous line broadenings. The vibrational energy relaxation rates are determined by a variation of the probe window spatial position via the probe quantum energy. A very large energy loss in the first excursion of the wave packet is observed near the dissociation limit. This strong interaction with the argon matrix is directly displayed in an experimental trajectory.

Journal Article↗
PubMed1998

Type VI microfilaments interact with a specific region of banded collagen fibrils in skin.

Immunolocalization studies demonstrate that Type VI collagen forms a flexible network that interweaves among collagen fibrils in the dermis of skin as well as in other loose connective tissues. Although binding of Type VI collagen with other matrix components has been suggested, no structural evidence supporting these studies has been reported. In this study, we demonstrate that Type VI microfilaments consistently crossbanded collagen fibrils near the "d" band, indicating that the interaction of Type VI collagen with banded fibrils is not passive. This "d" band is also the location of the binding domain of decorin to banded fibrils, suggesting that decorin mediates the interaction of Type VI microfilaments with banded fibers. Examination of the architecture of the Type VI network in a decorin nullizygous mouse demonstrates a continuance of this specific interaction, indicating that the association is not entirely dependent on the presence of decorin. At least one other component, whose identity is uncertain, persists near the "d" band, which may also serve to mediate the attachment of Type VI collagen to collagen fibrils.

Actin Cytoskeleton↗
PubMed1995

Thrombin induces the activation of progelatinase A in vascular endothelial cells. Physiologic regulation of angiogenesis.

Angiogenesis requires degradation of vascular basement membrane prior to migration and proliferation of endothelial cells; proteinases are essential ingredients in this process. Because of thrombin's multiple effects on endothelium, we have examined its role in matrix metalloproteinase activation using human umbilical vein endothelial cells. Gelatin zymography of endothelial conditioned media revealed a prominent 72-kDa progelatinase A band. Addition of alpha-thrombin to endothelial cells resulted in the generation of 64 and 62 kDa gelatinolytic bands which is consistent with the activation of progelatinase A; thrombin had no effect in the absence of cells. This effect requires the proteolytic site of thrombin since progelatinase A activation was abolished by specific inhibitors of thrombin. Matrix metaloproteinase inhibitors diminished thrombin-induced activation of progelatinase A. Pretreatment of endothelial cells with excess tissue inhibitor of metalloproteinase-2 or a COOH-terminal fragment of progelatinase A abrogated thrombin-mediated activation of progelatinase A presumably by competing with the COOH terminus of native progelatinase A for interaction with an activator site on endothelial plasma membranes. Although membrane-type matrix metalloproteinase was demonstrated in endothelial cells by Northern and Western blotting, the receptor function of this molecule in thrombin-induced activation of progelatinase A needs to be clarified. Progelatinase A activation did not require intracellular signal transduction events mediated by the thrombin receptor. These data demonstrate that 1) endothelial cells express a novel activation mechanism for progelatinase A, 2) proteolytically active thrombin regulates this activation mechanism, and 3) activation occurs independently of the functional thrombin receptor.

Amino Acid Chloromethyl Ketones↗
PubMed1999

Ezrin regulates cell-cell and cell-matrix adhesion, a possible role with E-cadherin/beta-catenin.

Ezrin, radixin, moesin and merlin form a subfamily of conserved proteins in the band 4.1 superfamily. The function of these proteins is to link the plasma membrane to the actin cytoskeleton. Merlin is defective or absent in schwannomas and meningiomas and has been suggested to function as a tumour suppressor. In this study, we have examined the role of ezrin as a potential regulator of the adhesive and invasive behaviour of tumour cells. We have shown that following inhibition of ezrin expression in colo-rectal cancer cells using antisense oligonucleotides, these cells displayed a reduced cell-cell adhesiveness together with a gain in their motile and invasive behaviour. These cells also displayed increased spreading over matrix-coated surfaces. Immunofluorescence studies revealed that antisense-treated cells also displayed an increased staining of paxillin in areas representing focal adhesions. Furthermore, coprecipitation studies revealed an association of ezrin with E-cadherin and beta-catenin. Induction of the phosphorylation of ezrin by orthovanadate and hepatocyte growth factor/scatter factor resulted in changes similar to those seen with antisense treatment, together with a marked decrease in the association of ezrin with both beta-catenin and E-cadherin. It is concluded that ezrin regulates cell-cell and cell-matrix adhesion, by interacting with cell adhesion molecules E-cadherin and beta-catenin, and may thus play an important role in the control of adhesion and invasiveness of cancer cells.

Base Sequence↗
PubMed1999

The fibrinogen gamma chain dodecapeptide inhibits agonist-induced aggregation of rabbit platelets and fibrinogen binding to rabbit glycoprotein IIb-IIIa.

The HHLGGAKQAGDV (H12) sequence at the carboxyl termini of the y chains and the RGD sequences in the Aalpha chains of human fibrinogen are potential recognition sites for the binding of soluble fibrinogen to glycoprotein IIb-IIIa (GPIIb-IIIa) on activated human platelets. Thus, addition of either H12 or RGD-containing peptides inhibits aggregation of and fibrinogen binding to human platelets. In contrast, we reported previously that RGDS had relatively little inhibitory effect on these functions of rabbit platelets. In the present study, we found that H12 inhibited ADP- and thrombin-induced aggregation of rabbit platelets in a dose-dependent manner. Specificity was demonstrated by the failure of the variant HHLGGAKQAGEV peptide to inhibit ADP-induced aggregation. Furthermore, flow cytometric analyses demonstrated that H12 inhibited the binding of FITC-fibrinogen to ADP-activated rabbit platelets in a dose-dependent manner. To examine the direct interaction of H12 with rabbit GPIIb-IIIa, we performed affinity chromatography by applying an octylglucoside extract of rabbit platelet proteins onto an affinity matrix containing the fibrinogen gamma chain sequence. Proteins of approximately 135 kDa and approximately 95 kDa were specifically eluted by soluble H12, and the 95 kDa protein band was immunoblotted by anti-LIBS1, a monoclonal antibody against human GPIIIa. In control samples, no detectable protein from rabbit platelet lysates was eluted from an RGD affinity matrix by GRGDSP. Collectively, our results demonstrated that H12 inhibits aggregation of and fibrinogen binding to rabbit platelets by directly interacting with rabbit GPIIb-IIIa. These findings suggest that rabbit platelets would serve as a suitable thrombosis model for testing the efficacy of peptide mimetics derived from H12.

Animals↗
PubMed2005

Analysis of electrophoretic patterns of arbitrarily primed PCR profiling.

We present a mathematical algorithm for the analysis of electrophoretic patterns resulting from arbitrarily primed PCR profiling. The algorithm is based on the established mathematical procedures applied to the analysis of digital images of gel patterns. The algorithm includes (a) transformation of the image into a matrix form, (b) identification of every electrophoretic lane as a set of matrix columns that are further mathematically processed, (c) averaging of matrix columns corresponding to electrophoretic lanes that define lane representatives, (d) elimination of "smiling" bands, (e) solving the problem of a lane offset, and (f) removal of the background. Representation of individual electrophoretic lanes in the form of functions allows interlane comparisons and further mathematical analysis. Direct comparison of selected lanes was obtained by employing correlation analysis. Gel images were those obtained after arbitrarily primed PCR analysis of DNA that underwent damage induced by gamma radiation from a (60)Co source. The applied method proved to be useful for elimination of subjectivity of visual inspection. It offers the possibility to avoid overlooking important differences in case of suboptimal electrophoretic resolution. In addition, higher precision is achieved in the assessment of quantitative differences due to better insight into experimental artifacts. These simple mathematical methods offer an open-type algorithm, i.e., this algorithm enables easy implementation of different parameters that may be useful for other analytical needs.

Algorithms↗
PubMed2002

Identification of polysaccharide binding proteins by affinity electrophoresis in inhomogeneous polyacrylamide gels and subsequent SDS-PAGE/matrix-assisted laser desorption ionization-time of flight analysis.

A procedure that allows the identification of polysaccharide binding polypeptides is described. The method can be applied to proteins whose enzymatic activity is either unknown or cannot be identified unambiguously by activity-staining procedures and it has been used for very complex protein mixtures, such as crude extracts of plant organs. The procedure consists of three steps. First, an affinity polyacrylamide gel electrophoresis using an inhomogeneous polyacrylamide slab gel composed of two triangular parts, an upper gel lacking the ligand and a lower triangular gel containing an immobilized ligand, is performed. Proteins that interact with the ligand form bands that deviate from those of nonbinding proteins and can be detected by protein staining (or, if possible, by activity staining). Second, the bands containing the interacting proteins are excised, denatured, and subjected to SDS-PAGE using a slab gel. In the resulting protein pattern the target proteins cover most of the length of the gel piece applied to the SDS gel, whereas contaminating proteins appear as spots or narrow bands. Suitable regions of the target protein bands are selected for tryptic digestion. Third, the resulting peptides are analyzed by matrix-assisted laser desorption ionization-mass spectrometry followed by database research.

Electrophoresis, Polyacrylamide Gel↗
PubMed1995

Antigenic and functional conservation of an integrin I-domain in Saccharomyces cerevisiae.

We sought evidence for precursors of the leukocyte integrin subunits alpha M and alpha X among unicellular eukaryotes such as Saccharomyces cerevisiae. Chromatography of cytosolic extracts of Saccharomyces cerevisiae on an affinity matrix coupled to BU-15, a monoclonal antibody that recognizes alpha X, revealed a band of M(r) > 205 kDa under nonreducing conditions. Screening a lambda gt11 library of S. cerevisiae DNA with BU-15 (anti-alpha X) and anti-Mo1 (anti-alpha M) led to the isolation of a 3.7-kb EcoRI fragment containing the 3' end of an open reading frame sufficient to encode a polypeptide in excess of 118 kDa. On the basis of Southern blotting at high stringency, this gene was present in S. cerevisiae, but not in other yeast species such as Candida glabrata. Analysis of the derived amino acid sequence demonstrated > 98% identity with the S. cerevisiae protein Uso1p, a myosin-like polypeptide found exclusively in the cytosol. The C-terminal 1016 aa, expressed from the 3.7-kb EcoRI fragment in Escherichia coli as a beta-galactosidase fusion protein, bound iC3b, a ligand for the I-domain in alpha M and alpha X, and were recognized by Mn41, a monoclonal antibody specific for the alpha M I-domain. Antigenic and functional conservation of an I-domain in S. cerevisiae suggests that this domain may be a prototype for integrin-like proteins in other primitive eukaryotes.

Amino Acid Sequence↗
PubMed1993

Identification of annexin II, annexin VI and glyceraldehyde-3-phosphate dehydrogenase as calcyclin-binding proteins in bovine heart.

1. Matrix-immobilized calcyclin as affinity ligand in chromatography led to purification of three protein bands at 68, 36 and 35 kDa from bovine heart that required Ca2+ for binding. 2. Polyacrylamide-immobilized phosphatidylserine separated this fraction into a phospholipid-binding part (68 kDa, 35 kDa), also attaching to phospholipid vesicles even in the presence of calcyclin, and a flow-through part, constituting approx 30% of the total fraction (36 kDa). 3. Enzyme assays and electrophoretic mobility showed an at least close relationship of the 36 kDa band to glyceraldehyde-3-phosphate dehydrogenase. Interaction between enzyme and calcyclin in a solid-phase assay was inhibited by sialoglycoproteins and depended strongly on the integrity of carboxyl and hydrophobic groups of the enzyme. The interaction between the two proteins had a KD value of 110 nM. 4. Application of annexin-specific antibodies revealed an immunological relationship of the 35 and 68 kDa calcyclin-binding proteins to members of the annexin family, namely to annexin II (35 kDa) and annexin VI (68 kDa). The N-terminal amino acid sequence of a cleavage peptide of the 68 kDa protein was identical to a sequence stretch in human annexin VI, corroborating this evidence.

Amino Acid Sequence↗
PubMed1996

One-step immunoaffinity purification and partial characterization of hypophyseal growth hormone from the African catfish, Clarias gariepinus (Burchell).

Growth hormone (GH) was purified from African catfish (Clarias gariepinus) pituitary extracts in a single step by use of immunoaffinity chromatography. A monoclonal antibody to chicken GH, which labels the catfish hypophyseal somatotropes in immunocytochemistry, was coupled to CNBr-activated Sepharose, and crude alkaline pituitary extracts were run over the immunoadsorbent. Reversed-phase high-performance liquid chromatography analysis of the eluted material suggested heterogeneity, whereas silver staining upon SDS-polyacrylamide gel electrophoresis showed one single band with an estimated molecular weight between 22,000 and 23,000 Da. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis of the same preparation revealed the presence of several components with molecular weights ranging from 20,170 to 20,900 Da. The amino terminus of the protein was homogeneous, and the first 50 residues matched the proposed sequence of GH from two other siluran species (Ictalurus punctatus and Pangasius pangasius), except for one substitution at position 3. These data unequivocally confirm the identity of the purified molecule as suggested by immunochemical evidence. The bioactivity of the GH preparation was demonstrated by the short-term effect of GH on T3 plasma levels in juvenile catfish.

Amino Acid Sequence↗
PubMed2001

Molecular design, expression, and affinity immobilization of a trypsin-streptavidin fusion protein*(1).

A trypsin-streptavidin (TRYPSA) fusion protein was designed and its expression in Escherichia coli was evaluated. The streptavidin gene was PCR modified and cloned into the pET expression vector. The trypsin gene was subsequently inserted into this plasmid, thus generating a colinear fusion of trypsin and streptavidin genes (pTRYPSA). This engineering strategy was verified, and TRYPSA was expressed after IPTG induction using the E. coli strains, BL21(DE3) and BL21(DE3)pLysS. Standard protein fractions of the cell lysate were prepared and trypsin activity was primarily detected in the periplasmic and inclusion body fractions. Immunoblotting showed a single Western-positive band exhibiting a molecular weight of 39,000 Da. A biotinylated porous glass affinity matrix was prepared and selective adsorption resulted in a one-step purification and immobilization of TRYPSA from crude cell lysate. Trypsin activity was verified using a synthetic substrate. This enzyme bioreactor should serve as an excellent prototype for future studies that will examine the effect of limited proteolysis on functional characteristics of milk proteins, including gelling, emulsifying and foaming properties.

Journal Article↗